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Conserved domains on  [gi|82127143|sp|Q6S9V6|]
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RecName: Full=Citrate synthase, mitochondrial; AltName: Full=Citrate (Si)-synthase; Flags: Precursor

Protein Classification

citrate synthase( domain architecture ID 10149814)

mitochondrial citrate synthase catalyzes the formation of citrate from acetyl-CoA and oxaloacetate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
36-463 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: 959.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVHKT 195
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 196 KYWEFIYEDSMDLIAKLPCIAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGNVSA 275
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 276 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLRK 355
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 356 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 435
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 82127143 436 LAQLVWSRALGFPLERPKSMSTDGLMTL 463
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
36-463 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: 959.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVHKT 195
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 196 KYWEFIYEDSMDLIAKLPCIAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGNVSA 275
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 276 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLRK 355
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 356 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 435
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 82127143 436 LAQLVWSRALGFPLERPKSMSTDGLMTL 463
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
33-460 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: 783.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143    33 STNLKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAP 112
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   113 GGEEPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGV 192
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   193 HKTKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGN 272
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   273 VSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAV 352
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   353 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 432
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 82127143   433 LGVLAQLVWSRALGFPLERPKSMSTDGL 460
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
36-467 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 619.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEG-VHK 194
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  195 TKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYSEPqFTELMRLYLTIHSDHEGGNVS 274
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPKP-YKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  275 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVS-DERMRDYIWNTLKSGRVVPGYGHAVL 353
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  354 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 433
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 82127143  434 GVLAQLVWSRALGFPLERPKSMSTDGLMTLVGAK 467
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
74-453 8.48e-132

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: 384.94  E-value: 8.48e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143    74 GMRGMKGLVYETSVLDPEEG-IRFRGYSIPEcqeLLPKAPggeeplPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPS 152
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   153 HVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAysegvHKTKYWEFIYEDsmDLIAKLPCIAAKIYRnlYREGSSIGA 232
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEAIS-----DKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   233 IDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 310
Cdd:pfam00285 143 PDPDLSYAENFLYMLFGYEPdpEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   311 VLVWLTALQKElggevsdERMRDYIWNTL-KSGRVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 386
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLnKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82127143   387 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLVWSRALGfPLERPK 453
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
65-454 1.71e-103

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: 313.57  E-value: 1.71e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  65 QITVDMVYGGMRGMKG-LVYETSV--LDPEEGI-RFRGYSIPECQEllpkapggeEPLPEGLFWLLVTGQVPTEEQVNWV 140
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLAE---------KSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 141 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALnseSSFaraYSEGVHKTKywEFIYEDSMDLIAKLPCIAAKIY 220
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 221 RnlYREGSSIGAIDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNG 298
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEEPdpEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 299 LAGPLHGLANQEVLVWLtalqKELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 375
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 376 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSRAlGFPLERPKS 454
Cdd:COG0372 297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
36-463 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: 959.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVHKT 195
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 196 KYWEFIYEDSMDLIAKLPCIAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGNVSA 275
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 276 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLRK 355
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 356 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 435
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 82127143 436 LAQLVWSRALGFPLERPKSMSTDGLMTL 463
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
36-460 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: 813.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEG-VHK 194
Cdd:cd06103  81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 195 TKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGNVS 274
Cdd:cd06103 161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 275 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLR 354
Cdd:cd06103 241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 355 KTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALG 434
Cdd:cd06103 321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                       410       420
                ....*....|....*....|....*.
gi 82127143 435 VLAQLVWSRALGFPLERPKSMSTDGL 460
Cdd:cd06103 401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
33-460 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: 783.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143    33 STNLKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAP 112
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   113 GGEEPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGV 192
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   193 HKTKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYSEPQFTELMRLYLTIHSDHEGGN 272
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   273 VSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAV 352
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   353 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 432
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 82127143   433 LGVLAQLVWSRALGFPLERPKSMSTDGL 460
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
36-460 0e+00

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: 636.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVHKT 195
Cdd:cd06106  81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 196 KYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGY-SEPQFTELMRLYLTIHSDHEGGNVS 274
Cdd:cd06106 161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYgDNLDFVDLLRLYIALHGDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 275 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLR 354
Cdd:cd06106 241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 355 KTDPRYTCQREFALKH--LPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 432
Cdd:cd06106 321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                       410       420
                ....*....|....*....|....*...
gi 82127143 433 LGVLAQLVWSRALGFPLERPKSMSTDGL 460
Cdd:cd06106 401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
36-467 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 619.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   36 LKDVLADLIPKEQTRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPEEGIRFRGYSIPECQELLPKAPGGE 115
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  116 EPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEG-VHK 194
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  195 TKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYSEPqFTELMRLYLTIHSDHEGGNVS 274
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPKP-YKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  275 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVS-DERMRDYIWNTLKSGRVVPGYGHAVL 353
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  354 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 433
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 82127143  434 GVLAQLVWSRALGFPLERPKSMSTDGLMTLVGAK 467
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
32-457 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 533.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   32 SSTNLKDVLADLIPKEQTRIKNFKQqyGKTNIGQITVDmvyGGMRGMKGLVYETSVLDPEEGI-RFRGYSIPECQELLPK 110
Cdd:PLN02456  30 TGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  111 apggeeplpEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSE 190
Cdd:PLN02456 105 ---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  191 GVHKTKYWEFIYEDSMDLIAKLPCIAAKIYRNLYREGSSIGaiDSNLDWSHNFTNMLGY-------SEPQFTELMRLYLT 263
Cdd:PLN02456 176 GQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP--DNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFI 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  264 IHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtalqKELGgevSDERMRDYIWNTLKSGR 343
Cdd:PLN02456 254 IHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KEIG---TVENIPEYVEGVKNSKK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  344 VVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLVAQLYKIVpnVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEm 420
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE- 403
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 82127143  421 NYYTVLFGVSRALGVLAQlvWSRALGFPLER---PKSMST 457
Cdd:PLN02456 404 EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYT 441
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
73-456 1.13e-147

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: 425.48  E-value: 1.13e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  73 GGMRGMKGLVYETSVLDPEEGI-RFRGYSIPECQELlpkapggeePLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALP 151
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 152 SHVVTMLDNFPTNLHPMSQFSAAITALNSESSFAraysegvhKTKYWEFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIG 231
Cdd:cd06118  72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFA--------RDKSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 232 AIDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 309
Cdd:cd06118 142 APDPDLSYAENFLYMLFGEEPdpEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 310 EVLVWLTALQKElggevsdERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 386
Cdd:cd06118 221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 387 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLVWSRALGFPLERPKSMS 456
Cdd:cd06118 294 ALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
74-453 8.48e-132

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: 384.94  E-value: 8.48e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143    74 GMRGMKGLVYETSVLDPEEG-IRFRGYSIPEcqeLLPKAPggeeplPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPS 152
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   153 HVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAysegvHKTKYWEFIYEDsmDLIAKLPCIAAKIYRnlYREGSSIGA 232
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEAIS-----DKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   233 IDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 310
Cdd:pfam00285 143 PDPDLSYAENFLYMLFGYEPdpEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   311 VLVWLTALQKElggevsdERMRDYIWNTL-KSGRVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 386
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLnKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82127143   387 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLVWSRALGfPLERPK 453
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
65-454 1.71e-103

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: 313.57  E-value: 1.71e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  65 QITVDMVYGGMRGMKG-LVYETSV--LDPEEGI-RFRGYSIPECQEllpkapggeEPLPEGLFWLLVTGQVPTEEQVNWV 140
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLAE---------KSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 141 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALnseSSFaraYSEGVHKTKywEFIYEDSMDLIAKLPCIAAKIY 220
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 221 RnlYREGSSIGAIDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNG 298
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEEPdpEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 299 LAGPLHGLANQEVLVWLtalqKELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 375
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 376 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSRAlGFPLERPKS 454
Cdd:COG0372 297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
73-456 1.03e-95

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: 289.60  E-value: 1.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  73 GGMRGMKGLVYETSVLDPEEGI-RFRGYSIPECQELlpkapggeePLPEGLFWLLVTGQVPteeqvnwvskewakraalp 151
Cdd:cd06101   1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAEN---------SSFEEVAYLLLTGELP------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 152 shvvtmldnfptnlhpmsqfsaaitalnsessfaraysegvhktkywefiyedsmdliaklpciaakiyrnlyregssig 231
Cdd:cd06101     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 232 aidsnlDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 309
Cdd:cd06101  53 ------SYAENFLYMLGGEEPdpEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 310 EVLVWLTALqkelgGEVSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 386
Cdd:cd06101 126 AVLKMLEEI-----GTPKNEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 387 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLVWSRALGFPLERPKSMS 456
Cdd:cd06101 201 APEVLYE----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
238-456 7.99e-89

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: 269.98  E-value: 7.99e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 238 DWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWL 315
Cdd:cd06099   1 SYAENFLYMLGGEEPdpEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 316 talqkELGGEVSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKIVPNVLL 392
Cdd:cd06099  80 -----EEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82127143 393 EqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLVWSRALGFPLERPKSMS 456
Cdd:cd06099 155 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
86-446 3.52e-45

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: 161.82  E-value: 3.52e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  86 SVLDPEEGI-RFRGYSIpecqELLPKAPGGEEplpegLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTN 164
Cdd:cd06112  16 SYIDGKNGIlEYRGYDI----EELAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 165 LHPMSQFSAAITALNSESSFARAYSEgvhKTKYwefIYEDSMDLIAKLPCIAAKIYRnlYREGSSIGAIDSNLDWSHNFT 244
Cdd:cd06112  87 GHPMDMLQATVAALGMFYPKPEVLKP---NPDY---IDAATVKLIAKMPTLVAMWAR--IRNGDDPIEPRPDLDYAENFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 245 NMLGYSEPQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtalqKEL 322
Cdd:cd06112 159 YMLFGEEPDpaTAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----EEI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 323 GgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPN-----DPMFKLVAQLYKIVPNVLLEQGKa 397
Cdd:cd06112 234 G---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKGV- 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 82127143 398 knpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQlvWSRALG 446
Cdd:cd06112 309 ---YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLG 351
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
76-439 3.22e-42

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: 153.20  E-value: 3.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  76 RGMKGLVYETSVL---DPEEGI-RFRGYSIpecQELLPKApGGEEPLpeglfWLLVTGQVPTEEQVNWVSKEWAKRAALP 151
Cdd:cd06110   1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDI---HDLAENS-TFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 152 SHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEgvhktkywEFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIG 231
Cdd:cd06110  72 AEIIDLLKLLPKDAHPMDVLRTAVSALALYDPEADDMSR--------EANLRKAIRLIAKMPTIVAAFHR--IRNGLEPV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 232 AIDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 309
Cdd:cd06110 142 APDPDLSHAANFLYMLTGEKPseEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 310 EVLVWLTalqkELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLvaqLYKI 386
Cdd:cd06110 221 RVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRrlgKETGEPKWYEM---SEAI 290
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 82127143 387 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQL 439
Cdd:cd06110 291 EQAMRDE----KGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHI 338
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
86-457 1.81e-41

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: 151.82  E-value: 1.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  86 SVLDPEEGI-RFRGYSIpecqELLPKAPGGEEPLpeglfWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTN 164
Cdd:cd06107  20 TYIDGDKGIlLYRGYPI----EQLAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 165 LHPMSQFSAAITALNSESSFARAYSEGVHKTKYWEFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIGAIDSNLDWSHNFT 244
Cdd:cd06107  91 AHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNPEVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIENFL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 245 NMLGYSE-------PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLta 317
Cdd:cd06107 169 YMMGYVDqepyepnPRLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKML-- 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 318 lqKELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVllEQ 394
Cdd:cd06107 246 --REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED--EY 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82127143 395 GKAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQlvWSRALGFPLE---RPKSMST 457
Cdd:cd06107 319 FVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
gltA PRK05614
citrate synthase;
88-439 2.41e-38

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 144.25  E-value: 2.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   88 LDPEEGI-RFRGYSIpecQELLPKAPGGEeplpegLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLH 166
Cdd:PRK05614  62 IDGDKGIlLYRGYPI---EQLAEKSDFLE------VCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAH 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  167 PMSQFSAAITALnseSSFaraysegvhktkywefiYEDSMD-------------LIAKLPCIAAKIYRnlYREGSSIGAI 233
Cdd:PRK05614 133 PMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQPFVYP 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  234 DSNLDWSHNFTNML-GYS------EPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGL 306
Cdd:PRK05614 191 RNDLSYAENFLRMMfATPceeyevNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  307 ANQEVLVWLtalqKELGgevSDERMRDYIwNTLK---SGRVVPGYGHAVLRKTDPRYTCQREFA---LKHL-PNDPMFKL 379
Cdd:PRK05614 270 ANEAVLKML----EEIG---SVDNIPEFI-ARAKdknDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDPLLEV 341
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82127143  380 VAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQL 439
Cdd:PRK05614 342 AMELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
PRK14036 PRK14036
citrate synthase; Provisional
86-446 9.37e-36

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 136.24  E-value: 9.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   86 SVLDPEEGI-RFRGYSIPEcqelLPKAPGGEEPLpeglfWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTN 164
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  165 LHPMSQFSAAITALnseSSFaraYS-EGVHKTKYwefIYEDSMDLIAKLPCIAAKIyrNLYREGSSIGAIDSNLDWSHNF 243
Cdd:PRK14036  90 GHPMDALQASAAAL---GLF---YSrRALDDPEY---IRDAVVRLIAKIPTMVAAF--QLIRKGNDPIQPRDDLDYAANF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  244 TNMLGYSEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtalqKE 321
Cdd:PRK14036 159 LYMLTEREPdpLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML----EE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  322 LGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVLLEQGKak 398
Cdd:PRK14036 234 IG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI-- 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 82127143  399 npWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQlvWSRALG 446
Cdd:PRK14036 309 --YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
86-448 4.61e-35

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: 134.88  E-value: 4.61e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  86 SVLDPEEGI-RFRGYSIpecQELLPKAPGGEeplpegLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTN 164
Cdd:cd06115  40 SYIDGDKGIlRYRGYPI---EELAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 165 LHPMSQFSAAITALNS---ESSFARAySEGVHKTKywEFIYEDSMDLIAKLPCIAAKIYRNlyREGSSIGAIDSNLDWSH 241
Cdd:cd06115 111 AHPMGMLVSAISALSAfhpEANPALA-GQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 242 NFTNML-GYSEPQFTELMRL------YLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVW 314
Cdd:cd06115 186 NFLYMLdSLGERKYKPNPRLaraldiLFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 315 LTalqkELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlpnDPMFKLVAQlykivpNVLLEQ 394
Cdd:cd06115 265 LA----EIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGK------DPLIEI 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82127143 395 GKA-------------KNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQlvWSRALGFP 448
Cdd:cd06115 326 AVAlekaalsdeyfvkRKLYPNVDFYSGLIYRAMGFpTDF--FPVLFAIPRMAGYLAH--WRESLDDP 389
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
88-457 2.67e-34

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: 132.26  E-value: 2.67e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  88 LDPEEGI-RFRGYSIPECQE---LLPKApggeeplpeglfWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPT 163
Cdd:cd06116  22 IDGEKGIlRYRGYPIEQLAEqssYLEVA------------YLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 164 NLHPMSQFSAAITALNSESSFAR-AYSEGVHKTKYWEfiyedsmdLIAKLPCIAAKIYRnlYREGSSIGAIDSNLDWSHN 242
Cdd:cd06116  90 DAHPMGILISSVAALSTFYPEAKnIGDEEQRNKQIIR--------LIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 243 FTNMLGY-------SEPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWL 315
Cdd:cd06116 160 FLSMLFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 316 talqKELGgevSDERMRDYIwNTLKSG-RVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVl 391
Cdd:cd06116 239 ----QQIG---SPKNIPDFI-ETVKQGkERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIALED- 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82127143 392 lEQGKAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQlvWSRALGFP---LERPKSMST 457
Cdd:cd06116 310 -EYFISRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
96-437 5.70e-32

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: 126.23  E-value: 5.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  96 FRGYSIpecQELLPKAPGGEEPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVV-TMLDNFPTNlHPMSQFSAA 174
Cdd:cd06113  40 YRGYDV---EDLVNGAQKENRFGFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK-DIMNKLQRS 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 175 ITALNSESSFARAYSEgvhktkywEFIYEDSMDLIAKLPCIAAKIYR--NLYREGSS--IGAIDSNLDWSHNFTNMLgYS 250
Cdd:cd06113 116 VLALYSYDDKPDDISL--------ENVLRQSIQLIARLPTIAVYAYQakRHYYDGESlyIHHPQPELSTAENILSML-RP 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 251 EPQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEV 326
Cdd:cd06113 187 DKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENVKDWT 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 327 SDERMRDYIWNTL------KSGrVVPGYGHAVLRKTDPRYTCQREFAlKHLPN----DPMFKLVAQLYKIVPNVLLEQ-G 395
Cdd:cd06113 267 DEDEVRAYLRKILnkeafdKSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERIERLAPEVIAEErG 344
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 82127143 396 KAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 437
Cdd:cd06113 345 IGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCA 385
PRK14032 PRK14032
citrate synthase; Provisional
59-437 1.63e-30

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 122.71  E-value: 1.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   59 GKTNIGQItvdmvyggmrgmKGLVYETSVLDPEEG-IRFRGYSIpecQELLpkapggEEPLPEGLF------WLLVTGQV 131
Cdd:PRK14032  44 GLTNIGDV------------HGYEIDDGEKIPDEGkLYYRGYDI---KDLV------NGFLKEKRFgfeevaYLLLFGEL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  132 PTEEQVNWVSKEWAKRAALPSHVV--TMLDNFPTNLhpMSQFSAAITALNSessfaraYSEGVHKTKYwEFIYEDSMDLI 209
Cdd:PRK14032 103 PTKEELAEFTELLGDYRELPDGFTrdMILKAPSKDI--MNSLARSVLALYS-------YDDNPDDTSI-DNVLRQSISLI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  210 AKLPCIAAKIYR--NLYREGSS--IGAIDSNLDWSHNFTNMLgYSEPQFTEL----MRLYLTIHSDHEGGNVSAHTSHLV 281
Cdd:PRK14032 173 ARFPTLAVYAYQayRHYHDGKSlyIHPPKPELSTAENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVV 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  282 GSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKELGGEVSDERMRDYIWNTL------KSGRVVpGYGHAVLRK 355
Cdd:PRK14032 252 SSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILnkeafdKSGLIY-GMGHAVYTI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  356 TDPRYTCQREFAL-----KHLPNDpmFKLVAQLYKIVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTV 425
Cdd:PRK14032 331 SDPRAVILKKFAEklakeKGREEE--FNLYEKIEKLAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTP 403
                        410
                 ....*....|..
gi 82127143  426 LFGVSRALGVLA 437
Cdd:PRK14032 404 LFAIARIVGWSA 415
PRK14034 PRK14034
citrate synthase; Provisional
76-439 1.47e-29

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 118.71  E-value: 1.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   76 RGMKGLVYETSVLDP--EEGIRFRGYSIPECqellpkapgGEEPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSH 153
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  154 VVTMLDNFPTN-LHPMSQFSAAITALNSESSFARAYSEgvhktkywEFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIGA 232
Cdd:PRK14034  76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDE--------EANYRKAVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  233 IDSNLDWSHNFTNMLGYSEPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 310
Cdd:PRK14034 146 PRKDLSLAANFLYMLNGEEPDEVEVeaFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  311 VLVWLTALqkelgGEVsdERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFA--LKHLPNDPM-FKLVAQLYKIV 387
Cdd:PRK14034 225 VMKMLTEI-----GEE--ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 82127143  388 PNvlleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQL 439
Cdd:PRK14034 298 TK-------EKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHI 341
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
76-444 1.90e-28

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 115.82  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   76 RGMKGLVYET---SVLDPE-EGIRFRGYSIpecQELLPKAPGgeeplpEGLFWLLVTGQVPTEEQVNWVSK-EWAKRAAL 150
Cdd:PRK14033  11 KGLAGVVVDTtaiSKVVPEtNSLTYRGYPV---QDLAARCSF------EEVAYLLWNGELPTDAELALFSQrERAYRRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  151 PShVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEgvhktkywEFIYEDSMDLIAKLPCIAAKIYRNlyREGSSI 230
Cdd:PRK14033  82 RS-VLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADDSSP--------EANLAKALRLFAVLPTIVAADQRR--RRGLDP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  231 GAIDSNLDWSHNFTNMLGYSEPQ------FTELMRLYltihSDHeGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLH 304
Cdd:PRK14033 151 IAPRSDLGYAENFLHMCFGEVPEpevvraFEVSLILY----AEH-SFNASTFTARVITSTLSDIYSAVTGAIGALKGPLH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  305 GLANQEVLVWLtalqKELGgevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREfALKHLPNDPMFKLVAQLY 384
Cdd:PRK14033 226 GGANEAVMHTM----LEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHGDSRVPTMKA-ALRRVAAVRDGQRWLDIY 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82127143  385 KIVPNVLLEqgkAKNPWPNVDAHSGVLlqYYGM---TEMnyYTVLFGVSRALGVLAQLVWSRA 444
Cdd:PRK14033 298 EALEKAMAE---ATGIKPNLDFPAGPA--YYLMgfdIDF--FTPIFVMSRITGWTAHIMEQRA 353
PRK14035 PRK14035
citrate synthase; Provisional
120-439 2.36e-28

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 115.63  E-value: 2.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  120 EGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPT-NLHPMsqfsaaiTALNSESSFARAYSEGVHKTKYw 198
Cdd:PRK14035  42 EEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEYSTdHVHPM-------TALRTSVSYLAHFDPDAEEESD- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  199 EFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIGAIDSNLDWSHNFTNMLGYSEPQFTEL--MRLYLTIHSDHEGgNVSAH 276
Cdd:PRK14035 114 EARYERAIRIQAKVASLVTAFAR--VRQGKEPLKPRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTF 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  277 TSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALqkelgGEVSDerMRDYIWNTLKSGRVVPGYGHAVLRKT 356
Cdd:PRK14035 191 TARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEI-----RSIGD--VDAYLDEKFANKEKIMGFGHRVYKDG 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  357 DPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNVLLEQgkaKNPWPNVDAHSGVLlqYYGM-TEMNYYTVLFGVSRALGV 435
Cdd:PRK14035 264 DPRAKYLREMS-RKITKGTGREELFEMSVKIEKRMKEE---KGLIPNVDFYSATV--YHVMgIPHDLFTPIFAVSRVAGW 337

                 ....
gi 82127143  436 LAQL 439
Cdd:PRK14035 338 IAHI 341
PRK14037 PRK14037
citrate synthase; Provisional
88-440 3.94e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 100.59  E-value: 3.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   88 LDPEEGI-RFRGYSIPECQELLPKapggeeplpEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLH 166
Cdd:PRK14037  21 IDGEKGIlRYRGYNIEDLVNYGSY---------EETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  167 PMSQFSAAITALNSESSfaraysegvhKTKYWEFIYEDSMDLIAKLPCIAAKIYRnlYREGSSIGAIDSNLDWSHNFTNM 246
Cdd:PRK14037  92 AIGLMEAAFAALASIDK----------NFKWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  247 LGYSEPQFTEL--MRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTALQKEl 322
Cdd:PRK14037 160 SFAREPTAEEIkaMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDP- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  323 ggEVSDERMRDYIWNTLKsgRVVpGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWP 402
Cdd:PRK14037 236 --NNVEMWFNDKIINGKK--RLM-GFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGIYP 310
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 82127143  403 NVDAHSGVLlqYYGMT-EMNYYTVLFGVSRALGVLAQLV 440
Cdd:PRK14037 311 NTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
PRK12349 PRK12349
citrate synthase;
77-440 4.49e-23

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 100.18  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143   77 GMKGLVY-ET--SVLDPEEG-IRFRGYSIPEcqelLPKAPGGEEplpegLFWLLVTGQVPTEEQVNWVSKEWAKRAALPS 152
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  153 HVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVHKTKywefiyedSMDLIAKLPCIAAKIYRNLyrEGSSIGA 232
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSR--------AYKLLSKVPNIVANSYHIL--NNEEPIE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  233 IDSNLDWSHNFTNMLGYSEP--QFTELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 310
Cdd:PRK12349 149 PLKELSYSANFLYMLTGKKPteLEEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  311 VLVWLtalqkeLGGEVSDERMRdYIWNTLKSGRVVPGYGHAV-LRKTDPRYTCQREfALKHL---PNDpmfklvAQLYKi 386
Cdd:PRK12349 228 VMYML------LEAGTVEKFEE-LLQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcdvKGD------YTLYE- 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 82127143  387 vpnvLLEQG-----KAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLV 440
Cdd:PRK12349 293 ----MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
76-454 6.81e-21

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: 93.52  E-value: 6.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  76 RGMKGLV-YETSVLDP--EEG-IRFRGYSIpecQELLPKAPGgeeplpEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALP 151
Cdd:cd06109   1 PGLEGVVaAETVLSDVdgEAGrLIIRGYSV---EDLAGSASF------EDVAALLWNGFFPDLPELEEFRAALAAARALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 152 SHVVTMLDNFpTNLHPMSQFSAAITALNSESSFaraysegvhktkywefiyEDSMDLIAKLPCIAAKIYRnlYREGSSIG 231
Cdd:cd06109  72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDL------------------ATALRLLAAAPVITAALLR--LSRGKQPI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 232 AIDSNLDWSHNFTNMLGYSEPQFTELMRL--YLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 309
Cdd:cd06109 131 APDPSLSHAADYLRMLTGEPPSEAHVRALdaYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 310 EVLVWLTALQkelggevSDERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREfALKHLPNDPMFKLVAQLYKIVPN 389
Cdd:cd06109 210 PVLDMLDAIG-------TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGAPDERLEFAEAVEQAAL 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82127143 390 VLLEQGKAKNP-WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSRALGfPLERPKS 454
Cdd:cd06109 282 ALLREYKPGRPlETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
93-444 2.74e-19

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: 88.90  E-value: 2.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  93 GIRFRGYSIPEcqelLPKAPGGEEplpegLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQF- 171
Cdd:cd06108  22 GLTYRGYDIED----LAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMr 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 172 --SAAITALNSESSFARAYsegvhktkywefiyEDSMDLIAKLPCIAAKIYRnLYREGSSIGAIDSNLDWSHNFTNMLGY 249
Cdd:cd06108  93 tgCSMLGCLEPENEFSQQY--------------EIAIRLLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLHG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 250 SEP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLvwltALQKELGgevS 327
Cdd:cd06108 158 KKPgeLEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAM----ELIERFK---S 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 328 DERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN--DPMfklvaqLYKI---VPNVLLEQgkaKNPWP 402
Cdd:cd06108 230 PEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEggDPL------LYQIserIEEVMWEE---KKLFP 300
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 82127143 403 NVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSRA 444
Cdd:cd06108 301 NLDFYSASAYHFCGIpTEL--FTPIFVMSRVTGWAAHIMEQRA 341
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
94-443 1.41e-13

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: 71.80  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  94 IRFRGYSIPEcqelLPKAPGGEEplpegLFWLLVTGQVPTEEQV-NWVSKEWAKRAaLPSHVVTMLDNFPTNLHPMSQFS 172
Cdd:cd06117  23 LHYRGYDILD----LAEKCEFEE-----VAHLLVHGKLPTKSELaAYKTKLKSLRG-LPANVKTALEQLPAAAHPMDVMR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 173 AAITALNSESSFARAYSEGVHKtkywefiyeDSMD-LIAKLPCIAAKIYrNLYREGSSIGAIDSNLDWSHNFTNMLGYSE 251
Cdd:cd06117  93 TGVSVLGCVLPEKEDHPVSGAR---------DIADrLMASLGSILLYWY-HYSHNGKRIEVETDDDSIGGHFLHLLHGEK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 252 PQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLvwltALQKELGGevSDE 329
Cdd:cd06117 163 PSesWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAF----EIQQRYES--ADE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143 330 RMRDyIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNVLLEQGKAknpWPNVDAHSG 409
Cdd:cd06117 236 AEAD-IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGGDMKMFDIAERLETVMWEEKKM---FPNLDWFSA 310
                       330       340       350
                ....*....|....*....|....*....|....*
gi 82127143 410 VLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSR 443
Cdd:cd06117 311 VSYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12351 PRK12351
methylcitrate synthase; Provisional
125-444 3.52e-10

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 61.48  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  125 LLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITAL------NSESSFARAYsegvhktkyw 198
Cdd:PRK12351  54 LLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR---------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  199 efiyeDSMD-LIAKLPCIAAKIYR--------NLYREGSSIGAidsnldwsHnFTNMLGYSEPQ--FTELMRLYLTIHSD 267
Cdd:PRK12351 124 -----DIADrLLASLGSILLYWYHyshngrriEVETDDDSIGG--------H-FLHLLHGKKPSesWVKAMHTSLILYAE 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  268 HEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANqEVlvwltALQKELGGEVSDERMRDyIWNTLKSGRVVPG 347
Cdd:PRK12351 190 HEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EV-----AFEIQQRYDTPDEAEAD-IRRRVENKEVVIG 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  348 YGHAVLRKTDPRYTCQREFALK---HLPNDPMFKLVAQLYKivpnVLLEQgkaKNPWPNVDAHSGVllQYYGM---TEMn 421
Cdd:PRK12351 262 FGHPVYTISDPRNKVIKEVAKKlskEAGDTKLYDIAERLET----VMWEE---KKMFPNLDWFSAV--SYHMMgvpTAM- 331
                        330       340
                 ....*....|....*....|...
gi 82127143  422 yYTVLFGVSRALGVLAQLVWSRA 444
Cdd:PRK12351 332 -FTPLFVISRTTGWAAHVIEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
234-454 2.51e-09

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 58.82  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  234 DSNLDWSHNFTNML-----GYSEPQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLAN 308
Cdd:PRK12350 129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82127143  309 QEVLVWLTALQKElggevsdERMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQREfALKHLpNDPMFKLVAQLYKIVp 388
Cdd:PRK12350 208 ARVLPMLDAVERT-------GDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRL-GAPRYEVAEAVEQAA- 277
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82127143  389 nvlLEQGKAKNP----WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLVWSRALGfPLERPKS 454
Cdd:PRK12350 278 ---LAELRERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
 
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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