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Conserved domains on  [gi|1751924788|ref|WP_150141331|]
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MULTISPECIES: citrate/2-methylcitrate synthase [unclassified Campylobacter]

Protein Classification

citrate synthase family protein( domain architecture ID 475)

citrate synthase family protein similar to citrate synthase that catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle

CATH:  1.10.580.10
EC:  2.3.-.-
Gene Ontology:  GO:0016746
PubMed:  3013232
SCOP:  3001050

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CS_ACL-C_CCL super family cl00416
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
11-372 0e+00

Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.


The actual alignment was detected with superfamily member cd06108:

Pssm-ID: 469765 [Multi-domain]  Cd Length: 363  Bit Score: 638.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:cd06108     1 GGLAGVVAGQTAISTVGKgGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDTHPMNLMQTAVSALGALESEkDDFSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAGYFLERLELKE 169
Cdd:cd06108    81 IPKDSHPMDVMRTGCSMLGCLEPE-NEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 170 PKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQ 249
Cdd:cd06108   160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 250 KLENKELLMGFGHRVYgLGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKrPSLPPNADFYSASAYHFMGIPT 326
Cdd:cd06108   240 KLERKELIMGFGHRVY-KEGDPRSDIIKKWSKKLseeGGDPLLYQISERIEEVMWEE-KKLFPNLDFYSASAYHFCGIPT 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:cd06108   318 ELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
 
Name Accession Description Interval E-value
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
11-372 0e+00

Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate though it has partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate and prefer PrCoA as substrate, but can also use AcCoA. Re 2-MCS1 can use butyryl-CoA and valeryl-CoA at a lower rate. A second Ralstonia eutropha 2MCS, Re 2-MCS2, which is induced on propionate is also found in this group. This group may include proteins which may function exclusively as a CS, those which may function exclusively as a 2MCS, or those with dual specificity which functions as both a CS and a 2MCS.


Pssm-ID: 99861 [Multi-domain]  Cd Length: 363  Bit Score: 638.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:cd06108     1 GGLAGVVAGQTAISTVGKgGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDTHPMNLMQTAVSALGALESEkDDFSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAGYFLERLELKE 169
Cdd:cd06108    81 IPKDSHPMDVMRTGCSMLGCLEPE-NEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 170 PKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQ 249
Cdd:cd06108   160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 250 KLENKELLMGFGHRVYgLGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKrPSLPPNADFYSASAYHFMGIPT 326
Cdd:cd06108   240 KLERKELIMGFGHRVY-KEGDPRSDIIKKWSKKLseeGGDPLLYQISERIEEVMWEE-KKLFPNLDFYSASAYHFCGIPT 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:cd06108   318 ELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
PRK12351 PRK12351
methylcitrate synthase; Provisional
4-375 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 561.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788   4 SEAKKKTG-GLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSE 81
Cdd:PRK12351    2 AAFKPKKSvALSGVVAGNTALCTVGKsGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  82 NLKAILRAIPKDTHPMNLMQTAVSALGALESEKDD--FSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAG 159
Cdd:PRK12351   82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEDhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 160 YFLERLELKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKN 239
Cdd:PRK12351  162 HFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDT 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 240 EEEAISGVNQKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRpSLPPNADFYSA 316
Cdd:PRK12351  242 PDEAEADIRRRVENKEVVIGFGHPVYTI-SDPRNKVIKEVAKKLskeAGDTKLYDIAERLETVMWEEK-KMFPNLDWFSA 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1751924788 317 SAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK12351  320 VSYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
12-375 0e+00

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 508.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:COG0372    16 GLEGVVAGETAISYIdGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFS--DQDDKIIRLLGVLPSVLCYWHHYvNSGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:COG0372    96 PRDAHPMDVLRTAVSALGAFDPDADDIDpeARLEKAIRLIAKLPTIAAYAYRY-RRGLPPVYPDPDLSYAENFLYMLFGE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:COG0372   175 EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMKEKRPS----LPPNADFYSASAYHF 321
Cdd:COG0372   255 KALDKKERIMGFGHRVYKN-YDPRAKILKEAAEELLeelGDDPLLEIAEELEEVALEDEYFiekkLYPNVDFYSGIVYHA 333
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1751924788 322 MGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:COG0372   334 LGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
12-375 1.34e-173

2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.


Pssm-ID: 130859  Cd Length: 368  Bit Score: 488.03  E-value: 1.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:TIGR01800   2 GLEGVIAGETALSTIDGsGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKD--DFSDQDDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:TIGR01800  82 PAESHPMDVLRTAVSYLGALDPEKFghTPEEARDIAIRLLAKLPTIVAYWYRIRH-GGEIIAPKDDDSIAGNFLYMLHGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:TIGR01800 161 EPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMkEKRPSLPPNADFYSASAYHFMGIP 325
Cdd:TIGR01800 241 KALENKERIMGFGHRVYKT-YDPRAKILKEYAKKLSakeGSSKWYEIAERLEDVM-EEEKGIYPNVDFFSASVYYMMGIP 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 326 TPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:TIGR01800 319 TDLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
12-358 3.42e-149

Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 425.38  E-value: 3.42e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFSDQDDKII---RLLGVLPSVLCYWHHYVNSGKEIDFNSQqDSIAGYFLERLEL 167
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENAlrdDLIAKLPTIAAYIYRHRRGLPPIYPDPD-LSYAENFLYMLFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 168 KEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGV 247
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 248 NQKLE-NKELLMGFGHRVYGLgGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLM----KEKRPSLPPNADFYSASAY 319
Cdd:pfam00285 240 RKVLNkGKERIMGFGHRVYKN-YDPRAKILKEFAEELaeeGGDDPLLELAEELEEVApedlYFVEKNLYPNVDFYSGVLY 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1751924788 320 HFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPS 358
Cdd:pfam00285 319 HALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
Cit_synThplmales NF041157
citrate synthase;
17-375 1.10e-93

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 284.98  E-value: 1.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  17 IAGESAIctcglgngLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHP 96
Cdd:NF041157   20 IDGEKGI--------LRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  97 MNLMQTAVSALGALESEKDDFSDQDDKIIRLLGVLPSVLC--YWHhyvNSGKEIDFNSQQDSIAGYFLERLELKEPKADF 174
Cdd:NF041157   92 LAMMETAFSALASIENYKWNKENDREKALKIIGKASTIVAnvYRH---KEGLKPRIPEPSESYAESFLRATFGRKPSEEE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 175 VKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQK-LEN 253
Cdd:NF041157  169 IKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNENiING 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 254 KELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYL----MKEKRpsLPPNADFYSASAYHFMGIPT 326
Cdd:NF041157  249 KKRLMGFGHRVYKT-YDPRAKIFKEYAEKLAstnEAKKYLEIAEKLEELgikhFGSKG--IYPNTDFYSGIVFYSLGFPV 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRAN-NKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:NF041157  326 YMFTSLFALSRVLGWLAHIIEYVEEqHRLIRPRALYVGPEKRDFVPIDER 375
 
Name Accession Description Interval E-value
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
11-372 0e+00

Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate though it has partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate and prefer PrCoA as substrate, but can also use AcCoA. Re 2-MCS1 can use butyryl-CoA and valeryl-CoA at a lower rate. A second Ralstonia eutropha 2MCS, Re 2-MCS2, which is induced on propionate is also found in this group. This group may include proteins which may function exclusively as a CS, those which may function exclusively as a 2MCS, or those with dual specificity which functions as both a CS and a 2MCS.


Pssm-ID: 99861 [Multi-domain]  Cd Length: 363  Bit Score: 638.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:cd06108     1 GGLAGVVAGQTAISTVGKgGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDTHPMNLMQTAVSALGALESEkDDFSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAGYFLERLELKE 169
Cdd:cd06108    81 IPKDSHPMDVMRTGCSMLGCLEPE-NEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 170 PKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQ 249
Cdd:cd06108   160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 250 KLENKELLMGFGHRVYgLGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKrPSLPPNADFYSASAYHFMGIPT 326
Cdd:cd06108   240 KLERKELIMGFGHRVY-KEGDPRSDIIKKWSKKLseeGGDPLLYQISERIEEVMWEE-KKLFPNLDFYSASAYHFCGIPT 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:cd06108   318 ELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
PRK12351 PRK12351
methylcitrate synthase; Provisional
4-375 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 561.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788   4 SEAKKKTG-GLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSE 81
Cdd:PRK12351    2 AAFKPKKSvALSGVVAGNTALCTVGKsGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  82 NLKAILRAIPKDTHPMNLMQTAVSALGALESEKDD--FSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAG 159
Cdd:PRK12351   82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEDhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 160 YFLERLELKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKN 239
Cdd:PRK12351  162 HFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDT 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 240 EEEAISGVNQKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRpSLPPNADFYSA 316
Cdd:PRK12351  242 PDEAEADIRRRVENKEVVIGFGHPVYTI-SDPRNKVIKEVAKKLskeAGDTKLYDIAERLETVMWEEK-KMFPNLDWFSA 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1751924788 317 SAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK12351  320 VSYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
12-375 0e+00

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 508.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:COG0372    16 GLEGVVAGETAISYIdGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFS--DQDDKIIRLLGVLPSVLCYWHHYvNSGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:COG0372    96 PRDAHPMDVLRTAVSALGAFDPDADDIDpeARLEKAIRLIAKLPTIAAYAYRY-RRGLPPVYPDPDLSYAENFLYMLFGE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:COG0372   175 EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMKEKRPS----LPPNADFYSASAYHF 321
Cdd:COG0372   255 KALDKKERIMGFGHRVYKN-YDPRAKILKEAAEELLeelGDDPLLEIAEELEEVALEDEYFiekkLYPNVDFYSGIVYHA 333
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1751924788 322 MGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:COG0372   334 LGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
12-375 1.34e-173

2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.


Pssm-ID: 130859  Cd Length: 368  Bit Score: 488.03  E-value: 1.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:TIGR01800   2 GLEGVIAGETALSTIDGsGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKD--DFSDQDDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:TIGR01800  82 PAESHPMDVLRTAVSYLGALDPEKFghTPEEARDIAIRLLAKLPTIVAYWYRIRH-GGEIIAPKDDDSIAGNFLYMLHGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:TIGR01800 161 EPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMkEKRPSLPPNADFYSASAYHFMGIP 325
Cdd:TIGR01800 241 KALENKERIMGFGHRVYKT-YDPRAKILKEYAKKLSakeGSSKWYEIAERLEDVM-EEEKGIYPNVDFFSASVYYMMGIP 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 326 TPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:TIGR01800 319 TDLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
13-372 4.00e-153

Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate, but has a partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate, prefer PrCoA as substrate, but can also can use AcCoA. Re 2-MCS1 at a low rate can use butyryl-CoA and valeryl-CoA. A second Ralstonia eutropha 2MCS is also found in this group, Re 2-MCS2, which is induced on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 435.81  E-value: 4.00e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  13 LAGIIAGESAICTCG-LGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIP 91
Cdd:cd06117     3 LSGVAAGNTALCTVGrSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  92 KDTHPMNLMQTAVSALGALESEKDDF--SDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAGYFLERLELKE 169
Cdd:cd06117    83 AAAHPMDVMRTGVSVLGCVLPEKEDHpvSGARDIADRLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLHGEK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 170 PKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQ 249
Cdd:cd06117   163 PSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRR 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 250 KLENKELLMGFGHRVYGLgGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRpSLPPNADFYSASAYHFMGIPT 326
Cdd:cd06117   243 RVENKEVVIGFGHPVYTI-ADPRNQVIKEVAKQLskeGGDMKMFDIAERLETVMWEEK-KMFPNLDWFSAVSYHMMGVPT 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:cd06117   321 AMFTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
12-358 3.42e-149

Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 425.38  E-value: 3.42e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFSDQDDKII---RLLGVLPSVLCYWHHYVNSGKEIDFNSQqDSIAGYFLERLEL 167
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENAlrdDLIAKLPTIAAYIYRHRRGLPPIYPDPD-LSYAENFLYMLFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 168 KEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGV 247
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 248 NQKLE-NKELLMGFGHRVYGLgGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLM----KEKRPSLPPNADFYSASAY 319
Cdd:pfam00285 240 RKVLNkGKERIMGFGHRVYKN-YDPRAKILKEFAEELaeeGGDDPLLELAEELEEVApedlYFVEKNLYPNVDFYSGVLY 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1751924788 320 HFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPS 358
Cdd:pfam00285 319 HALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
12-363 1.57e-140

Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99863 [Multi-domain]  Cd Length: 356  Bit Score: 403.58  E-value: 1.57e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:cd06110     2 GLEGVIAADSKISYIdGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFSDQD--DKIIRLLGVLPSVLCYWHHyVNSGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:cd06110    82 PKDAHPMDVLRTAVSALALYDPEADDMSREAnlRKAIRLIAKMPTIVAAFHR-IRNGLEPVAPDPDLSHAANFLYMLTGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:cd06110   161 KPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMKEKRpSLPPNADFYSASAYHFMGIP 325
Cdd:cd06110   241 DKLANKEKIMGFGHRVYKT-GDPRAKHLREMSRRLGketGEPKWYEMSEAIEQAMRDEK-GLNPNVDFYSASVYYMLGIP 318
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1751924788 326 TPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIG 363
Cdd:cd06110   319 VDLFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-361 3.44e-140

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.


Pssm-ID: 99871 [Multi-domain]  Cd Length: 358  Bit Score: 402.75  E-value: 3.44e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:cd06118     1 PGLEGVKAKETSISYIDGDEGiLRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDTHPMNLMQTAVSALGALESEKDDFSDQ--DDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFLERLEL 167
Cdd:cd06118    81 LPKNAHPMDVLRTAVSALGSFDPFARDKSPEarYEKAIRLIAKLPTIAANIYRNRE-GLEIIAPDPDLSYAENFLYMLFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 168 KEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGV 247
Cdd:cd06118   160 EEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 248 NQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRPS--LPPNADFYSASAYHFM 322
Cdd:cd06118   240 WKKLANKRRIMGFGHRVYK-TYDPRAKILKELAEELaeeKGDDKLFEIAEELEEIALEVLGEkgIYPNVDFYSGVVYKAL 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1751924788 323 GIPTPYFTPIFIMSRVSGWCAHIKEQRANN-KLIRPSSEY 361
Cdd:cd06118   319 GFPTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
1-372 4.30e-129

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 375.06  E-value: 4.30e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788   1 MSVSEAKKktgGLAGIIAGESAIC-----TcglgNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIK 75
Cdd:PRK14033    4 DETPEIKK---GLAGVVVDTTAISkvvpeT----NSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  76 HRALSENLKAILRAIPKDTHPMNLMQTAVSALGALESEKDDfSDQD---DKIIRLLGVLPSVLCYWHHYvNSGKEIDFNS 152
Cdd:PRK14033   77 YRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADD-SSPEanlAKALRLFAVLPTIVAADQRR-RRGLDPIAPR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 153 QQDSIAGYFLERLELKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMG 232
Cdd:PRK14033  155 SDLGYAENFLHMCFGEVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMH 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 233 LISSFKNEEEAISGVNQKLENKELLMGFGHRVYGlGGDPR-----NALIKVwSKRLGGDTMLfKISEAIEYLMkEKRPSL 307
Cdd:PRK14033  235 TMLEIGDPARAAEWLRDALARKEKVMGFGHRVYK-HGDSRvptmkAALRRV-AAVRDGQRWL-DIYEALEKAM-AEATGI 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751924788 308 PPNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:PRK14033  311 KPNLDFPAGPAYYLMGFDIDFFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVPPI 375
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
12-368 1.12e-128

Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. DsCS, compared with CS from the hyperthermophile Pyrococcus furiosus (not included in this group), has an increase in the size of surface loops, a higher proline content in the loop regions, a more accessible active site, and a higher number of intramolecular ion pairs. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. For example, included in this group are Corynebacterium glutamicum (Cg) PrpC1 and -2, which are only synthesized during growth on propionate-containing medium, can use PrCoA, AcCoA and butyryl-CoA as substrates, and have comparable catalytic activity with AcCoA as the major CgCS (GltA, not included in this group).


Pssm-ID: 99864 [Multi-domain]  Cd Length: 362  Bit Score: 373.67  E-value: 1.12e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGL-GNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:cd06111     2 GLAGVVADTTAISKVMPeTNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDfSDQD---DKIIRLLGVLPSVLCYWHHYvNSGKEIDFNSQQDSIAGYFLERLEL 167
Cdd:cd06111    82 PKNCHPMDVLRTAVSVLGAEDSETDD-SSPDanlAKAIRLLAQLPTVVAADIRR-RKGLDPIPPDSDLGIAENFLHMCFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 168 KEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGV 247
Cdd:cd06111   160 EVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 248 NQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMkEKRPSLPPNADFYSASAYHFMGI 324
Cdd:cd06111   240 LDALARKEKVMGFGHRVYK-SGDSRVPTMEKALRRVAavhDGQKWLAMYDALEDAM-VAAKGIKPNLDFPAGPAYYLMGF 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1751924788 325 PTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRS 368
Cdd:cd06111   318 DIDFFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPEQRP 361
PRK14035 PRK14035
citrate synthase; Provisional
10-375 1.06e-117

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 345.98  E-value: 1.06e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  10 TGGLAGIIAGESAICTCgLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENL-KAILR 88
Cdd:PRK14035    4 QRGLEGVIAAETKISSI-IDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVyQHFEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  89 AIPKDTHPMNLMQTAVSALGALESEKDDFSDQD--DKIIRLLGVLPSVLCYWHHyVNSGKEIDFNSQQDSIAGYFLERLE 166
Cdd:PRK14035   83 YSTDHVHPMTALRTSVSYLAHFDPDAEEESDEAryERAIRIQAKVASLVTAFAR-VRQGKEPLKPRPDLSYAANFLYMLR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 167 LKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISG 246
Cdd:PRK14035  162 GELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVDAY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 247 VNQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRpSLPPNADFYSASAYHFMG 323
Cdd:PRK14035  242 LDEKFANKEKIMGFGHRVYK-DGDPRAKYLREMSRKItkgTGREELFEMSVKIEKRMKEEK-GLIPNVDFYSATVYHVMG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1751924788 324 IPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK14035  320 IPHDLFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
PRK14034 PRK14034
citrate synthase; Provisional
10-375 1.29e-115

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 340.59  E-value: 1.29e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  10 TGGLAGIIAGESAICTCgLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:PRK14034    4 TRGLEGVVATTSSVSSI-IDDTLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDT-HPMNLMQTAVSALGALESEKDDFSDQDD--KIIRLLGVLPSVLCYWHHyVNSGKEIDFNSQQDSIAGYFLERLE 166
Cdd:PRK14034   83 YDLKKvHPMSVLRTAISMLGLYDEEAEIMDEEANyrKAVRLQAKVPTIVAAFSR-IRKGLDPVEPRKDLSLAANFLYMLN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 167 LKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISG 246
Cdd:PRK14034  162 GEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVESY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 247 VNQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMKEKRpSLPPNADFYSASAYHFMG 323
Cdd:PRK14034  242 IHNKLQNKEKIMGFGHRVYR-QGDPRAKHLREMSKRLTvllGEEKWYNMSIKIEEIVTKEK-GLPPNVDFYSASVYHCLG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1751924788 324 IPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK14034  320 IDHDLFTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
12-370 4.85e-107

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.


Pssm-ID: 99865  Cd Length: 373  Bit Score: 318.98  E-value: 4.85e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:cd06112     4 GLAGVPAAESSISYIDGKNGiLEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGAL----ESEKDDFSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDsIAGYFLERLE 166
Cdd:cd06112    84 PETGHPMDMLQATVAALGMFypkpEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLD-YAENFLYMLF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 167 LKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISG 246
Cdd:cd06112   163 GEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVKAY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 247 VNQKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRL----GGDTMLFKISEAIEYLMKEKRPS--LPPNADFYSASAYH 320
Cdd:cd06112   243 LDKKLANKQKIWGFGHRVYKT-KDPRATILQKLAEDLfakmGELSKLYEIALEVERLCEELLGHkgVYPNVDFYSGIVYK 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 321 FMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFV 370
Cdd:cd06112   322 ELGIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYV 371
PRK14036 PRK14036
citrate synthase; Provisional
12-375 1.69e-104

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 312.66  E-value: 1.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:PRK14036    7 GLEGVPATQSSISYVDGQKGiLEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALES--EKDDFSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDsIAGYFLERLELK 168
Cdd:PRK14036   87 PETGHPMDALQASAAALGLFYSrrALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLD-YAANFLYMLTER 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:PRK14036  166 EPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSVENVRPYLD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLgGDPR----NALIKVWSKRLGGDTMlFKISEAIEYLMKEKRPS--LPPNADFYSASAYHFM 322
Cdd:PRK14036  246 ERLANKQKIMGFGHREYKV-KDPRatilQKLAEELFARFGHDEY-YEIALELERVAEERLGPkgIYPNVDFYSGLVYRKL 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1751924788 323 GIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK14036  324 GIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
PRK12349 PRK12349
citrate synthase;
12-365 1.99e-103

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 309.73  E-value: 1.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:PRK12349    8 GLDGVIAAETKISFLDTVKGeIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 PKDTHPMNLMQTAVSALGALESEKDDFSD--QDDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFLERLELK 168
Cdd:PRK12349   88 PKETHPMDGLRTGVSALAGYDNDIEDRSLevNKSRAYKLLSKVPNIVANSYHILN-NEEPIEPLKELSYSANFLYMLTGK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 169 EPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVN 248
Cdd:PRK12349  167 KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEELLQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 249 QKLENKELLMGFGHRVYGLGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRpSLPPNADFYSASAYHFMGIP 325
Cdd:PRK12349  247 KKLYNKEKIMGFGHRVYMKKMDPRALMMKEALKQLcdvKGDYTLYEMCEAGEKIMEKEK-GLYPNLDYYAAPVYWMLGIP 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1751924788 326 TPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPK 365
Cdd:PRK12349  326 IQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIGER 365
Cit_synThplmales NF041157
citrate synthase;
17-375 1.10e-93

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 284.98  E-value: 1.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  17 IAGESAIctcglgngLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHP 96
Cdd:NF041157   20 IDGEKGI--------LRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  97 MNLMQTAVSALGALESEKDDFSDQDDKIIRLLGVLPSVLC--YWHhyvNSGKEIDFNSQQDSIAGYFLERLELKEPKADF 174
Cdd:NF041157   92 LAMMETAFSALASIENYKWNKENDREKALKIIGKASTIVAnvYRH---KEGLKPRIPEPSESYAESFLRATFGRKPSEEE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 175 VKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQK-LEN 253
Cdd:NF041157  169 IKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNENiING 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 254 KELLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYL----MKEKRpsLPPNADFYSASAYHFMGIPT 326
Cdd:NF041157  249 KKRLMGFGHRVYKT-YDPRAKIFKEYAEKLAstnEAKKYLEIAEKLEELgikhFGSKG--IYPNTDFYSGIVFYSLGFPV 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRAN-NKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:NF041157  326 YMFTSLFALSRVLGWLAHIIEYVEEqHRLIRPRALYVGPEKRDFVPIDER 375
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
12-363 4.26e-88

Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-I, one of two CS isozymes in the gram-positive B. subtilis. The majority of CS activity in B. subtilis is provided by the other isozyme, BsCS-II (not included in this group). BsCS-I has a lower catalytic activity than BsCS-II, and has a Glu in place of a key catalytic Asp residue. This change is conserved in other members of this group. For E. coli CS (not included in this group), site directed mutagenesis of the key Asp residue to a Glu converts the enzyme into citryl-CoA lyase which cleaves citryl-CoA to AcCoA and OAA. A null mutation in the gene encoding BsCS-I (citA) had little effect on B. subtilis CS activity or on sporulation. However, disruption of the citA gene in a strain null for the gene encoding BsCS-II resulted in a sporulation deficiency, a characteristic of strains defective in the Krebs cycle. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. Many of the gram-negative species represented in this group have a second CS isozyme which is in another group.


Pssm-ID: 99862 [Multi-domain]  Cd Length: 349  Bit Score: 269.56  E-value: 4.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAI 90
Cdd:cd06109     2 GLEGVVAAETVLSDVdGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  91 pKDTHPMNLMQTAVSALGAlesekddfSDQDDKIIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAGYfLERLELKEP 170
Cdd:cd06109    82 -AGLDPMDALRALLALLPD--------SPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADY-LRMLTGEPP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 171 KADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQK 250
Cdd:cd06109   152 SEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 251 LENKELLMGFGHRVYGLgGDPRNALIKVWSKRLGGDTMLFKISEAIEY----LMKEKRP--SLPPNADFYSASAYHFMGI 324
Cdd:cd06109   232 LARGERLMGFGHRVYRV-RDPRADVLKAAAERLGAPDERLEFAEAVEQaalaLLREYKPgrPLETNVEFYTALLLEALGL 310
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1751924788 325 PTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIG 363
Cdd:cd06109   311 PREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
32-363 1.07e-82

Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding.


Pssm-ID: 99867  Cd Length: 400  Bit Score: 257.51  E-value: 1.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:cd06114    51 LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFY 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SE---KDDFSDQDDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFL-----ERLELKEPKADFVKAMHCSLI 183
Cdd:cd06114   131 PDsldVNDPEQRELAAIRLIAKVPTIAAMAYRYSI-GQPFIYPDNDLSYVENFLhmmfaVPYEPYEVDPVVVKALDTILI 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 184 LYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL---ISSFKNEEEAISGVNQKlENKELLMGF 260
Cdd:cd06114   210 LHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMleeIGSVGNVDKYIAKAKDK-NDPFRLMGF 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 261 GHRVYGlGGDPRNALIKVWSKR----LGGDTMLFKISEAIE-------YLMKEKrpsLPPNADFYSASAYHFMGIPTPYF 329
Cdd:cd06114   289 GHRVYK-NYDPRAKILKKTCDEvlaeLGKDDPLLEIAMELEeialkddYFIERK---LYPNVDFYSGIILRALGIPTEMF 364
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1751924788 330 TPIFIMSRVSGWCAHIKEQRAN--NKLIRPSSEYIG 363
Cdd:cd06114   365 TVLFALGRTPGWIAQWREMHEDpeLKIGRPRQLYTG 400
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-361 3.33e-82

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and form homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99855 [Multi-domain]  Cd Length: 265  Bit Score: 251.46  E-value: 3.33e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLLQYGELPkkdelkaykekiikhralsenlkailra 89
Cdd:cd06101     1 PGLRGVAALESEISVIdGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 ipkdthpmnlmqtavsalgalesekddfsdqddkiirllgvlpsvlcywhhyvnsgkeidfnsqqdSIAGYFLERLELKE 169
Cdd:cd06101    53 ------------------------------------------------------------------SYAENFLYMLGGEE 66
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 170 PKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNE--EEAISGV 247
Cdd:cd06101    67 PDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPknEPAEAYI 146
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 248 NQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRPS--LPPNADFYSASAYHFM 322
Cdd:cd06101   147 RKKLNSKRVLMGFGHRVYK-KYDPRATVLKKFAEKLlkeKGLDPMFELAAELEKIAPEVLYEkkLYPNVDFYSGVLYKAM 225
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1751924788 323 GIPTPYFTPIFIMSRVSGWCAHIKEQRANN-KLIRPSSEY 361
Cdd:cd06101   226 GFPTELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
32-363 5.27e-79

Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs, including EcCS, are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding. C. aurantiacus is a gram-negative thermophilic green gliding bacterium; its CS belonging to this group may be a type I CS. It is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group. This group also contains three Arabidopsis peroxisomal CS proteins, CYS-1, -2, and -3 which participate in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and perhaps is located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99860  Cd Length: 382  Bit Score: 247.35  E-value: 5.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:cd06107    29 LLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRDAHPMGILCAGLSALSAFY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SEKDDFSDQDD----------KIIRLLGVLPSV--LCYWHHyvnSGKEIDFNSQQDSIAGYFLERLELK-----EPKADF 174
Cdd:cd06107   109 PEAIPAHTGDLyqnnpevrdkQIIRTLAKMPTIaaAAYCHR---IGRPFVYPRANLSYIENFLYMMGYVdqepyEPNPRL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 175 VKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAA---MGLISSFKNEEEAISGVNQKl 251
Cdd:cd06107   186 ARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAAlkmLREIGTPENVPAFIERVKNG- 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 252 enKELLMGFGHRVYGlGGDPRNALIKVWSKRLGGDTM---LFKISEAIE-------YLMKEKrpsLPPNADFYSASAYHF 321
Cdd:cd06107   265 --KRRLMGFGHRVYK-NYDPRAKVIREILHEVLTEVEkdpLLKVAMELErialedeYFVSRK---LYPNVDFYSGFIYKA 338
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1751924788 322 MGIPTPYFTPIFIMSRVSGWCAHIKEQ--RANNKLIRPSSEYIG 363
Cdd:cd06107   339 LGFPPEFFTVLFAVARTSGWMAHWREMmeDPLQRIWRPRQVYTG 382
PRK14037 PRK14037
citrate synthase; Provisional
32-375 6.84e-79

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 246.97  E-value: 6.84e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:PRK14037   28 LRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGLMEAAFAALASID 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SEKDDFSDQDDKIIRLLGVLPSVLCYWHHYVNsGKEIDFNSQQDSIAGYFLERLELKEPKADFVKAMHCSLILYAEHEFN 191
Cdd:PRK14037  108 KNFKWKENDKEKAISIIAKMATIVANVYRRKE-GNKPRIPEPSDSFAESFLLASFAREPTAEEIKAMDAALILYTDHEVP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 192 ASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNEEEAISGVNQK-LENKELLMGFGHRVYGLgGD 270
Cdd:PRK14037  187 ASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKiINGKKRLMGFGHRVYKT-YD 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 271 PRNALIKVWSKRLGGDT----MLFKISEAIEYLMKEKRPS--LPPNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAH 344
Cdd:PRK14037  266 PRAKIFKELAETLIERNseakKYFEIAQKLEELGIKQFGSkgIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAH 345
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1751924788 345 IKEQRAN-NKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PRK14037  346 IIEYVEEqHRLIRPRALYVGPEHREYVPIDKR 377
gltA PRK05614
citrate synthase;
32-363 5.51e-78

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 245.94  E-value: 5.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:PRK05614   69 LLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SEKDDFSDQDDK---IIRLLGVLPSVLCYWHHYvNSGKEIDFNSQQDSIAGYFLERL-----ELKEPKADFVKAMHCSLI 183
Cdd:PRK05614  149 HDSLDINDPEHReiaAIRLIAKMPTLAAMAYKY-SIGQPFVYPRNDLSYAENFLRMMfatpcEEYEVNPVLVRALDRIFI 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 184 LYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL---ISSFKNEEEAISGVNQKlENKELLMGF 260
Cdd:PRK05614  228 LHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMleeIGSVDNIPEFIARAKDK-NDGFRLMGF 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 261 GHRVYGlGGDPRNALIK-----VWSKrLGGDTMLFKISEAIE-------YLMKEKrpsLPPNADFYSASAYHFMGIPTPY 328
Cdd:PRK05614  307 GHRVYK-NYDPRAKIMRetcheVLKE-LGLNDPLLEVAMELEeialndeYFIERK---LYPNVDFYSGIILKALGIPTSM 381
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1751924788 329 FTPIFIMSRVSGWCAHIKEQRAN--NKLIRPSSEYIG 363
Cdd:PRK05614  382 FTVIFALARTVGWIAHWNEMHSDpeQKIGRPRQLYTG 418
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
156-361 1.11e-76

Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.


Pssm-ID: 99853 [Multi-domain]  Cd Length: 213  Bit Score: 235.69  E-value: 1.11e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 156 SIAGYFLERLELKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL-- 233
Cdd:cd06099     1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMle 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 234 -ISSFKNEE-EAIsgVNQKLENKELLMGFGHRVYGlGGDPRNALIKVWSKRL---GGDTMLFKISEAIEYLMKEKRPS-- 306
Cdd:cd06099    81 eIGTPKNEPaEAY--IRKKLESKRVIMGFGHRVYK-KYDPRATVLKKFAEELlkeDGDDPMFELAAELEKIAEEVLYEkk 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1751924788 307 LPPNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANN-KLIRPSSEY 361
Cdd:cd06099   158 LYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
32-370 1.15e-73

Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99868  Cd Length: 410  Bit Score: 234.64  E-value: 1.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:cd06115    49 LRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SE-------KDDFSD---QDDKIIRLLGVLPSVL-CYWHHyvNSGKEIDFNSQQDSIAGYFLERLE-LKE----PKADFV 175
Cdd:cd06115   129 PEanpalagQDIYKNkqvRDKQIVRILGKAPTIAaAAYRR--RAGRPPNLPSQDLSYTENFLYMLDsLGErkykPNPRLA 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 176 KAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL---ISSFKNEEEAISGVNQKle 252
Cdd:cd06115   207 RALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMlaeIGTVENIPAFIEGVKNR-- 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 253 nKELLMGFGHRVYGlGGDPRNALIKVWSKR----LGGD------TMLFKISEAIEYLMKEKrpsLPPNADFYSASAYHFM 322
Cdd:cd06115   285 -KRKLSGFGHRVYK-NYDPRAKIIKKLADEvfeiVGKDplieiaVALEKAALSDEYFVKRK---LYPNVDFYSGLIYRAM 359
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1751924788 323 GIPTPYFTPIFIMSRVSGWCAHIKEQRAN--NKLIRPSSEYIGPKPRSFV 370
Cdd:cd06115   360 GFPTDFFPVLFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYV 409
PLN02456 PLN02456
citrate synthase
11-375 1.89e-71

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 230.30  E-value: 1.89e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGLGNG-LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRA 89
Cdd:PLN02456   66 PGYRNTAPVLSEISLIDGDEGiLRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  90 IPKDTHPMNLMQTAVSALGALESEKDDFSDQDDK----------IIRLLGVLPSVLCYWHHYVNSGKEIDFNSQQDSIAG 159
Cdd:PLN02456  146 LPHDAHPMTQLVSGVMALSTFSPDANAYLRGQHKykswevrdedIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAEN 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 160 --YFLERLELKEPKAD--FVKAMHCSLILYAEHEFNASTFTAR-VCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLI 234
Cdd:PLN02456  226 flYMLGSLGDRSYKPDprLARLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 235 SSFKNEEEAISGVNQKLENKELLMGFGHRVYGlGGDPRNALIKVWS---KRLGGDTMLFKISEAI-------EYLMKEKr 304
Cdd:PLN02456  306 KEIGTVENIPEYVEGVKNSKKVLPGFGHRVYK-NYDPRAKCIREFAlevFKHVGDDPLFKVASALeevalldEYFKVRK- 383
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751924788 305 psLPPNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQR--ANNKLIRPSSEYIGPKPRSFVAIDKR 375
Cdd:PLN02456  384 --LYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALglPDERIMRPKQVYTGEWLRHYCPKAER 454
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
32-363 7.46e-71

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) a carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) hydrolysis of citryl-CoA to produce citrate and CoA. CSs are found in two structural types: type I (homodimeric) and type II CSs (homohexameric). Type II CSs are unique to gram-negative bacteria. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria. Type I CS is active as a homodimer, both subunits participating in the active site. Type II CS is a hexamer of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99866  Cd Length: 406  Bit Score: 227.15  E-value: 7.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAE------FEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLK--AILRAIPKDThpMNLMQTA 103
Cdd:cd06113    38 LYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVedVILKAPSKDI--MNKLQRS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 104 VSALGALESEKDDFSDQD--DKIIRLLGVLPSVLCYW-----HHYVNSGKEIDFNSQQDSIAGYFLERLElkePKADF-- 174
Cdd:cd06113   116 VLALYSYDDKPDDISLENvlRQSIQLIARLPTIAVYAyqakrHYYDGESLYIHHPQPELSTAENILSMLR---PDKKYte 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 175 --VKAMHCSLILYAEHEF-NASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL-------ISSFKNEEEaI 244
Cdd:cd06113   193 leAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMledikenVKDWTDEDE-V 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 245 SGVNQKLENKE------LLMGFGHRVYGLgGDPRNALIKVWSKRLG---GDTMLFKISEAIEYLMKE-------KRPSLP 308
Cdd:cd06113   272 RAYLRKILNKEafdksgLIYGMGHAVYTL-SDPRAVVLKKYARSLAkekGREEEFALYERIERLAPEviaeergIGKTVC 350
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1751924788 309 PNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAH-IKEQRANNKLIRPSSEYIG 363
Cdd:cd06113   351 ANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHrIEELLNSGRIIRPAYKYVG 406
PRK14032 PRK14032
citrate synthase; Provisional
32-375 8.23e-70

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 225.55  E-value: 8.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAE------FEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKA--ILRAIPKDThpMNLMQTA 103
Cdd:PRK14032   68 LYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRdmILKAPSKDI--MNSLARS 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 104 VSALGALESEKDDFSDQD--DKIIRLLGVLPSVLCYWH----HYVNSGKEIDFNSQQD-SIAGYFLERLElkePKADFVK 176
Cdd:PRK14032  146 VLALYSYDDNPDDTSIDNvlRQSISLIARFPTLAVYAYqayrHYHDGKSLYIHPPKPElSTAENILYMLR---PDNKYTE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 177 --AM--HCSLILYAEHEF-NASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNE------EEAIS 245
Cdd:PRK14032  223 leARllDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENvkdwedEDEIA 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 246 GVNQKLENKE------LLMGFGHRVYGLgGDPRNALIKVWSKRLGGDTML---FKISEAIEYLMKE---------KRPSl 307
Cdd:PRK14032  303 DYLTKILNKEafdksgLIYGMGHAVYTI-SDPRAVILKKFAEKLAKEKGReeeFNLYEKIEKLAPEliaeergiyKGVS- 380
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751924788 308 pPNADFYSASAYHFMGIPTPYFTPIFIMSRVSGWCAH-IKEQRANNKLIRPSSEYIGPkPRSFVAIDKR 375
Cdd:PRK14032  381 -ANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHrIEELVNGGKIIRPAYKSVLE-RREYVPLEER 447
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
32-369 4.88e-65

citrate synthase I (hexameric type); This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes. [Energy metabolism, TCA cycle]


Pssm-ID: 273811  Cd Length: 412  Bit Score: 212.33  E-value: 4.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:TIGR01798  56 LLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFY 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SEKDDFSDQDDK---IIRLLGVLPSV--LCYWHHYvnsGKEIDFNSQQDSIAGYFLERL-----ELKEPKADFVKAMHCS 181
Cdd:TIGR01798 136 HDALDINDPRHReisAIRLIAKIPTLaaMSYKYSI---GQPFVYPRNNLSYAENFLHMMfatpcEDYKVNPVLARAMDRI 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 182 LILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL---ISSFKNEEEAISGVNQKlENKELLM 258
Cdd:TIGR01798 213 FILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMleeIGSVKNIDEFIKKVKDK-NDPFRLM 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 259 GFGHRVYGlGGDPRNALIKVWS----KRLG-GDTMLFKISEAIE-------YLMKEKrpsLPPNADFYSASAYHFMGIPT 326
Cdd:TIGR01798 292 GFGHRVYK-NYDPRAKVMRETChevlKELGlHDDPLFKLAMELEkialndpYFIERK---LYPNVDFYSGIILKAMGIPT 367
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1751924788 327 PYFTPIFIMSRVSGWCAHIKEQRANN--KLIRPSSEYIGPKPRSF 369
Cdd:TIGR01798 368 SMFTVIFALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
PRK12350 PRK12350
citrate synthase 2; Provisional
12-368 3.02e-64

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 208.28  E-value: 3.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  12 GLAGIIAGESAICTC-GLGNGLNYYGYNIEDLAQNAEFEEIAFLL---QYGELPKKDElkaykekiikhralSENLKAIL 87
Cdd:PRK12350    4 GLEGVVAFETEIAEPdGDGGALRYRGVDIEDLVGRVTFEDVWALLvdgRFGPGLPPAE--------------PFPLPVHL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  88 RAIPKDTHPMNLMQTAVSALGALESEkDDFSDQDDkiirLLGVLPSVLCY-------WHHYVNSGKEIDfnsQQDSIAGY 160
Cdd:PRK12350   70 GDARVDVQAALAMLAPVWGFRPLLDI-DDLTARLD----LARASVMALSAvaqsargIGQPAVPQREID---HAATILER 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 161 FLERLElKEPKADFVKAMHCSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNE 240
Cdd:PRK12350  142 FMGRWR-GEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVERT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 241 EEAISGVNQKLENKELLMGFGHRVYgLGGDPRNALIKVWSKRLGGDtmLFKISEAIEY----LMKEKRP--SLPPNADFY 314
Cdd:PRK12350  221 GDARGWVKGALDRGERLMGFGHRVY-RAEDPRARVLRATAKRLGAP--RYEVAEAVEQaalaELRERRPdrPLETNVEFW 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1751924788 315 SASAYHFMGIPTPYFTPIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIGPKPRS 368
Cdd:PRK12350  298 AAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPAPRS 351
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
32-372 1.32e-63

Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.


Pssm-ID: 99869  Cd Length: 384  Bit Score: 207.76  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  32 LNYYGYNIEDLAQNAEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGALE 111
Cdd:cd06116    29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 112 SEKDDFSDQDDK---IIRLLGVLPSVLCY-WHHYVnsGKEIDFNSQQDSIAGYFLERL-ELKEPKAD----FVKAMHCSL 182
Cdd:cd06116   109 PEAKNIGDEEQRnkqIIRLIGKMPTIAAFaYRHRL--GLPYVLPDNDLSYTGNFLSMLfKMTEPKYEpnpvLAKALDVLF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 183 ILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL---ISSFKNEEEAISGVNQkleNKELLMG 259
Cdd:cd06116   187 ILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMlqqIGSPKNIPDFIETVKQ---GKERLMG 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 260 FGHRVYGlGGDPRNALIKVWSKRLGGDT----------MLFKISEAIEYLMKEKrpsLPPNADFYSASAYHFMGIPTPYF 329
Cdd:cd06116   264 FGHRVYK-NYDPRARIIKKIADEVFEATgrnplldiavELEKIALEDEYFISRK---LYPNVDFYSGLIYQALGFPTEAF 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1751924788 330 TPIFIMSRVSGWCAHIKE--QRANNKLIRPSSEYIGPKPRSFVAI 372
Cdd:cd06116   340 TVLFAIPRTSGWLAQWIEmlRDPEQKIARPRQVYTGPRDRDYVPI 384
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
154-363 2.70e-41

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 146.25  E-value: 2.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 154 QDSIAGYFLERLELKEPKADFVKAmhcSLILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGL 233
Cdd:cd06102    80 DAPVHRRLARAWGLDPAAADLLRR---ALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEAL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 234 ISSFKNEEEAISGVNQKLENKELLMGFGHRVYgLGGDPRNALIKVWSKRLGGDTMLF--KISEAIEYLMKEkrpslPPNA 311
Cdd:cd06102   157 LDEALRAGDAEAAVRERLRRGEALPGFGHPLY-PDGDPRAAALLAALRPLGPAAPPAarALIEAARALTGA-----RPNI 230
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1751924788 312 DFYSASAYHFMGIP-TPYFTpIFIMSRVSGWCAHIKEQRANNKLIRPSSEYIG 363
Cdd:cd06102   231 DFALAALTRALGLPaGAAFA-LFALGRSAGWIAHALEQRAQGKLIRPRARYVG 282
PRK09569 PRK09569
citrate (Si)-synthase;
11-375 1.09e-30

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 121.40  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGLGNGLNYYGYNIEDLAQN---------AEFEEIAFLLQYGELPKKDELKAYKEKIIKHRALSE 81
Cdd:PRK09569   40 GGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEAlpkapgseyPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  82 NLKAILRAIPKDTHPMNLMQTAVSAL------------GALEsEKDDFSDQDDKIIRLLGVLPSVLC--YWHHYVNsGKE 147
Cdd:PRK09569  120 YVIDAIRALPRDSHPMVMLSVGILAMqreskfakfyneGKFN-KMDAWEYMYEDASDLVARIPVIAAyiYNLKYKG-DKQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 148 IDFNSQQDsIAGYFLERLELKEPKADfvkAMHCSLILYAEHEF-NASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGA 226
Cdd:PRK09569  198 IPSDPELD-YGANFAHMIGQPKPYKD---VARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 227 NEAAMGLISSFK--------NEEEAISGVNQKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLGGDTMLFKI-----S 293
Cdd:PRK09569  274 NQEVLGWIQQFQeklggeepTKEQVEQALWDTLNAGQVIPGYGHAVLRK-TDPRYTAQREFCLKHLPDDPLFKLvamifE 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 294 EAIEYLMKEKRPSLP-PNADFYSASAYHFMGIPTP-YFTPIFIMSRVSGWCAHIKEQRA-NNKLIRPSSEYIGPKpRSFV 370
Cdd:PRK09569  353 VAPGVLTEHGKTKNPwPNVDAQSGVIQWYYGVKEWdFYTVLFGVGRALGVMANITWDRGlGYAIERPKSVTTEML-EKWA 431

                  ....*
gi 1751924788 371 AIDKR 375
Cdd:PRK09569  432 AEGGR 436
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
11-359 3.11e-22

Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99857  Cd Length: 426  Bit Score: 97.37  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  11 GGLAGIIAGESAICTCGLGNGLNYYGYNIEDL------AQNAEF---EEIAFLLQYGELPKKDELKAYKEKIIKHRALSE 81
Cdd:cd06103    38 GGMRGMKGLVYETSVLDPDEGIRFRGKTIPECqellpkADGGGEplpEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  82 NLKAILRAIPKDTHPMNLMQTAVSALGAL----------ESEKDD-----FSDQDDKIIRllgvLPSV--LCYWHHYVNS 144
Cdd:cd06103   118 HVVKMIDNLPRNLHPMTQLSAAILALQSEskfakayaegKINKTTyweyvYEDAMDLIAK----LPVVaaKIYRRKYRKG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 145 GKEIDFNSQQDsIAGYFLERLELKEPkaDFVKAMHCSLILYAEHEF-NASTFTARVCASTKSDIFSAVAAAIGALRGPLH 223
Cdd:cd06103   194 GEIGAIDSKLD-WSANFAHMLGYEDE--EFTDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLH 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 224 GGANEAAMGLISSFKNE-------EEAISGVNQKLENKELLMGFGHRVYGLgGDPRNALIKVWSKRLGGDTMLFKISEAI 296
Cdd:cd06103   271 GLANQEVLKWLLKMQKElgkdvsdEELEKYIWDTLNSGRVVPGYGHAVLRK-TDPRFTCQREFALKHLPDDPLFKLVAQC 349
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751924788 297 -----EYLMKEKRPSLP-PNADFYSASAYHFMGIPTP-YFTPIFIMSRVSGWCAHIKEQRANNKLI-RPSS 359
Cdd:cd06103   350 ykiipGVLKEHGKVKNPyPNVDAHSGVLLQHYGMTEPqYYTVLFGVSRALGVLAQLVWSRALGLPIeRPKS 420
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
182-357 7.86e-20

Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.


Pssm-ID: 99854 [Multi-domain]  Cd Length: 227  Bit Score: 87.24  E-value: 7.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 182 LILYAEH-EFNASTFTARVCAST-KSDIFSAVAAAIGALrGPLHGGANEAAMGLISSFK-----NEEEAISGVNQKLENK 254
Cdd:cd06100    38 LVALADHgPATPSAHAARLTASAgPEDLQSAVAAGLLGI-GDRFGGAGEGAARLFKEAVdsgdaLDAAAAEFVAEYRAAK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 255 ELLMGFGHRVYgLGGDPRNALIKVWSKRLGGDTMLFKISEAIE-YLMKEKRPSLPPNADFYSASAYHFMGIPTPYFTPIF 333
Cdd:cd06100   117 KRIPGFGHPVH-KNPDPRVPRLLELARELGPAGPHLDYALAVEkALTAAKGKPLPLNVDGAIAAILLDLGFPPGALRGLF 195
                         170       180
                  ....*....|....*....|....
gi 1751924788 334 IMSRVSGWCAHIKEQRANNKLIRP 357
Cdd:cd06100   196 VLGRSPGLIAHALEEKRLGQPLYR 219
PRK06224 PRK06224
citryl-CoA lyase;
182-369 1.13e-19

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 87.62  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 182 LILYAEHEFNASTFTARVCASTKSDIFSAVAAAIGALrGPLHGGANEAAMGLISSFKN--------EEEAISGVNQKLEN 253
Cdd:PRK06224   62 LVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIAAaadagadlDAAARAIVAEYRAA 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 254 KELLMGFGHRVYgLGGDPRNALIKVWSKRLGGDTMLFKISEAIE-YLMKEKRPSLPPNADFYSASAYHFMGIPTPYFTPI 332
Cdd:PRK06224  141 GKRVPGFGHPLH-KPVDPRAPRLLALAREAGVAGRHCRLAEALEaALAAAKGKPLPLNVDGAIAAILADLGFPPALARGL 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1751924788 333 FIMSRVSGWCAHIKEQRANNKLIR------PSSEYIGPKPRSF 369
Cdd:PRK06224  220 FVISRAAGLVAHVWEELQQPIGFRiwdpaeEAVEYTGPPPREL 262
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
31-340 5.74e-18

Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99859  Cd Length: 428  Bit Score: 84.86  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  31 GLNYYGYNIEDlAQN--------AEF--EEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLM 100
Cdd:cd06106    58 GIRFHGKTIPE-CQKelpkapigGEMlpESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 101 QTAVSAL--------------GALESEKDDFSDQDDKIIRLLGVLPSVlcywhhYVNSGKEID----FNSQQDsIAGYFL 162
Cdd:cd06106   137 SIGVAALnhdskfaaayekgiKKTEYWEPTLEDSLNLIARLPALAARI------YRNVYGEGHglgkIDPEVD-WSYNFT 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 163 ERLElKEPKADFVKAMHCSLILYAEHE-FNASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLI------- 234
Cdd:cd06106   210 SMLG-YGDNLDFVDLLRLYIALHGDHEgGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWIlemqkni 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 235 SSFKNEEEAISGVNQKLENKELLMGFGHRVYgLGGDPR-NALIKVWSKR--LGGD---TMLFKISEAIEYLMKE----KR 304
Cdd:cd06106   289 GSKATDQDIRDYLWKTLKSGRVVPGYGHAVL-RKPDPRfTALMEFAQTRpeLENDpvvQLVQKLSEIAPGVLTEhgktKN 367
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1751924788 305 PSlpPNADFYSASAYHFMGIPTP-YFTPIFIMSRVSG 340
Cdd:cd06106   368 PF--PNVDAASGVLFYHYGIREFlYYTVIFGVSRALG 402
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
49-359 1.19e-14

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99858  Cd Length: 427  Bit Score: 74.71  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788  49 EEIAFLLQYGELPKKDELKAYKEKIIKHRALSENLKAILRAIPKDTHPMNLMQTAVSALGAlESE----------KDD-- 116
Cdd:cd06105    85 EGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNS-ESKfakayaegihKSKyw 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 117 ---FSDQDDkiirLLGVLPSVLCYWHHYV-NSGKEIDFNSQQDsIAGYFLERLELKEPkaDFVKAMHCSLILYAEHEF-N 191
Cdd:cd06105   164 eyvYEDSMD----LIAKLPCVAAKIYRNLyRGGKIIAIDSNLD-WSANFANMLGYTDP--QFTELMRLYLTIHSDHEGgN 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 192 ASTFTARVCASTKSDIFSAVAAAIGALRGPLHGGANEAAMGLISSFKNE------EEAISG-VNQKLENKELLMGFGHRV 264
Cdd:cd06105   237 VSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEvgkdvsDEQLREyVWKTLNSGRVVPGYGHAV 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751924788 265 YgLGGDPRN------ALikvwsKRLGGDTM------LFKISEAIeyLMKEKRPSLP-PNADFYSASAYHFMGI-PTPYFT 330
Cdd:cd06105   317 L-RKTDPRYtcqrefAL-----KHLPNDPLfklvsqLYKIVPPV--LTEQGKAKNPwPNVDAHSGVLLQYYGLtEMNYYT 388
                         330       340       350
                  ....*....|....*....|....*....|
gi 1751924788 331 PIFIMSRVSGWCAHIKEQRANNKLI-RPSS 359
Cdd:cd06105   389 VLFGVSRALGVLSQLIWDRALGLPLeRPKS 418
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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