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Conserved domains on  [gi|70887268|gb|EAO00028|]
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citrate synthase, putative [Trypanosoma cruzi]

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 ...
28-465 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 cd06103:

Pssm-ID: 469765  Cd Length: 426  Bit Score: 694.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  28 LKAAVMARHEADAPKMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKsWKGG 107
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPK-ADGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 108 TSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRAdnEAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGK 187
Cdd:cd06103  80 GEPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRA--EVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 188 AIKSNFWEYALEDSLDIIARTPYLAAAIYNRlTTGRAAVLNPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEG 267
Cdd:cd06103 158 INKTTYWEYVYEDAMDLIAKLPVVAAKIYRR-KYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 268 GNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRdkcKAAGVNMKDRKelaagLEKLTWERLNAK 347
Cdd:cd06103 237 GNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQ---KELGKDVSDEE-----LEKYIWDTLNSG 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 348 RVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNF 427
Cdd:cd06103 309 RVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQY 388
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 70887268 428 YTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:cd06103 389 YTVLFGVSRALGVLAQLVWSRALGLPIERPKSMSTEGL 426
 
Name Accession Description Interval E-value
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
28-465 0e+00

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: 694.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  28 LKAAVMARHEADAPKMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKsWKGG 107
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPK-ADGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 108 TSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRAdnEAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGK 187
Cdd:cd06103  80 GEPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRA--EVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 188 AIKSNFWEYALEDSLDIIARTPYLAAAIYNRlTTGRAAVLNPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEG 267
Cdd:cd06103 158 INKTTYWEYVYEDAMDLIAKLPVVAAKIYRR-KYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 268 GNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRdkcKAAGVNMKDRKelaagLEKLTWERLNAK 347
Cdd:cd06103 237 GNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQ---KELGKDVSDEE-----LEKYIWDTLNSG 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 348 RVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNF 427
Cdd:cd06103 309 RVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQY 388
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 70887268 428 YTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:cd06103 389 YTVLFGVSRALGVLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
42-465 0e+00

citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal forms of citrate synthase. Citrate synthase is the entry point to the TCA cycle from acetyl-CoA. Peroxisomal forms, such as SP:P08679 from yeast (recognized by the C-terminal targeting motif SKL) act in the glyoxylate cycle. Eukaryotic homologs excluded by the high trusted cutoff of this model include a Tetrahymena thermophila citrate synthase that doubles as a filament protein, a putative citrate synthase from Plasmodium falciparum (no TCA cycle), and a methylcitrate synthase from Aspergillus nidulans.


Pssm-ID: 130853  Cd Length: 427  Bit Score: 532.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268    42 KMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwKGGTSPLPEGMLWLLMT 121
Cdd:TIGR01793  18 KVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKA-KGGEEPLPEGLLWLLLT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   122 GSIPTDKQVKELHVELHRRADneAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGKAiKSNFWEYALEDS 201
Cdd:TIGR01793  97 GKVPSEEQVDALSAEWRARAD--LPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIH-KTKYWEYTYEDS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   202 LDIIARTPYLAAAIYNRL-TTGRAAvlnPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEGGNVSAHATTLVAS 280
Cdd:TIGR01793 174 MDLIAKLPTVAAYIYRNMyKDGQSI---SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNVSAHTGHLVGS 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   281 ALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCkaaGVNMKDRKelaagLEKLTWERLNAKRVIPGYGHAVLRI 360
Cdd:TIGR01793 251 ALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSEC---GENVTKEQ-----LKDYIWKTLNSGKVVPGYGHAVLRK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   361 PDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNFYTVLFGISRQLGA 440
Cdd:TIGR01793 323 TDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGI 402
                         410       420
                  ....*....|....*....|....*
gi 70887268   441 LTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:TIGR01793 403 LSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
28-467 1.82e-180

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 511.99  E-value: 1.82e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   28 LKAAVMARHEADAPKMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwKGG 107
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKA-PGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  108 TSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRAdnEAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGK 187
Cdd:PRK09569  82 EYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQ--NVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  188 AIKSNFWEYALEDSLDIIARTPYLAAAIYNRltTGRAAVLNPANPDLDWAANFTNMLGyQDEKFWDCMRLYLSLHADHEG 267
Cdd:PRK09569 160 FNKMDAWEYMYEDASDLVARIPVIAAYIYNL--KYKGDKQIPSDPELDYGANFAHMIG-QPKPYKDVARMYFILHSDHES 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  268 GNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKckaagvnMKDRKELAAGLEKLTWERLNAK 347
Cdd:PRK09569 237 GNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEK-------LGGEEPTKEQVEQALWDTLNAG 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  348 RVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNF 427
Cdd:PRK09569 310 QVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDF 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 70887268  428 YTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDALFK 467
Cdd:PRK09569 390 YTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLEK 429
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
66-458 3.22e-108

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: 324.84  E-value: 3.22e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268    66 GMRGITGLIYESSMLDKEQG-ICFRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVEL-HRRADN 143
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEELAER---------SSFEE-VAYLLLTGELPTKEELEEFSAELaAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   144 EAITAAtktIASLPENTHPMTQLSTGVLALQAFSKFAPAyasgkaIKSNFWEYALEDSLdiIARTPYLAAAIYnRLTTGR 223
Cdd:pfam00285  71 EDVLEL---LRALPRDAHPMAVLRAAVSALAAFDPEAIS------DKADYWENALRDDL--IAKLPTIAAYIY-RHRRGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   224 AAVlnPANPDLDWAANFTNML-GYQ-DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLH 301
Cdd:pfam00285 139 PPI--YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   302 GLANQESLSYLFEMRDkckaagvnmkdrkelAAGLEKLTWERLN-AKRVIPGYGHAVLRIPDPRYMCLREYCLKHFP--- 377
Cdd:pfam00285 216 GGANEAVLEMLEEIGS---------------PDEVEEYIRKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEegg 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   378 DDELFFLVDTIYSIMPDILKKHGktKNPFPNVDAHSGMLLQHFGLTEqNFYTVLFGISRQLGALTGVVWDRLQGRpIERP 457
Cdd:pfam00285 281 DDPLLELAEELEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADNR-IIRP 356

                  .
gi 70887268   458 K 458
Cdd:pfam00285 357 R 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
78-460 2.04e-80

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: 254.63  E-value: 2.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  78 SMLDKEQGIC-FRGMTIPECCEKipkswkggtsPLPEGMLWLLMTGSIPTDKQVKELHVEL-HRRADNEAITaatKTIAS 155
Cdd:COG0372  28 SYIDGEKGILrYRGYPIEDLAEK----------SSFEEVAYLLLYGELPTKEELAEFKAELaRHRELPEEVK---EFLDG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 156 LPENTHPMTQLSTGVLALQAFskfapaYASGKAIKsnfWEYALEDSLDIIARTPYLAAAIYnRLTTGRAAVlnPANPDLD 235
Cdd:COG0372  95 FPRDAHPMDVLRTAVSALGAF------DPDADDID---PEARLEKAIRLIAKLPTIAAYAY-RYRRGLPPV--YPDPDLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 236 WAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLF 313
Cdd:COG0372 163 YAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 314 EMRDKckaagvnmkdrKELAAGLEKltweRLNAKRVIPGYGHAVLRIPDPRYMCLREYC---LKHFPDDELFFLVDTIYS 390
Cdd:COG0372 242 EIGSP-----------DNVEEYIRK----ALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEE 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 391 IMPDilKKHGKTKNPFPNVDAHSGMLLQHFGLTEqNFYTVLFGISRQLGALTGVVWDRLQGRpIERPKSI 460
Cdd:COG0372 307 VALE--DEYFIEKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRADNR-IIRPRQI 372
 
Name Accession Description Interval E-value
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
28-465 0e+00

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: 694.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  28 LKAAVMARHEADAPKMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKsWKGG 107
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPK-ADGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 108 TSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRAdnEAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGK 187
Cdd:cd06103  80 GEPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRA--EVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 188 AIKSNFWEYALEDSLDIIARTPYLAAAIYNRlTTGRAAVLNPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEG 267
Cdd:cd06103 158 INKTTYWEYVYEDAMDLIAKLPVVAAKIYRR-KYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 268 GNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRdkcKAAGVNMKDRKelaagLEKLTWERLNAK 347
Cdd:cd06103 237 GNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQ---KELGKDVSDEE-----LEKYIWDTLNSG 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 348 RVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNF 427
Cdd:cd06103 309 RVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQY 388
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 70887268 428 YTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:cd06103 389 YTVLFGVSRALGVLAQLVWSRALGLPIERPKSMSTEGL 426
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
42-468 0e+00

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: 613.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  42 KMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwKGGTSPLPEGMLWLLMT 121
Cdd:cd06105  15 RIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKA-PGGEEPLPEGLFWLLLT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 122 GSIPTDKQVKELHVELHRRADneAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGKAiKSNFWEYALEDS 201
Cdd:cd06105  94 GEVPTKEQVSALSKEWAARAA--LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIH-KSKYWEYVYEDS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 202 LDIIARTPYLAAAIYNRLTtgRAAVLNPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEGGNVSAHATTLVASA 281
Cdd:cd06105 171 MDLIAKLPCVAAKIYRNLY--RGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSA 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 282 LSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCkaaGVNMKDRKelaagLEKLTWERLNAKRVIPGYGHAVLRIP 361
Cdd:cd06105 249 LSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEV---GKDVSDEQ-----LREYVWKTLNSGRVVPGYGHAVLRKT 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 362 DPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNFYTVLFGISRQLGAL 441
Cdd:cd06105 321 DPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVL 400
                       410       420
                ....*....|....*....|....*..
gi 70887268 442 TGVVWDRLQGRPIERPKSITSDALFKK 468
Cdd:cd06105 401 SQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
42-465 0e+00

citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal forms of citrate synthase. Citrate synthase is the entry point to the TCA cycle from acetyl-CoA. Peroxisomal forms, such as SP:P08679 from yeast (recognized by the C-terminal targeting motif SKL) act in the glyoxylate cycle. Eukaryotic homologs excluded by the high trusted cutoff of this model include a Tetrahymena thermophila citrate synthase that doubles as a filament protein, a putative citrate synthase from Plasmodium falciparum (no TCA cycle), and a methylcitrate synthase from Aspergillus nidulans.


Pssm-ID: 130853  Cd Length: 427  Bit Score: 532.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268    42 KMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwKGGTSPLPEGMLWLLMT 121
Cdd:TIGR01793  18 KVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKA-KGGEEPLPEGLLWLLLT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   122 GSIPTDKQVKELHVELHRRADneAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGKAiKSNFWEYALEDS 201
Cdd:TIGR01793  97 GKVPSEEQVDALSAEWRARAD--LPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIH-KTKYWEYTYEDS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   202 LDIIARTPYLAAAIYNRL-TTGRAAvlnPANPDLDWAANFTNMLGYQDEKFWDCMRLYLSLHADHEGGNVSAHATTLVAS 280
Cdd:TIGR01793 174 MDLIAKLPTVAAYIYRNMyKDGQSI---SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNVSAHTGHLVGS 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   281 ALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCkaaGVNMKDRKelaagLEKLTWERLNAKRVIPGYGHAVLRI 360
Cdd:TIGR01793 251 ALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSEC---GENVTKEQ-----LKDYIWKTLNSGKVVPGYGHAVLRK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   361 PDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNFYTVLFGISRQLGA 440
Cdd:TIGR01793 323 TDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGI 402
                         410       420
                  ....*....|....*....|....*
gi 70887268   441 LTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:TIGR01793 403 LSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
28-467 1.82e-180

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 511.99  E-value: 1.82e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   28 LKAAVMARHEADAPKMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwKGG 107
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKA-PGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  108 TSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRAdnEAITAATKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGK 187
Cdd:PRK09569  82 EYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQ--NVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  188 AIKSNFWEYALEDSLDIIARTPYLAAAIYNRltTGRAAVLNPANPDLDWAANFTNMLGyQDEKFWDCMRLYLSLHADHEG 267
Cdd:PRK09569 160 FNKMDAWEYMYEDASDLVARIPVIAAYIYNL--KYKGDKQIPSDPELDYGANFAHMIG-QPKPYKDVARMYFILHSDHES 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  268 GNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKckaagvnMKDRKELAAGLEKLTWERLNAK 347
Cdd:PRK09569 237 GNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEK-------LGGEEPTKEQVEQALWDTLNAG 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  348 RVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNF 427
Cdd:PRK09569 310 QVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDF 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 70887268  428 YTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDALFK 467
Cdd:PRK09569 390 YTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLEK 429
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
26-465 1.24e-173

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: 494.33  E-value: 1.24e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  26 DELKAAVMARHEAdapkMKILKEKYKNEKLSDATIDAAYGGMRGITGLIYESSMLDKEQGICFRGMTIPECCEKIPKSwK 105
Cdd:cd06106   3 EALKEVIPAKREQ----LKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKA-P 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 106 GGTSPLPEGMLWLLMTGSIPTDKQVKELHVELHRRADNEAITaaTKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYAS 185
Cdd:cd06106  78 IGGEMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYI--EKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 186 GKAiKSNFWEYALEDSLDIIARTPYLAAAIYnRLTTGRAAVLNPANPDLDWAANFTNMLGYQDEK-FWDCMRLYLSLHAD 264
Cdd:cd06106 156 GIK-KTEYWEPTLEDSLNLIARLPALAARIY-RNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 265 HEGGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCKAAGVNMKDRKELaaglekltWERL 344
Cdd:cd06106 234 HEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYL--------WKTL 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 345 NAKRVIPGYGHAVLRIPDPRYMCLREYCLKH--FPDDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGL 422
Cdd:cd06106 306 KSGRVVPGYGHAVLRKPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGI 385
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 70887268 423 TEQNFYTVLFGISRQLGALTGVVWDRLQGRPIERPKSITSDAL 465
Cdd:cd06106 386 REFLYYTVIFGVSRALGPLTQLVWDRILGLPIERPKSLSLEGL 428
PLN02456 PLN02456
citrate synthase
5-469 2.98e-138

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 405.18  E-value: 2.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268    5 CARAGILLNAPSAARRHLTIVD-----ELKAAVMARHEADAPKMKILKEKYKNEKLsdATIDaayGGMRGITGLIYESSM 79
Cdd:PLN02456   6 CTSSSLSRAAPGGGSGSLTIVDnrtgkDYESPLSELGPVQAERLKKIKAGKDDLGL--KTVD---PGYRNTAPVLSEISL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   80 LDKEQGIC-FRGMTIPECCEKIPKswkggtsplpEGMLWLLMTGSIPTDKQVKELHVELHRRAD-NEAITAAtktIASLP 157
Cdd:PLN02456  81 IDGDEGILrFRGYPIEELAEKSPF----------EEVAYLLLYGNLPTKEQLADWEAELRQHSAvPEHVLDV---IDALP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  158 ENTHPMTQLSTGVLALQAFSKFAPAYASGKAiKSNFWEYALEDSLDIIARTPYLAAAIYNRlTTGRAAVLnpANPDLDWA 237
Cdd:PLN02456 148 HDAHPMTQLVSGVMALSTFSPDANAYLRGQH-KYKSWEVRDEDIVRLIGKLPTLAAAIYRR-MYGRGPVI--PDNSLDYA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  238 ANFTNMLGYQ-------DEKFWDCMRLYLSLHADHEGGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLS 310
Cdd:PLN02456 224 ENFLYMLGSLgdrsykpDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLK 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  311 YLFEmrdkckaagVNMKDRkelaagLEKLTWERLNAKRVIPGYGHAVLRIPDPRYMCLREYCL---KHFPDDELFFLVDT 387
Cdd:PLN02456 304 MLKE---------IGTVEN------IPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASA 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  388 IYSIMpdILKKHGKTKNPFPNVDAHSGMLLQHFGLTeQNFYTVLFGISRQLGALTGvvWDRLQGRPIER---PKSITSDA 464
Cdd:PLN02456 369 LEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFP-EEFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTGE 443

                 ....*
gi 70887268  465 LFKKF 469
Cdd:PLN02456 444 WLRHY 448
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
66-458 3.22e-108

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: 324.84  E-value: 3.22e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268    66 GMRGITGLIYESSMLDKEQG-ICFRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVEL-HRRADN 143
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEELAER---------SSFEE-VAYLLLTGELPTKEELEEFSAELaAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   144 EAITAAtktIASLPENTHPMTQLSTGVLALQAFSKFAPAyasgkaIKSNFWEYALEDSLdiIARTPYLAAAIYnRLTTGR 223
Cdd:pfam00285  71 EDVLEL---LRALPRDAHPMAVLRAAVSALAAFDPEAIS------DKADYWENALRDDL--IAKLPTIAAYIY-RHRRGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   224 AAVlnPANPDLDWAANFTNML-GYQ-DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLH 301
Cdd:pfam00285 139 PPI--YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   302 GLANQESLSYLFEMRDkckaagvnmkdrkelAAGLEKLTWERLN-AKRVIPGYGHAVLRIPDPRYMCLREYCLKHFP--- 377
Cdd:pfam00285 216 GGANEAVLEMLEEIGS---------------PDEVEEYIRKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEegg 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   378 DDELFFLVDTIYSIMPDILKKHGktKNPFPNVDAHSGMLLQHFGLTEqNFYTVLFGISRQLGALTGVVWDRLQGRpIERP 457
Cdd:pfam00285 281 DDPLLELAEELEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADNR-IIRP 356

                  .
gi 70887268   458 K 458
Cdd:pfam00285 357 R 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
65-460 3.22e-97

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: 296.82  E-value: 3.22e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  65 GGMRGITGLIYESSMLDKEQGIC-FRGMTIPECCEKipkswkggtsPLPEGMLWLLMTGSIPTDKQVKELHVEL--HRRA 141
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGILrYRGYDIEELAEK----------SSFEEVAYLLLYGKLPTKEELAEFKKKLasHRAL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 142 DNEAITAatktIASLPENTHPMTQLSTGVLALQAFSKFApayasgkaiKSNFWEYALEDSLDIIARTPYLAAAIYnRLTT 221
Cdd:cd06118  71 PEHVVEI----LDLLPKNAHPMDVLRTAVSALGSFDPFA---------RDKSPEARYEKAIRLIAKLPTIAANIY-RNRE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 222 GRAAVlnPANPDLDWAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGP 299
Cdd:cd06118 137 GLEII--APDPDLSYAENFLYMLFGEepDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGP 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 300 LHGLANQESLSYLFEMRDKCKAagvnmkdrkelaaglEKLTWERLNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFP-- 377
Cdd:cd06118 214 LHGGANEAVLKMLLEIGTPENV---------------EAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEek 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 378 -DDELFFLVDTIYSIMPDILKKhgktKNPFPNVDAHSGMLLQHFGLtEQNFYTVLFGISRQLGALTGVVWDRLQGRPIER 456
Cdd:cd06118 279 gDDKLFEIAEELEEIALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIR 353

                ....
gi 70887268 457 PKSI 460
Cdd:cd06118 354 PRAE 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
78-460 2.04e-80

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: 254.63  E-value: 2.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  78 SMLDKEQGIC-FRGMTIPECCEKipkswkggtsPLPEGMLWLLMTGSIPTDKQVKELHVEL-HRRADNEAITaatKTIAS 155
Cdd:COG0372  28 SYIDGEKGILrYRGYPIEDLAEK----------SSFEEVAYLLLYGELPTKEELAEFKAELaRHRELPEEVK---EFLDG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 156 LPENTHPMTQLSTGVLALQAFskfapaYASGKAIKsnfWEYALEDSLDIIARTPYLAAAIYnRLTTGRAAVlnPANPDLD 235
Cdd:COG0372  95 FPRDAHPMDVLRTAVSALGAF------DPDADDID---PEARLEKAIRLIAKLPTIAAYAY-RYRRGLPPV--YPDPDLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 236 WAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLF 313
Cdd:COG0372 163 YAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 314 EMRDKckaagvnmkdrKELAAGLEKltweRLNAKRVIPGYGHAVLRIPDPRYMCLREYC---LKHFPDDELFFLVDTIYS 390
Cdd:COG0372 242 EIGSP-----------DNVEEYIRK----ALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEE 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 391 IMPDilKKHGKTKNPFPNVDAHSGMLLQHFGLTEqNFYTVLFGISRQLGALTGVVWDRLQGRpIERPKSI 460
Cdd:COG0372 307 VALE--DEYFIEKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRADNR-IIRPRQI 372
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
235-459 6.32e-65

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: 208.35  E-value: 6.32e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 235 DWAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYL 312
Cdd:cd06099   1 SYAENFLYMLGGEepDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 313 FEMrdkckaaGVNMKDRkelaagLEKLTWERLNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFP---DDELFFLVDTIY 389
Cdd:cd06099  80 EEI-------GTPKNEP------AEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKedgDDPMFELAAELE 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 390 SIMPDILKKhgktKNPFPNVDAHSGMLLQHFGLTeQNFYTVLFGISRQLGALTGVVWDRLQGRPIERPKS 459
Cdd:cd06099 147 KIAEEVLYE----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRS 211
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
235-460 2.98e-64

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: 208.71  E-value: 2.98e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 235 DWAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYL 312
Cdd:cd06101  53 SYAENFLYMLGGEepDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKML 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 313 FEMrdkckaagvnmkdRKELAAGLEKLTWERLNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFP---DDELFFLVDTIY 389
Cdd:cd06101 132 EEI-------------GTPKNEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKekgLDPMFELAAELE 198
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887268 390 SIMPDILKKhgktKNPFPNVDAHSGMLLQHFGLTeQNFYTVLFGISRQLGALTGVVWDRLQGRPIERPKSI 460
Cdd:cd06101 199 KIAPEVLYE----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAE 264
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
66-469 6.30e-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.


Pssm-ID: 99865  Cd Length: 373  Bit Score: 150.27  E-value: 6.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  66 GMRGITGLIYESSMLDKEQGIC-FRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVEL--HRRAD 142
Cdd:cd06112   4 GLAGVPAAESSISYIDGKNGILeYRGYDIEELAEY---------SSFEE-VALLLLDGDLPTAAELEEFDKELrqHRRVK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 143 NEAITaatkTIASLPENTHPMTQLSTGVLALQAFskfapaYASGKAIKSNfWEYALEDSLDIIARTPYLAAAiYNRLTTG 222
Cdd:cd06112  74 YNIRD----MMKCFPETGHPMDMLQATVAALGMF------YPKPEVLKPN-PDYIDAATVKLIAKMPTLVAM-WARIRNG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 223 RAAVlnPANPDLDWAANFTNML-GYQDEKFW-DCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPL 300
Cdd:cd06112 142 DDPI--EPRPDLDYAENFLYMLfGEEPDPATaKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 301 HGLANQESLSYLFEmrdkckaagvnMKDRKELAAGLEKltweRLNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDE 380
Cdd:cd06112 219 HGGANEDVLEMLEE-----------IGSPENVKAYLDK----KLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMG 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 381 LFflvDTIYSIMPDILKKHGKT---KNPFPNVDAHSGMLLQHFGLtEQNFYTVLFGISRQLGALTGvvW-DRLQGRPIER 456
Cdd:cd06112 284 EL---SKLYEIALEVERLCEELlghKGVYPNVDFYSGIVYKELGI-PADLFTPIFAVARVAGWLAH--WkEQLGDNRIFR 357
                       410
                ....*....|...
gi 70887268 457 PKSITSDALFKKF 469
Cdd:cd06112 358 PTQIYIGEIDRKY 370
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
78-460 3.04e-36

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: 137.57  E-value: 3.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  78 SMLDKEQGIC-FRGMTIPECCEKipKSWkggtsplpEGMLWLLMTGSIPTDKQVKELHvelhRRADNEAIT--AATKTIA 154
Cdd:cd06107  20 TYIDGDKGILlYRGYPIEQLAES--STY--------EEVAYLLLWGELPTQEQYDEFQ----RRLSEHMMVpeSVHRLIQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 155 SLPENTHPMTQLSTGVLALQAFSKFAPAYASGKAIKSNFwEYALEDSLDIIARTPYLAAAIYNRlTTGRAavLNPANPDL 234
Cdd:cd06107  86 TFPRDAHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNP-EVRDKQIIRTLAKMPTIAAAAYCH-RIGRP--FVYPRANL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 235 DWAANFTNMLGYQD-------EKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQE 307
Cdd:cd06107 162 SYIENFLYMMGYVDqepyepnPRLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 308 SLSYLFEMRDKckaagvnmkdrKELAAGLEKLTwerlNAKRVIPGYGHAVLRIPDPRYMCLREYC---LKHFPDDELF-- 382
Cdd:cd06107 241 ALKMLREIGTP-----------ENVPAFIERVK----NGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLkv 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 383 -FLVDTIYSIMPDILKkhgktKNPFPNVDAHSGMLLQHFGLtEQNFYTVLFGISRQLGALTGvvWDRLQGRP---IERPK 458
Cdd:cd06107 306 aMELERIALEDEYFVS-----RKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPlqrIWRPR 377

                ..
gi 70887268 459 SI 460
Cdd:cd06107 378 QV 379
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
113-439 3.72e-36

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: 137.78  E-value: 3.72e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 113 EGMLWLLMTGSIPTDKQVKELHVEL-HRRA------DNEAITAATKTIaslpenthpMTQLSTGVLALqafskfapaYAS 185
Cdd:cd06113  61 EETAYLLLFGYLPNKEELEEFCEILsSYRTlpdnfvEDVILKAPSKDI---------MNKLQRSVLAL---------YSY 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 186 GKAIKSNFWEYALEDSLDIIARTPYLAAAIYN---RLTTGRAAVLNPANPDLDWAANFTNMLgYQDEKF--WDCMRL--Y 258
Cdd:cd06113 123 DDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrHYYDGESLYIHHPQPELSTAENILSML-RPDKKYteLEAKLLdlC 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 259 LSLHADHEGGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQEslsyLFEMRDKCKAAGVNMKDRKELAAGLEK 338
Cdd:cd06113 202 LVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIK----VMEMLEDIKENVKDWTDEDEVRAYLRK 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 339 -LTWERLNAKRVIPGYGHAVLRIPDPRYMCLREYCL-----KHFpdDELFFLVDTIYSIMPDILKKH-GKTKNPFPNVDA 411
Cdd:cd06113 278 iLNKEAFDKSGLIYGMGHAVYTLSDPRAVVLKKYARslakeKGR--EEEFALYERIERLAPEVIAEErGIGKTVCANVDF 355
                       330       340
                ....*....|....*....|....*...
gi 70887268 412 HSGMLLQHFGLTeQNFYTVLFGISRQLG 439
Cdd:cd06113 356 YSGFVYKMLGIP-QELYTPLFAVARIVG 382
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
76-460 7.44e-33

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: 128.85  E-value: 7.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  76 ESSM--LDKEQGIC-FRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVELHRRAD-NEAITaatK 151
Cdd:cd06114  38 ESAItyIDGEKGILrYRGYPIEQLAEK---------SSFLE-VCYLLLYGELPTAEQLQEFREEITRHTLvHEQMK---R 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 152 TIASLPENTHPMTQLSTGVLALQAFSKfapayasgKAIKSNFWEYALEDSLDIIARTPYLAAAIYnRLTTGRAAVLnpAN 231
Cdd:cd06114 105 FFNGFPRDAHPMAILSAMVNALSAFYP--------DSLDVNDPEQRELAAIRLIAKVPTIAAMAY-RYSIGQPFIY--PD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 232 PDLDWAANFTNML------GYQ-DEKFWDCMRLYLSLHADHEgGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLA 304
Cdd:cd06114 174 NDLSYVENFLHMMfavpyePYEvDPVVVKALDTILILHADHE-QNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGA 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 305 NQESLSYLFEMRDkckaagvNMKDRKELAAGLEKLTWERLNakrvipGYGHAVLRIPDPRYMCLREYC---LKHFP-DDE 380
Cdd:cd06114 253 NEAVLEMLEEIGS-------VGNVDKYIAKAKDKNDPFRLM------GFGHRVYKNYDPRAKILKKTCdevLAELGkDDP 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 381 LFflvdtiysimpDILKKHGKT---------KNPFPNVDAHSGMLLQHFGLTEqNFYTVLFGISRqlgaLTGVV--WDRL 449
Cdd:cd06114 320 LL-----------EIAMELEEIalkddyfieRKLYPNVDFYSGIILRALGIPT-EMFTVLFALGR----TPGWIaqWREM 383
                       410
                ....*....|....
gi 70887268 450 QGRP---IERPKSI 460
Cdd:cd06114 384 HEDPelkIGRPRQL 397
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
66-439 9.00e-33

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: 127.39  E-value: 9.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  66 GMRGITGLIYESSMLDKEQGI-CFRGMTIPECCEKipKSWkggtsplpEGMLWLLMTGSIPTDKQVKELHVEL--HRRAD 142
Cdd:cd06110   2 GLEGVIAADSKISYIDGDAGIlIYRGYDIHDLAEN--STF--------EEVAYLLWNGELPTAEELDAFKAQLaaERELP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 143 NEAITAatktIASLPENTHPMTQLSTGVLALQAFSKFAPAyasgkaiksNFWEYALEDSLDIIARTPYLAAAiYNRLTTG 222
Cdd:cd06110  72 AEIIDL----LKLLPKDAHPMDVLRTAVSALALYDPEADD---------MSREANLRKAIRLIAKMPTIVAA-FHRIRNG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 223 RAAVlnPANPDLDWAANFTNMLGYQ--DEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPL 300
Cdd:cd06110 138 LEPV--APDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPL 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 301 HGLANQESLSYLFEMrdkckaagvnmKDRKELAAGLEKltweRLNAKRVIPGYGHAVLRIPDPRYMCLREYCL---KHFP 377
Cdd:cd06110 215 HGGANERVMKMLLEI-----------GSVDNVAAYVKD----KLANKEKIMGFGHRVYKTGDPRAKHLREMSRrlgKETG 279
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887268 378 DDELFFLVDTIYSIMPDIlkkhgktKNPFPNVDAHSGMLLQHFGLtEQNFYTVLFGISRQLG 439
Cdd:cd06110 280 EPKWYEMSEAIEQAMRDE-------KGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSG 333
PRK14032 PRK14032
citrate synthase; Provisional
113-439 2.68e-31

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 125.02  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  113 EGMLWLLMTGSIPTDKQVKELHVEL-HRRADNEAITAatKTIASLPENtHPMTQLSTGVLALQAFSKfapaYASGKAIKS 191
Cdd:PRK14032  91 EEVAYLLLFGELPTKEELAEFTELLgDYRELPDGFTR--DMILKAPSK-DIMNSLARSVLALYSYDD----NPDDTSIDN 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  192 NfweyaLEDSLDIIARTPYLAAAIYNRL---TTGRAAVLNPANPDLDWAANFTNMLgYQDEKFW----DCMRLYLSLHAD 264
Cdd:PRK14032 164 V-----LRQSISLIARFPTLAVYAYQAYrhyHDGKSLYIHPPKPELSTAENILYML-RPDNKYTeleaRLLDLALVLHAE 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  265 HEGGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCKaagvNMKDRKELAAGLEK-LTWER 343
Cdd:PRK14032 238 HGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVK----DWEDEDEIADYLTKiLNKEA 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  344 LNAKRVIPGYGHAVLRIPDPRYMCLREYCL-----KHFPDDelFFLVDTIYSIMPDILKKH-GKTKNPFPNVDAHSGMLL 417
Cdd:PRK14032 314 FDKSGLIYGMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNLYEKIEKLAPELIAEErGIYKGVSANVDFYSGFVY 391
                        330       340
                 ....*....|....*....|..
gi 70887268  418 QHFGLTEqNFYTVLFGISRQLG 439
Cdd:PRK14032 392 DMLGIPE-ELYTPLFAIARIVG 412
PRK14036 PRK14036
citrate synthase; Provisional
78-460 7.04e-30

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 120.06  E-value: 7.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   78 SMLDKEQGIC-FRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVEL--HRRadneaITAATKTI- 153
Cdd:PRK14036  19 SYVDGQKGILeYRGYPIEELAEK---------SSFLE-TAYLLIWGELPTAEELEEFEQEVrmHRR-----VKYRIRDMm 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  154 ASLPENTHPMTQLSTGVLALQAFskfapaYaSGKAIKSNfwEYALEDSLDIIARTPYLAAAiYNRLTTGRAAVlnPANPD 233
Cdd:PRK14036  84 KCFPETGHPMDALQASAAALGLF------Y-SRRALDDP--EYIRDAVVRLIAKIPTMVAA-FQLIRKGNDPI--QPRDD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  234 LDWAANFTNMLGYQDE-----KFWD-CmrlyLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQE 307
Cdd:PRK14036 152 LDYAANFLYMLTEREPdplaaRIFDrC----LILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANED 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  308 SLSYLFEmrdkckaagvnMKDRKELAAGLEkltwERLNAKRVIPGYGHAVLRIPDPRYMCLR---EYCLKHFPDDELFFL 384
Cdd:PRK14036 227 VLAMLEE-----------IGSVENVRPYLD----ERLANKQKIMGFGHREYKVKDPRATILQklaEELFARFGHDEYYEI 291
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70887268  385 VDTIYSIMPDILKKhgktKNPFPNVDAHSGMLLQHFGLTEQNFyTVLFGISRQLGALTGvvW-DRLQGRPIERPKSI 460
Cdd:PRK14036 292 ALELERVAEERLGP----KGIYPNVDFYSGLVYRKLGIPRDLF-TPIFAIARVAGWLAH--WrEQLGANRIFRPTQI 361
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
78-441 5.39e-29

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: 117.93  E-value: 5.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  78 SMLDKEQGIC-FRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVELHRRAdneAI-TAATKTIAS 155
Cdd:cd06115  40 SYIDGDKGILrYRGYPIEELAEK---------STFLE-VAYLLIYGNLPTKSQLSDWEFAVSQHT---AVpTGVLDMIKS 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 156 LPENTHPMTQLSTGVLALQAFSKFA-PAYASGKAIKSNfweyALEDS--LDIIARTPYLAAAIYnRLTTGRAAVLnPANp 232
Cdd:cd06115 107 FPHDAHPMGMLVSAISALSAFHPEAnPALAGQDIYKNK----QVRDKqiVRILGKAPTIAAAAY-RRRAGRPPNL-PSQ- 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 233 DLDWAANFTNML-GYQDEKFWDCMRLYLSL------HADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLAN 305
Cdd:cd06115 180 DLSYTENFLYMLdSLGERKYKPNPRLARALdilfilHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGAN 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 306 QESLSYLFEMRDkckaagvnMKDRKELAAGLEkltwerlNAKRVIPGYGHAVLRIPDPRYMCLREYClkhfpdDELFFLV 385
Cdd:cd06115 259 EAVLRMLAEIGT--------VENIPAFIEGVK-------NRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIV 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887268 386 --DTIYSIMPDILK-----KHGKTKNPFPNVDAHSGMLLQHFGLTEQnFYTVLFGISRQLGAL 441
Cdd:cd06115 318 gkDPLIEIAVALEKaalsdEYFVKRKLYPNVDFYSGLIYRAMGFPTD-FFPVLFAIPRMAGYL 379
PRK14035 PRK14035
citrate synthase; Provisional
113-459 3.10e-27

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 112.16  E-value: 3.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  113 EGMLWLLMTGSIPTDKQVKELHVELHrraDNEAITAATKT---IASLPeNTHPMTQLSTGVLALQAFSKFApayasgkai 189
Cdd:PRK14035  42 EEVIFLLWNYRLPTEEELAHLKGKLR---KYMTLNDRVYQhfeEYSTD-HVHPMTALRTSVSYLAHFDPDA--------- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  190 KSNFWEYALEDSLDIIARTPYLAAAiYNRLTTGRAAVlnPANPDLDWAANFTNMLGYQD--EKFWDCMRLYLSLHADHEG 267
Cdd:PRK14035 109 EEESDEARYERAIRIQAKVASLVTA-FARVRQGKEPL--KPRPDLSYAANFLYMLRGELptDIEVEAFNKALVLHADHEL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  268 gNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKckaagvnmkdrKELAAGLEkltwERLNAK 347
Cdd:PRK14035 186 -NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSI-----------GDVDAYLD----EKFANK 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  348 RVIPGYGHAVLRIPDPRYMCLREYCLK---HFPDDELFFLVDTIYSIMPDilkkhgkTKNPFPNVDAHSGMLLQHFGLtE 424
Cdd:PRK14035 250 EKIMGFGHRVYKDGDPRAKYLREMSRKitkGTGREELFEMSVKIEKRMKE-------EKGLIPNVDFYSATVYHVMGI-P 321
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 70887268  425 QNFYTVLFGISRQLGALTGVVWDRLQGRpIERPKS 459
Cdd:PRK14035 322 HDLFTPIFAVSRVAGWIAHILEQYKDNR-IMRPRA 355
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
80-460 1.41e-24

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: 104.91  E-value: 1.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  80 LDKEQGIC-FRGMTIPECCEKipkswkggtSPLPEgMLWLLMTGSIPTDKQVKELHVELHRRADNEAitAATKTIASLPE 158
Cdd:cd06116  22 IDGEKGILrYRGYPIEQLAEQ---------SSYLE-VAYLLLHGELPTKERLAQWVYDITRHTMTHE--NLKKFMDGFRY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 159 NTHPMTQLSTGVLALQAFSKFAPAYASGKAIKSNFWEyaledsldIIARTPYLAAAIYnRLTTGRAAVLnpANPDLDWAA 238
Cdd:cd06116  90 DAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIR--------LIGKMPTIAAFAY-RHRLGLPYVL--PDNDLSYTG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 239 NFTNMLGYQDEKFWD-------CMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSY 311
Cdd:cd06116 159 NFLSMLFKMTEPKYEpnpvlakALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRM 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 312 LFEmrdkckaagvnMKDRKELAAGLEKLTwerlNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDELFFLVDTIYSI 391
Cdd:cd06116 238 LQQ-----------IGSPKNIPDFIETVK----QGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVEL 302
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887268 392 MPDILKKHGKTKNP-FPNVDAHSGMLLQHFGLTEQNFyTVLFGISRQLGALTGvvWDRLQGRP---IERPKSI 460
Cdd:cd06116 303 EKIALEDEYFISRKlYPNVDFYSGLIYQALGFPTEAF-TVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQV 372
gltA PRK05614
citrate synthase;
117-439 2.32e-24

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 104.57  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  117 WLLMTGSIPTDKQVKELHVELHRRAD-NEAITaatKTIASLPENTHPMTQLSTGVLALQAFskfapayasgkaiksnfwe 195
Cdd:PRK05614  90 YLLLYGELPTAEQKAEFDTTVTRHTMvHEQLK---RFFRGFRRDAHPMAVLCGVVGALSAF------------------- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  196 YalEDSLDI-------------IARTPYLAAAIYnRLTTGRAAVlNPANpDLDWAANFTNML-GYQDEKF------WDCM 255
Cdd:PRK05614 148 Y--HDSLDIndpehreiaairlIAKMPTLAAMAY-KYSIGQPFV-YPRN-DLSYAENFLRMMfATPCEEYevnpvlVRAL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  256 RLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEM-----------RDKCKAAGV 324
Cdd:PRK05614 223 DRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIgsvdnipefiaRAKDKNDGF 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  325 nmkdrkelaaglekltweRLNakrvipGYGHAVLRIPDPRYMCLREYC---LKHF-PDDELFflvdtiysimpDILKKHG 400
Cdd:PRK05614 302 ------------------RLM------GFGHRVYKNYDPRAKIMRETChevLKELgLNDPLL-----------EVAMELE 346
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 70887268  401 KT---------KNPFPNVDAHSGMLLQHFGLTeQNFYTVLFGISRQLG 439
Cdd:PRK05614 347 EIalndeyfieRKLYPNVDFYSGIILKALGIP-TSMFTVIFALARTVG 393
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
118-439 2.86e-23

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 100.80  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  118 LLMTGSIPTDKQVKELHVEL--HRRADNEAITAatktIASLPENTHPMTQLSTGVLALQAFSKFAPAyASGKAIksnfwe 195
Cdd:PRK14033  55 LLWNGELPTDAELALFSQREraYRRLDRSVLSL----IDKLPTTCHPMDVVRTAVSYLGAEDPEADD-SSPEAN------ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  196 yaLEDSLDIIARTPYLAAAIYnRLTTGRAAVlnPANPDLDWAANFTNM-LG-YQDEKFWDCMRLYLSLHADHeGGNVSAH 273
Cdd:PRK14033 124 --LAKALRLFAVLPTIVAADQ-RRRRGLDPI--APRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  274 ATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCKAAgvnmkdrkelaagleklTW--ERLNAKRVIP 351
Cdd:PRK14033 198 TARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAA-----------------EWlrDALARKEKVM 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  352 GYGHAVLRIPDPRYMCLREYCLK---HFPDDELFFLVDTIYSIMpdilkkhGKTKNPFPNVDAHSGMLLQHFGLtEQNFY 428
Cdd:PRK14033 261 GFGHRVYKHGDSRVPTMKAALRRvaaVRDGQRWLDIYEALEKAM-------AEATGIKPNLDFPAGPAYYLMGF-DIDFF 332
                        330
                 ....*....|.
gi 70887268  429 TVLFGISRQLG 439
Cdd:PRK14033 333 TPIFVMSRITG 343
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
113-459 9.22e-23

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: 99.30  E-value: 9.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 113 EGMLWLLMTGSIPTDKQVKELHVELH--RRadneaITAATKTI-ASLPENTHPMTQLSTGVLALQAFSKfapayasgkai 189
Cdd:cd06108  40 EEVAYLLLYGKLPTRKQLDAYKTKLValRR-----LPAALKTVlELIPKDSHPMDVMRTGCSMLGCLEP----------- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 190 ksnfwEYALEDSLDIIAR----TPYLAAAIYNRLTTGRaaVLNPANPDLDWAANFTNML-GYQDEKFW-DCMRLYLSLHA 263
Cdd:cd06108 104 -----ENEFSQQYEIAIRllaiFPSILLYWYHYSHSGK--RIETETDEDSIAGHFLHLLhGKKPGELEiKAMDVSLILYA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 264 DHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLfemrdkckaagVNMKDRKELAAGLEkltwER 343
Cdd:cd06108 177 EHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELI-----------ERFKSPEEAEQGLL----EK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 344 LNAKRVIPGYGHAVLRIPDPRYMCLREYCLK---HFPDDELFFLVDTIYSIMPdilkkhgKTKNPFPNVDAHSGMLLQHF 420
Cdd:cd06108 241 LERKELIMGFGHRVYKEGDPRSDIIKKWSKKlseEGGDPLLYQISERIEEVMW-------EEKKLFPNLDFYSASAYHFC 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 70887268 421 GL-TEqnFYTVLFGISRQLGALTGVVWDRLQGRPIeRPKS 459
Cdd:cd06108 314 GIpTE--LFTPIFVMSRVTGWAAHIMEQRANNRLI-RPSA 350
PRK12349 PRK12349
citrate synthase;
66-458 1.81e-22

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 98.64  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268   66 GMRGITGLIYESSMLDKEQG-ICFRGMTIPECCEKipKSWKGgtsplpegMLWLLMTGSIPTDKQVKELHvelHRRADNE 144
Cdd:PRK12349   8 GLDGVIAAETKISFLDTVKGeIVIQGYDLIELSKT--KEYLD--------IVHLLLEEHLPNEDEKATLE---KKLKEEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  145 AITAATKTI-ASLPENTHPMTQLSTGVLALQAFSkfapayasgKAIKSNFWEYALEDSLDIIARTPYLAAAIYnRLTTGR 223
Cdd:PRK12349  75 AVPEGVFNIlKALPKETHPMDGLRTGVSALAGYD---------NDIEDRSLEVNKSRAYKLLSKVPNIVANSY-HILNNE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  224 AAVlnPANPDLDWAANFTNML-----GYQDEKFWDcmRLyLSLHADHEGGNvSAHATTLVASALSDPYLSFSAGLNGLAG 298
Cdd:PRK12349 145 EPI--EPLKELSYSANFLYMLtgkkpTELEEKIFD--RS-LVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  299 PLHGLANQESLSYLFEMRDkckaagvnmkdrkelAAGLEKLTWERLNAKRVIPGYGHAV-LRIPDPRYMCLRE----YCL 373
Cdd:PRK12349 219 SLHGGANEAVMYMLLEAGT---------------VEKFEELLQKKLYNKEKIMGFGHRVyMKKMDPRALMMKEalkqLCD 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  374 KHfPDDELFFLVDTIYSIMPdilkkhgKTKNPFPNVDAHSGMLLQHFGLTEQnFYTVLFGISRQLGaLTGVVWDRLQGRP 453
Cdd:PRK12349 284 VK-GDYTLYEMCEAGEKIME-------KEKGLYPNLDYYAAPVYWMLGIPIQ-LYTPIFFSSRTVG-LCAHVIEQHANNR 353

                 ....*
gi 70887268  454 IERPK 458
Cdd:PRK12349 354 LFRPR 358
PRK14034 PRK14034
citrate synthase; Provisional
113-441 2.96e-20

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 92.14  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  113 EGMLWLLMTGSIPTDKQVKELHVELHRRAD--NEAITaatkTIASLP-ENTHPMTQLSTGVLALQAFSKFA----PAYAS 185
Cdd:PRK14034  42 EEVVYLLWHRKLPNKQELAEFKEQLSENAKvpGEIIE----HLKQYDlKKVHPMSVLRTAISMLGLYDEEAeimdEEANY 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  186 GKAIKsnfweyaledsldIIARTPYLAAAiYNRLTTGRAAVlnPANPDLDWAANFTNMLGYQ--DEKFWDCMRLYLSLHA 263
Cdd:PRK14034 118 RKAVR-------------LQAKVPTIVAA-FSRIRKGLDPV--EPRKDLSLAANFLYMLNGEepDEVEVEAFNKALVLHA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  264 DHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDkckaagvnmkdrkelAAGLEKLTWER 343
Cdd:PRK14034 182 DHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGE---------------EENVESYIHNK 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  344 LNAKRVIPGYGHAVLRIPDPRYMCLREYclkhfpDDELFFLV--DTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFG 421
Cdd:PRK14034 246 LQNKEKIMGFGHRVYRQGDPRAKHLREM------SKRLTVLLgeEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLG 319
                        330       340
                 ....*....|....*....|
gi 70887268  422 LtEQNFYTVLFGISRQLGAL 441
Cdd:PRK14034 320 I-DHDLFTPIFAISRMSGWL 338
PRK14037 PRK14037
citrate synthase; Provisional
113-460 9.17e-19

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 87.88  E-value: 9.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  113 EGMLWLLMTGSIPTDKQVKELHVELHRraDNEAITAATKTIASLPENTHPMTQLSTGVLALqafskfapayasgKAIKSN 192
Cdd:PRK14037  45 EETIYLMLYGELPTKKELNDLKEKLNE--EYEVPQEVIDSIYLMPRDSDAIGLMEAAFAAL-------------ASIDKN 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  193 FWEYAL--EDSLDIIARTPYLAAAIYNRLTTGRAAVLNPANpdlDWAANFTN--MLGYQDEKFWDCMRLYLSLHADHEgg 268
Cdd:PRK14037 110 FKWKENdkEKAISIIAKMATIVANVYRRKEGNKPRIPEPSD---SFAESFLLasFAREPTAEEIKAMDAALILYTDHE-- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  269 nVSAHATT-LVA-SALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDkckaagVNMKDRkelaaglekltWER--- 343
Cdd:PRK14037 185 -VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGD------PNNVEM-----------WFNdki 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  344 LNAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFPDDElffLVDTIYSIMPDILKKHGKT---KNPFPNVDAHSGMLLQHF 420
Cdd:PRK14037 247 INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNS---EAKKYFEIAQKLEELGIKQfgsKGIYPNTDFYSGIVFYAL 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 70887268  421 GLTeQNFYTVLFGISRQLGALTGVV-WDRLQGRPIeRPKSI 460
Cdd:PRK14037 324 GFP-VYMFTALFALSRTLGWLAHIIeYVEEQHRLI-RPRAL 362
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
113-460 5.75e-18

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: 85.05  E-value: 5.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 113 EGMLWLLMTGSIPTDKQVKELHVELHRRadnEAITAATKTIASLPENTHPMTQLSTGVLALQAfskfapayasgkaiksn 192
Cdd:cd06109  40 EDVAALLWNGFFPDLPELEEFRAALAAA---RALPDVVAALLPALAGLDPMDALRALLALLPD----------------- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 193 fwEYALEDSLDIIARTPYLAAAiYNRLTTGRAAVlNPaNPDLDWAANFTNMLGYQ--DEKFWDCMRLYLSLHADHeGGNV 270
Cdd:cd06109 100 --SPDLATALRLLAAAPVITAA-LLRLSRGKQPI-AP-DPSLSHAADYLRMLTGEppSEAHVRALDAYLVTVADH-GMNA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 271 SAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESLSYLFEMRDKCKAAGVNmkdRKELAAGlekltwERLNakrvi 350
Cdd:cd06109 174 STFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWL---REALARG------ERLM----- 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 351 pGYGHAVLRIPDPRYMCLREyCLKHFP-DDELFFLVDTIYSIMPDILKKHGKTKNPFPNVDAHSGMLLQHFGLTEQNFyT 429
Cdd:cd06109 240 -GFGHRVYRVRDPRADVLKA-AAERLGaPDERLEFAEAVEQAALALLREYKPGRPLETNVEFYTALLLEALGLPREAF-T 316
                       330       340       350
                ....*....|....*....|....*....|.
gi 70887268 430 VLFGISRQLGALTGVVWDRLQGRPIeRPKSI 460
Cdd:cd06109 317 PTFAAGRTAGWTAHVLEQARTGRLI-RPQSR 346
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
113-457 4.18e-17

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: 82.59  E-value: 4.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 113 EGMLWLLMTGSIPTDKQVKELHVELHRRADNEAITaaTKTIASLPENTHPMTQLSTGVLALQAFSKFAPAYASGKAiksn 192
Cdd:cd06117  40 EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANV--KTALEQLPAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGA---- 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 193 fweyalEDSLD-IIARTPYLAAAIYNRLTTGRAavLNPANPDLDWAANFTNML-GYQDEKFW-DCMRLYLSLHADHEGgN 269
Cdd:cd06117 114 ------RDIADrLMASLGSILLYWYHYSHNGKR--IEVETDDDSIGGHFLHLLhGEKPSESWeKAMHISLILYAEHEF-N 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 270 VSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESlsylFEMRDKCKAAgvnmkdrKELAAGLEKltweRLNAKRV 349
Cdd:cd06117 185 ASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVA----FEIQQRYESA-------DEAEADIRR----RVENKEV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 350 IPGYGHAVLRIPDPRYMCLREYClKHFPDD----ELFFLVDTIYSIMPDilkkhgkTKNPFPNVDAHSGMLLQHFGLTEQ 425
Cdd:cd06117 250 VIGFGHPVYTIADPRNQVIKEVA-KQLSKEggdmKMFDIAERLETVMWE-------EKKMFPNLDWFSAVSYHMMGVPTA 321
                       330       340       350
                ....*....|....*....|....*....|..
gi 70887268 426 NFyTVLFGISRQLGALTGVVWDRLQGRPIeRP 457
Cdd:cd06117 322 MF-TPLFVIARTTGWSAHIIEQRQDGKII-RP 351
PRK12351 PRK12351
methylcitrate synthase; Provisional
255-457 2.21e-13

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 71.49  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  255 MRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGLANQESlsylFEMRDKckaagvnMKDRKELAA 334
Cdd:PRK12351 180 MHTSLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVA----FEIQQR-------YDTPDEAEA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  335 GLEkltwERLNAKRVIPGYGHAVLRIPDPRYMCLREYCLK---HFPDDELFFLVDTIYSIMPDIlkkhgktKNPFPNVDA 411
Cdd:PRK12351 248 DIR----RRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKlskEAGDTKLYDIAERLETVMWEE-------KKMFPNLDW 316
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 70887268  412 HSGMLLQHFGLTEQNFyTVLFGISRQLGALTGVVWDRLQGRPIeRP 457
Cdd:PRK12351 317 FSAVSYHMMGVPTAMF-TPLFVISRTTGWAAHVIEQRQDNKII-RP 360
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
224-364 9.17e-11

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: 62.66  E-value: 9.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 224 AAVLNPANPDLDWAANFTNMLGyQDEKFWDCMRLYLSLHADHEGgNVSAHATTLVASALSDPYLSFSAGLNGLAGPLHGL 303
Cdd:cd06102  71 AALLGAAPSDAPVHRRLARAWG-LDPAAADLLRRALVLLADHEL-NASTFAARVAASTGASLYAAVLAGLAALSGPRHGG 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887268 304 ANQESLSYLFEMRDkckaagvnmkdrkelAAGLEKLTWERLNAKRVIPGYGHAVLRIPDPR 364
Cdd:cd06102 149 ATARVEALLDEALR---------------AGDAEAAVRERLRRGEALPGFGHPLYPDGDPR 194
PRK12350 PRK12350
citrate synthase 2; Provisional
229-372 1.94e-06

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 49.58  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268  229 PANPD--LDWAANFTNML-----GYQDEKFWDCMRLYLSLHADHeGGNVSAHATTLVASALSDPYLSFSAGLNGLAGPLH 301
Cdd:PRK12350 125 PAVPQreIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLH 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887268  302 GLANQESLSYLFEMRDKCKAAGVNmkdRKELAAGlekltwERLNakrvipGYGHAVLRIPDPRYMCLREYC 372
Cdd:PRK12350 204 GGAPARVLPMLDAVERTGDARGWV---KGALDRG------ERLM------GFGHRVYRAEDPRARVLRATA 259
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
263-378 1.29e-04

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: 43.32  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887268 263 ADHEGGNVSAHATTLVASALSDPYLS-FSAGLNGlAGPLHGLANQESLSYLFEMRDKCKAAGVNMKD-RKELAAgleklt 340
Cdd:cd06100  42 ADHGPATPSAHAARLTASAGPEDLQSaVAAGLLG-IGDRFGGAGEGAARLFKEAVDSGDALDAAAAEfVAEYRA------ 114
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 70887268 341 werlnAKRVIPGYGHAVLRIPDPRYMCLREYCLKHFPD 378
Cdd:cd06100 115 -----AKKRIPGFGHPVHKNPDPRVPRLLELARELGPA 147
 
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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