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Conserved domains on  [gi|966972916|ref|XP_015007477|]
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citrate synthase, mitochondrial isoform X1 [Macaca mulatta]

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 ...
33-459 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: 969.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGISRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 193 KYWELIYEDSMDLIAKLPCIAAKIYRNLYReGSGIGAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 353 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 966972916 433 LAQLIWSRALGFPLERPKSMSTEGLMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 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: 969.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGISRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 193 KYWELIYEDSMDLIAKLPCIAAKIYRNLYReGSGIGAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 353 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 966972916 433 LAQLIWSRALGFPLERPKSMSTEGLMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 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: 786.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916   30 STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  110 GGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGI 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  190 SRTKYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIgAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  270 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  350 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 966972916  430 LGVLAQLIWSRALGFPLERPKSMSTEGL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
33-464 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 607.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEG-ISR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 192 TKYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIgAIDSNLDWSHNFTNMLGYTDsQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPK-PYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 351 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 966972916 431 GVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSK 464
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
71-450 3.75e-131

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: 383.39  E-value: 3.75e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916   71 GMRGMKGLVYETSVLDPDEG-IRFRGFSIPEcqkLLpkakggEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPS 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LA------ERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  150 HVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEgisrtKYWELIYEDsmDLIAKLPCIAAKIYRnlYREGSGIGA 229
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKA-----DYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  230 IDSNLDWSHNFTNML-GYT-DSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  308 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 383
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966972916  384 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 450
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 7.69e-104

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: 314.73  E-value: 7.69e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGFSIPECQkllpkakggEEPLPEGLFWLLVTGQIPTEEQVSWL 137
Cdd:COG0372    4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 138 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALnseSNFaraYAEGISRTKywELIYEDSMDLIAKLPCIAAKIY 217
Cdd:COG0372   75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 218 RnlYREGSGIGAIDSNLDWSHNFTNMLGYT--DSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 295
Cdd:COG0372  147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 296 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 372
Cdd:COG0372  224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 373 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 451
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 ...
33-459 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: 969.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGISRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 193 KYWELIYEDSMDLIAKLPCIAAKIYRNLYReGSGIGAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 353 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 966972916 433 LAQLIWSRALGFPLERPKSMSTEGLMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
33-457 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: 818.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:cd06103    1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEG-ISR 191
Cdd:cd06103   81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 192 TKYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06103  161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06103  241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 352 KTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALG 431
Cdd:cd06103  321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                        410       420
                 ....*....|....*....|....*.
gi 966972916 432 VLAQLIWSRALGFPLERPKSMSTEGL 457
Cdd:cd06103  401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 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: 786.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916   30 STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  110 GGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGI 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  190 SRTKYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIgAIDSNLDWSHNFTNMLGYTDSQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  270 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  350 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 966972916  430 LGVLAQLIWSRALGFPLERPKSMSTEGL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
33-457 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: 641.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:cd06106    1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGISRT 192
Cdd:cd06106   81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 193 KYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDSQ-FTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06106  161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06106  241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 352 KTDPRYTCQREFALKH--LPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:cd06106  321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                        410       420
                 ....*....|....*....|....*...
gi 966972916 430 LGVLAQLIWSRALGFPLERPKSMSTEGL 457
Cdd:cd06106  401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
33-464 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 607.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  33 LKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGE 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 113 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEG-ISR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 192 TKYWELIYEDSMDLIAKLPCIAAKIYRNLYREGSGIgAIDSNLDWSHNFTNMLGYTDsQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPK-PYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 351 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 966972916 431 GVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSK 464
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
29-465 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 526.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  29 SSTNLKDILADLIPKEQARIKTFrqQHGKTVVGQITVDmmyGGMRGMKGLVYETSVLDPDEGI-RFRGFSIPECQKLLPK 107
Cdd:PLN02456  30 TGKDYESPLSELGPVQAERLKKI--KAGKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 108 akggeeplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAE 187
Cdd:PLN02456 105 ---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 188 GISRTKYWELIYEDSMDLIAKLPCIAAKIYRNLYreGSGIGAIDSNLDWSHNFTNMLGY-------TDSQFTELMRLYLT 260
Cdd:PLN02456 176 GQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMY--GRGPVIPDNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFI 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 261 IHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGR 340
Cdd:PLN02456 254 IHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KEIG---TVENIPEYVEGVKNSKK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 341 VVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLVAQLYKIVpnVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEm 417
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE- 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966972916 418 NYYTVLFGVSRALGVLAQliWSRALGFPLER---PKSMST-EGLMKFVDSKS 465
Cdd:PLN02456 404 EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTgEWLRHYCPKAE 453
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 4.52e-151

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: 433.95  E-value: 4.52e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  70 GGMRGMKGLVYETSVLDPDEGI-RFRGFSIPECQkllpkakggEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALP 148
Cdd:cd06118    1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELA---------EKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 149 SHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARayaegisrTKYWELIYEDSMDLIAKLPCIAAKIYRnlYREGSGIG 228
Cdd:cd06118   72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFAR--------DKSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 229 AIDSNLDWSHNFTNMLGY--TDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06118  142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 307 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 383
Cdd:cd06118  221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 384 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
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.
71-450 3.75e-131

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: 383.39  E-value: 3.75e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916   71 GMRGMKGLVYETSVLDPDEG-IRFRGFSIPEcqkLLpkakggEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPS 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LA------ERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  150 HVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEgisrtKYWELIYEDsmDLIAKLPCIAAKIYRnlYREGSGIGA 229
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKA-----DYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  230 IDSNLDWSHNFTNML-GYT-DSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  308 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 383
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966972916  384 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 450
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 7.69e-104

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: 314.73  E-value: 7.69e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGFSIPECQkllpkakggEEPLPEGLFWLLVTGQIPTEEQVSWL 137
Cdd:COG0372    4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 138 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALnseSNFaraYAEGISRTKywELIYEDSMDLIAKLPCIAAKIY 217
Cdd:COG0372   75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 218 RnlYREGSGIGAIDSNLDWSHNFTNMLGYT--DSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 295
Cdd:COG0372  147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 296 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 372
Cdd:COG0372  224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 373 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 451
Cdd:COG0372  297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 2.54e-97

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and 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: 293.45  E-value: 2.54e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  70 GGMRGMKGLVYETSVLDPDEGI-RFRGFSIPECQkllpkakggEEPLPEGLFWLLVTGQIPteeqvswlskewakraalp 148
Cdd:cd06101    1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELA---------ENSSFEEVAYLLLTGELP------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 149 shvvtmldnfptnlhpmsqlsaavtalnsesnfarayaegisrtkyweliyedsmdliaklpciaakiyrnlyregsgig 228
Cdd:cd06101      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 229 aidsnlDWSHNFTNMLGY--TDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06101   53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 307 EVLVWLTQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 383
Cdd:cd06101  126 AVLKMLEEIGTPK-----NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 384 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
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 ...
235-453 2.58e-90

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: 273.44  E-value: 2.58e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 235 DWSHNFTNMLGY--TDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 312
Cdd:cd06099    1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 313 TQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKIVPNVLL 389
Cdd:cd06099   80 EEIGTPK-----NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966972916 390 EqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
Cdd:cd06099  155 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
83-454 4.98e-46

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: 164.15  E-value: 4.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  83 SVLDPDEGI-RFRGFSIPEcqklLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06107   20 TYIDGDKGIlLYRGYPIEQ----LAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 162 LHPMSQLSAAVTALNS---ESNFARAYAEGISRTkywELIYEDSMDLIAKLPCIAAKIYRnlYREGSGIGAIDSNLDWSH 238
Cdd:cd06107   91 AHPMGILCAGLSALSAfypEAIPAHTGDLYQNNP---EVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 239 NFTNMLGYTDSQ-------FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 311
Cdd:cd06107  166 NFLYMMGYVDQEpyepnprLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 312 LtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVl 388
Cdd:cd06107  245 L----REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED- 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966972916 389 lEQGKAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQliWSRALGFPLE---RPKSMST 454
Cdd:cd06107  317 -EYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
73-437 2.43e-44

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: 158.98  E-value: 2.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  73 RGMKGLVYETSVL---DPDEGI-RFRGFSIPEcqklLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALP 148
Cdd:cd06110    1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD----LAENSTFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 149 SHVVTMLDNFPTNLHPMSQLSAAVTAL---NSEsnfarayAEGISRtkywELIYEDSMDLIAKLPCIAAKIYRnlYREGS 225
Cdd:cd06110   72 AEIIDLLKLLPKDAHPMDVLRTAVSALalyDPE-------ADDMSR----EANLRKAIRLIAKMPTIVAAFHR--IRNGL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 226 GIGAIDSNLDWSHNFTNMLGYT--DSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGL 303
Cdd:cd06110  139 EPVAPDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGG 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 304 ANQEVLVWLTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLvaqL 380
Cdd:cd06110  218 ANERVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRrlgKETGEPKWYEM---S 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966972916 381 YKIVPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 437
Cdd:cd06110  288 EAIEQAMRDE----KGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
83-462 1.00e-43

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: 157.58  E-value: 1.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  83 SVLDPDEGI-RFRGFSIPEcqklLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06112   16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 162 LHPMSQLSAAVTALNSesNFARAYAEGISRTKYWELIyedsMDLIAKLPCIAAKIYRnlYREGSGIGAIDSNLDWSHNFT 241
Cdd:cd06112   87 GHPMDMLQATVAALGM--FYPKPEVLKPNPDYIDAAT----VKLIAKMPTLVAMWAR--IRNGDDPIEPRPDLDYAENFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 242 NML--GYTDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEV 319
Cdd:cd06112  159 YMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----EEI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 320 GkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPN-----DPMFKLVAQLYKIVPNVLLEQGKa 394
Cdd:cd06112  234 G---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKGV- 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 395 knpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALGF-PLERPKSMST-EGLMKFVD 462
Cdd:cd06112  309 ---YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLGDnRIFRPTQIYIgEIDRKYVP 372
gltA PRK05614
citrate synthase;
85-436 3.89e-40

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 148.87  E-value: 3.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  85 LDPDEGI-RFRGFSIpecQKLLPKAKGGEeplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLH 163
Cdd:PRK05614  62 IDGDKGIlLYRGYPI---EQLAEKSDFLE------VCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAH 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 164 PMSQLSAAVTALnseSNFarayaegisrtkyweliYEDSMD-------------LIAKLPCIAAKIYRnlYREGSGIGAI 230
Cdd:PRK05614 133 PMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQPFVYP 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 231 DSNLDWSHNFTNML-GYTDSQF------TELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGL 303
Cdd:PRK05614 191 RNDLSYAENFLRMMfATPCEEYevnpvlVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 304 ANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTL--NSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHL-PNDPMFKLV 377
Cdd:PRK05614 270 ANEAVLKML----EEIG---SVDNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDPLLEVA 342
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 378 AQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQL 436
Cdd:PRK05614 343 MELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
83-462 2.27e-37

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: 141.42  E-value: 2.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  83 SVLDPDEGI-RFRGFSIPEcqkLLPKAKGGEeplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06115   40 SYIDGDKGIlRYRGYPIEE---LAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 162 LHPMSQLSAAVTALNS---ESNFARAyAEGISRTKywELIYEDSMDLIAKLPCIAAKIYRNlyREGSGIGAIDSNLDWSH 238
Cdd:cd06115  111 AHPMGMLVSAISALSAfhpEANPALA-GQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 239 NFTNML-GYTDSQFTELMRL------YLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 311
Cdd:cd06115  186 NFLYMLdSLGERKYKPNPRLaraldiLFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 312 LTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlpnDPMFKLVAQlykivpNVLLEQ 391
Cdd:cd06115  265 LA----EIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGK------DPLIEI 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 392 GKA-------------KNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 454
Cdd:cd06115  326 AVAlekaalsdeyfvkRKLYPNVDFYSGLIYRAMGFpTDF--FPVLFAIPRMAGYLAH--WRESLDDPdtkIMRPQQLYT 401

                 ....*....
gi 966972916 455 -EGLMKFVD 462
Cdd:cd06115  402 gVWLRHYVP 410
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
87-434 1.09e-36

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


Pssm-ID: 99866  Cd Length: 406  Bit Score: 139.32  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  87 PDEG-IRFRGFSIPEcqkLLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVV-TMLDNFPTNlHP 164
Cdd:cd06113   33 PCPGkLYYRGYDVED---LVNGAQKENRFGFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK-DI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 165 MSQLSAAVTALNSesnfaraY---AEGISRtkywELIYEDSMDLIAKLPCIAAKIY----RNLYREGSGIGAIDSNLDWS 237
Cdd:cd06113  109 MNKLQRSVLALYS-------YddkPDDISL----ENVLRQSIQLIARLPTIAVYAYqakrHYYDGESLYIHHPQPELSTA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 238 HNFTNMLgYTDSQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLT 313
Cdd:cd06113  178 ENILSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 314 QLQKEVgKDVSDEK-LRDYIWNTLN------SGrVVPGYGHAVLRKTDPRYTCQREFAlKHLPN----DPMFKLVAQLYK 382
Cdd:cd06113  257 DIKENV-KDWTDEDeVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERIER 333
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966972916 383 IVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 434
Cdd:cd06113  334 LAPEVIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCA 385
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
85-454 2.24e-35

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: 135.34  E-value: 2.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  85 LDPDEGI-RFRGFSIpecQKLLPKAKGGEeplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLH 163
Cdd:cd06116   22 IDGEKGIlRYRGYPI---EQLAEQSSYLE------VAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 164 PMSQLSAAVTALNSESNFARAYAEGISRTKyweliyeDSMDLIAKLPCIAAKIYRnlYREGSGIGAIDSNLDWSHNFTNM 243
Cdd:cd06116   93 PMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNFLSM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 244 LGY-------TDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 316
Cdd:cd06116  164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML---- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 317 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVllEQGK 393
Cdd:cd06116  239 QQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIALED--EYFI 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966972916 394 AKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 454
Cdd:cd06116  314 SRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14036 PRK14036
citrate synthase; Provisional
83-443 1.43e-34

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 132.77  E-value: 1.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  83 SVLDPDEGI-RFRGFSIPEcqklLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 161
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 162 LHPMSQLSAAVTALNSesNFARAyaeGISRTKYwelIYEDSMDLIAKLPCIAAKIyrNLYREGSGIGAIDSNLDWSHNFT 241
Cdd:PRK14036  90 GHPMDALQASAAALGL--FYSRR---ALDDPEY---IRDAVVRLIAKIPTMVAAF--QLIRKGNDPIQPRDDLDYAANFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 242 NMLG--YTDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEV 319
Cdd:PRK14036 160 YMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML----EEI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 320 GkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVLLEQGKakn 396
Cdd:PRK14036 235 G---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI--- 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 966972916 397 pWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 443
Cdd:PRK14036 309 -YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
PRK14032 PRK14032
citrate synthase; Provisional
87-434 6.27e-34

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 132.34  E-value: 6.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  87 PDEG-IRFRGFSIPECQKLLPKAK--GGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVV--TMLDNFPTN 161
Cdd:PRK14032  63 PDEGkLYYRGYDIKDLVNGFLKEKrfGFEE-----VAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrdMILKAPSKD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 162 LhpMSQLSAAVTALNS-ESNfarayAEGISRtkywELIYEDSMDLIAKLPCIAA---KIYRNLYREGSGIgaI---DSNL 234
Cdd:PRK14032 138 I--MNSLARSVLALYSyDDN-----PDDTSI----DNVLRQSISLIARFPTLAVyayQAYRHYHDGKSLY--IhppKPEL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 235 DWSHNFTNMLgYTDSQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLV 310
Cdd:PRK14032 205 STAENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVME 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 311 WLTQLQKEVGKDVSDEKLRDYIWNTLN------SGRVVpGYGHAVLRKTDPRYTCQREFAL-----KHLPNDpmFKLVAQ 379
Cdd:PRK14032 284 MFEDIKENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNLYEK 360
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 380 LYKIVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 434
Cdd:PRK14032 361 IEKLAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVGWSA 415
PRK14034 PRK14034
citrate synthase; Provisional
73-437 4.74e-29

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 117.56  E-value: 4.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  73 RGMKGLVYETSVLDP--DEGIRFRGFSIPECqkllpkakgGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSH 150
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 151 VVTMLDNFPTN-LHPMSQLSAAVTALNSESNFARAYAEgisrtkywELIYEDSMDLIAKLPCIAAKIYRnlYREGSGIGA 229
Cdd:PRK14034  76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDE--------EANYRKAVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 230 IDSNLDWSHNFTNMLG--YTDSQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:PRK14034 146 PRKDLSLAANFLYMLNgeEPDEVEVEAFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 308 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA--LKHLPNDPM-FKLVAQLYKIV 384
Cdd:PRK14034 225 VMKMLTEIGEE-------ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966972916 385 PNvlleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK14034 298 TK-------EKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHIL 342
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
117-441 9.61e-29

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 116.59  E-value: 9.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 117 EGLFWLLVTGQIPTEEQVSWLSK-EWAKRAALPShVVTMLDNFPTNLHPMSQLSAAVTALNSESnfarAYAEGISRtkyw 195
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQrERAYRRLDRS-VLSLIDKLPTTCHPMDVVRTAVSYLGAED----PEADDSSP---- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 196 ELIYEDSMDLIAKLPCIAAKIYRNlyREGSGIGAIDSNLDWSHNFTNM-LG-YTDSQFTELMRLYLTIHSDHeGGNVSAH 273
Cdd:PRK14033 121 EANLAKALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 274 TSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKT 353
Cdd:PRK14033 198 TARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHG 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 354 DPRYTCQREfALKHLPNDPMFKLVAQLYKIVPNVLLEqgkAKNPWPNVDAHSGVLlqYYGM---TEMnyYTVLFGVSRAL 430
Cdd:PRK14033 271 DSRVPTMKA-ALRRVAAVRDGQRWLDIYEALEKAMAE---ATGIKPNLDFPAGPA--YYLMgfdIDF--FTPIFVMSRIT 342
                        330
                 ....*....|.
gi 966972916 431 GVLAQLIWSRA 441
Cdd:PRK14033 343 GWTAHIMEQRA 353
PRK14035 PRK14035
citrate synthase; Provisional
117-436 1.52e-27

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 112.93  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 117 EGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPT-NLHPMSQLSAAVTALNSESNFARAYAEgisrtkyw 195
Cdd:PRK14035  42 EEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEYSTdHVHPMTALRTSVSYLAHFDPDAEEESD-------- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 196 ELIYEDSMDLIAKLPCIAAKIYRnlYREGSGIGAIDSNLDWSHNFTNMLG---YTDSQfTELMRLYLTIHSDHEGgNVSA 272
Cdd:PRK14035 114 EARYERAIRIQAKVASLVTAFAR--VRQGKEPLKPRPDLSYAANFLYMLRgelPTDIE-VEAFNKALVLHADHEL-NAST 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLqKEVGkDVSdeklrDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:PRK14035 190 FTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEI-RSIG-DVD-----AYLDEKFANKEKIMGFGHRVYKD 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 353 TDPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNVLLEQgkaKNPWPNVDAHSGVLlqYYGM-TEMNYYTVLFGVSRALG 431
Cdd:PRK14035 263 GDPRAKYLREMS-RKITKGTGREELFEMSVKIEKRMKEE---KGLIPNVDFYSATV--YHVMgIPHDLFTPIFAVSRVAG 336

                 ....*
gi 966972916 432 VLAQL 436
Cdd:PRK14035 337 WIAHI 341
PRK12349 PRK12349
citrate synthase;
74-437 5.51e-25

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 105.96  E-value: 5.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  74 GMKGLVY-ET--SVLDPDEG-IRFRGFSIPEcqklLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPS 149
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 150 HVVTMLDNFPTNLHPMSQLSAAVTAL----------NSESNFARAYaegisrtkyweliyedsmDLIAKLPCIAAKIYRN 219
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALagydndiedrSLEVNKSRAY------------------KLLSKVPNIVANSYHI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 220 LyrEGSGIGAIDSNLDWSHNFTNML-GYTDSQF-TELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFAAAMNGLA 297
Cdd:PRK12349 141 L--NNEEPIEPLKELSYSANFLYMLtGKKPTELeEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 298 GPLHGLANQEVLVWLTQlqkevGKDVSD-EKLrdyIWNTLNSGRVVPGYGHAV-LRKTDPRYTCQREfALKHL---PNDp 372
Cdd:PRK12349 218 GSLHGGANEAVMYMLLE-----AGTVEKfEEL---LQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcdvKGD- 287
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 373 mfklvAQLYKivpnvLLEQG-----KAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK12349 288 -----YTLYE-----MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
PRK14037 PRK14037
citrate synthase; Provisional
85-437 1.66e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 101.75  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  85 LDPDEGI-RFRGFSIPEcqklLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLH 163
Cdd:PRK14037  21 IDGEKGIlRYRGYNIED----LVNYGSYEE-----TIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 164 PMSQLSAAVTALNSesnfarayaegiSRTKYW--ELIYEDSMDLIAKLPCIAAKIYRnlYREGSGIGAIDSNLDWSHNFt 241
Cdd:PRK14037  92 AIGLMEAAFAALAS------------IDKNFKwkENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESF- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 242 nMLGYTDSQFTE----LMRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVlvwLTQL 315
Cdd:PRK14037 157 -LLASFAREPTAeeikAMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEA---FKQF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 316 QkEVGK-DVSDEKLRDyiwNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKA 394
Cdd:PRK14037 230 V-EIGDpNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGS 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 966972916 395 KNPWPNVDAHSGVLlqYYGMT-EMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK14037 306 KGIYPNTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
73-451 3.60e-19

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: 88.52  E-value: 3.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  73 RGMKGLV-YETSVLDPD--EG-IRFRGFSIPEcqkLLPKAKGgeeplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALP 148
Cdd:cd06109    1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED---LAGSASF------EDVAALLWNGFFPDLPELEEFRAALAAARALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 149 SHVVTMLDNFpTNLHPMSQLSAAVTALNSESNFarayaegisrtkyweliyEDSMDLIAKLPCIAAKIYRnlYREGSGIG 228
Cdd:cd06109   72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDL------------------ATALRLLAAAPVITAALLR--LSRGKQPI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 229 AIDSNLDWSHNFTNML-GYTDSQ-FTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06109  131 APDPSLSHAADYLRMLtGEPPSEaHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 307 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREfALKHLPNDPMFKLVAQLYKIVPN 386
Cdd:cd06109  210 PVLDML----DAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGAPDERLEFAEAVEQAAL 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966972916 387 VLLEQGKAKNP-WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 451
Cdd:cd06109  282 ALLREYKPGRPlETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
90-441 3.91e-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: 88.52  E-value: 3.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916  90 GIRFRGFSIPEcqklLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLS 169
Cdd:cd06108   22 GLTYRGYDIED----LAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 170 AAVTALNS---ESNFARAYAEGISrtkyweliyedsmdLIAKLPCIAAKIYRnLYREGSGIGAIDSNLDWSHNFTNML-G 245
Cdd:cd06108   93 TGCSMLGClepENEFSQQYEIAIR--------------LLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLhG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 246 YTDSQ-FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQkevgkdvS 324
Cdd:cd06108  158 KKPGElEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-------S 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 325 DEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN--DPMfklvaqLYKI---VPNVLLEQgkaKNPWP 399
Cdd:cd06108  230 PEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEggDPL------LYQIserIEEVMWEE---KKLFP 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 966972916 400 NVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRA 441
Cdd:cd06108  301 NLDFYSASAYHFCGIpTEL--FTPIFVMSRVTGWAAHIMEQRA 341
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
117-461 1.19e-14

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: 75.27  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 117 EGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAEGISRtkywe 196
Cdd:cd06117   40 EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGAR----- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 197 liyeDSMD-LIAKLPCIAAKIYrNLYREGSGIGAIDSNLDWSHNFTNML-GYTDSQ-FTELMRLYLTIHSDHEGgNVSAH 273
Cdd:cd06117  115 ----DIADrLMASLGSILLYWY-HYSHNGKRIEVETDDDSIGGHFLHLLhGEKPSEsWEKAMHISLILYAEHEF-NASTF 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 274 TSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGKdvSDEKLRDyIWNTLNSGRVVPGYGHAVLRKT 353
Cdd:cd06117  189 TARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAF----EIQQRYES--ADEAEAD-IRRRVENKEVVIGFGHPVYTIA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 354 DPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNVLLEQGKAknpWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGV 432
Cdd:cd06117  262 DPRNQVIKEVA-KQLSKEGGDMKMFDIAERLETVMWEEKKM---FPNLDWFSAVSYHMMGVpTAM--FTPLFVIARTTGW 335
                        330       340       350
                 ....*....|....*....|....*....|.
gi 966972916 433 LAQLIWSRALGfPLERPKSMST--EGLmKFV 461
Cdd:cd06117  336 SAHIIEQRQDG-KIIRPSANYTgpEDL-KFV 364
PRK12351 PRK12351
methylcitrate synthase; Provisional
122-441 9.24e-12

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 66.49  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 122 LLVTGQIPTEEQV-SWLSKEWAKRAaLPSHVVTMLDNFPTNLHPMSQLSAAVTAL------NSESNFARAYaegisrtky 194
Cdd:PRK12351  54 LLVHGKLPTQAELaAYKTKLKALRG-LPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR--------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 195 weliyeDSMD-LIAKLPCIAAKIYRnlyregsgigaidsnldWSHN----------------FTNML-GYTDSQ-FTELM 255
Cdd:PRK12351 124 ------DIADrLLASLGSILLYWYH-----------------YSHNgrrievetdddsigghFLHLLhGKKPSEsWVKAM 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 256 RLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANqEVLVwltQLQKevGKDVSDEKLRDyIWNT 335
Cdd:PRK12351 181 HTSLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQ--RYDTPDEAEAD-IRRR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 336 LNSGRVVPGYGHAVLRKTDPRYTCQREFALK---HLPNDPMFKLVAQLYKivpnVLLEQgkaKNPWPNVDAHSGVllQYY 412
Cdd:PRK12351 253 VENKEVVIGFGHPVYTISDPRNKVIKEVAKKlskEAGDTKLYDIAERLET----VMWEE---KKMFPNLDWFSAV--SYH 323
                        330       340       350
                 ....*....|....*....|....*....|..
gi 966972916 413 GM---TEMnyYTVLFGVSRALGVLAQLIWSRA 441
Cdd:PRK12351 324 MMgvpTAM--FTPLFVISRTTGWAAHVIEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
258-451 1.08e-08

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 56.90  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 258 YLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTqlqkEVGKDvsdEKLRDYIWNTLN 337
Cdd:PRK12350 161 YWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLD----AVERT---GDARGWVKGALD 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 338 SGRVVPGYGHAVLRKTDPRYTCQREfALKHLpNDPMFKLVAQLYKIVpnvlLEQGKAKNP----WPNVDAHSGVLLQYYG 413
Cdd:PRK12350 233 RGERLMGFGHRVYRAEDPRARVLRA-TAKRL-GAPRYEVAEAVEQAA----LAELRERRPdrplETNVEFWAAVLLDFAG 306
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 966972916 414 M-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 451
Cdd:PRK12350 307 VpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
210-448 1.37e-04

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 44.43  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 210 PCIAAKIYRNLYREGSGIGAIDSNLdWshnFTNMLGYTDSQFTElMRLYLTihSDHeGGNVS-AHTSHLVGSALSDPYLS 288
Cdd:PLN02522 365 PCYAGVPMSSIIEKDYGVGDVISLL-W---FKRSLPRYCTKFIE-MCIMLC--ADH-GPCVSgAHNTIVTARAGKDLVSS 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 289 FAAAMNGLaGPLHGLANQEVLVWLtqlqkevgKDVSDEKL--RDYIWNTLNSGRVVPGYGHAVLRKT--DPRYTCQREFA 364
Cdd:PLN02522 437 LVSGLLTI-GPRFGGAIDDAARYF--------KDAYDRGLtpYEFVEGMKKKGIRVPGIGHRIKSRDnrDKRVELLQKYA 507
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966972916 365 LKHLPNDPMFKLVAQlykiVPNVLLEqgKAKNPWPNVDAHSGV----LLQYYGM---------TEMNYYTVLFGVSRALG 431
Cdd:PLN02522 508 RTHFPSVKYMEYAVQ----VETYTLS--KANNLVLNVDGAIGSlfldLLAGSGMftkqeideiVEIGYLNGLFVLARSIG 581
                        250
                 ....*....|....*..
gi 966972916 432 VLAQLIWSRALGFPLER 448
Cdd:PLN02522 582 LIGHTFDQKRLKQPLYR 598
 
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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