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Conserved domains on  [gi|230994|pdb|4CTS|B]
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Chain B, CITRATE SYNTHASE

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 ...
6-433 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: 971.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRT 165
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      166 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSA 245
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      246 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 325
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      326 TDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 405
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
4CTS_B      406 LAQLIWSRALGFPLERPKSMSTDGLIKL 433
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
6-433 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: 971.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRT 165
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      166 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSA 245
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      246 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 325
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      326 TDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 405
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
4CTS_B      406 LAQLIWSRALGFPLERPKSMSTDGLIKL 433
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
3-430 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B          3 STNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAK 82
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         83 GGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGI 162
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        163 HRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGN 242
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        243 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 322
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        323 LRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 402
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
4CTS_B        403 LGVLAQLIWSRALGFPLERPKSMSTDGL 430
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
6-437 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 602.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-IHR 164
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       165 TKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSKLDWSHNFTNMLGYTDaQFTELMRLYLTIHSDHEGGNVS 244
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPK-PYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       245 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 323
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       324 RKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 403
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
4CTS_B       404 GVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK 437
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
44-423 4.75e-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: 381.85  E-value: 4.75e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         44 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALP 121
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        122 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEgihrtKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 201
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKA-----DYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        202 AIDSKLDWSHNFTNML-GYT-DAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        280 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---HDPMFKLVAQLYK 355
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4CTS_B        356 IVPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 423
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
35-424 3.31e-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: 314.34  E-value: 3.31e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       35 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQIPTEEQVSWL 110
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      111 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGIHRTKywELIYEDCMDLIAKLPCVAAKIY 190
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      191 RnlYREGSSIGAIDSKLDWSHNFTNMLGYT--DAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 268
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      269 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPHDP 345
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      346 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 424
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 ...
6-433 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: 971.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRT 165
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      166 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSA 245
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      246 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 325
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      326 TDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 405
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
4CTS_B      406 LAQLIWSRALGFPLERPKSMSTDGLIKL 433
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
6-430 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: 819.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-IHR 164
Cdd:cd06103  81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      165 TKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVS 244
Cdd:cd06103 161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      245 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 324
Cdd:cd06103 241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      325 KTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALG 404
Cdd:cd06103 321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                       410       420
                ....*....|....*....|....*.
4CTS_B      405 VLAQLIWSRALGFPLERPKSMSTDGL 430
Cdd:cd06103 401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
3-430 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B          3 STNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAK 82
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         83 GGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGI 162
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        163 HRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGN 242
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        243 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 322
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        323 LRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 402
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
4CTS_B        403 LGVLAQLIWSRALGFPLERPKSMSTDGL 430
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
6-430 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: 632.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRT 165
Cdd:cd06106  81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      166 KYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQ-FTELMRLYLTIHSDHEGGNVS 244
Cdd:cd06106 161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      245 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 324
Cdd:cd06106 241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      325 KTDPRYTCQREFALKH--LPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 402
Cdd:cd06106 321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                       410       420
                ....*....|....*....|....*...
4CTS_B      403 LGVLAQLIWSRALGFPLERPKSMSTDGL 430
Cdd:cd06106 401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
6-437 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 602.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         6 LKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 85
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        86 EPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-IHR 164
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       165 TKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSKLDWSHNFTNMLGYTDaQFTELMRLYLTIHSDHEGGNVS 244
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQPK-PYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       245 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 323
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       324 RKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 403
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
4CTS_B       404 GVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK 437
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
2-432 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 528.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         2 SSTNLKDILADLIPKEQARIKTFrqQHGNTVVGQITVDmmyGGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMLPK 80
Cdd:PLN02456  30 TGKDYESPLSELGPVQAERLKKI--KAGKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        81 akggeeplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAE 160
Cdd:PLN02456 105 ---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       161 GIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGaiDSKLDWSHNFTNMLGY-------TDAQFTELMRLYLT 233
Cdd:PLN02456 176 GQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP--DNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFI 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       234 IHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGR 313
Cdd:PLN02456 254 IHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KEIG---TVENIPEYVEGVKNSKK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       314 VVPGYGHAVLRKTDPRYTCQREFAL---KHLPHDPMFKLVAQLYKIVpnVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEm 390
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE- 403
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
4CTS_B       391 NYYTVLFGVSRALGVLAQliWSRALGFPLER---PKSMSTDGLIK 432
Cdd:PLN02456 404 EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTGEWLR 446
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
43-426 1.02e-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: 434.34  E-value: 1.02e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       43 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALP 121
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      122 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARayaegihrTKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIG 201
Cdd:cd06118  72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFAR--------DKSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      202 AIDSKLDWSHNFTNMLGY--TDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:cd06118 142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      280 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPH---DPMFKLVAQLYKI 356
Cdd:cd06118 221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      357 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 426
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.
44-423 4.75e-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: 381.85  E-value: 4.75e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B         44 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALP 121
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        122 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEgihrtKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 201
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKA-----DYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        202 AIDSKLDWSHNFTNML-GYT-DAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        280 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---HDPMFKLVAQLYK 355
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4CTS_B        356 IVPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 423
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
35-424 3.31e-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: 314.34  E-value: 3.31e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       35 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQIPTEEQVSWL 110
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      111 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGIHRTKywELIYEDCMDLIAKLPCVAAKIY 190
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      191 RnlYREGSSIGAIDSKLDWSHNFTNMLGYT--DAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 268
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      269 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPHDP 345
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      346 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 424
Cdd:COG0372 297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
43-426 2.92e-99

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: 297.30  E-value: 2.92e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       43 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQIPteeqvswlskewakraalp 121
Cdd:cd06101   1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAEN---------SSFEEVAYLLLTGELP------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      122 shvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegihrtkyweliyedcmdliaklpcvaakiyrnlyregssig 201
Cdd:cd06101     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      202 aidsklDWSHNFTNMLGY--TDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:cd06101  53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      280 EVLVWLTQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPH---DPMFKLVAQLYKI 356
Cdd:cd06101 126 AVLKMLEEIGTPK-----NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      357 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 426
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 ...
208-426 3.79e-91

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: 274.60  E-value: 3.79e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      208 DWSHNFTNMLGY--TDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 285
Cdd:cd06099   1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      286 TQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPH---DPMFKLVAQLYKIVPNVLL 362
Cdd:cd06099  80 EEIGTPK-----NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4CTS_B      363 EqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 426
Cdd:cd06099 155 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
56-427 1.08e-45

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: 162.60  E-value: 1.08e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       56 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 134
Cdd:cd06107  20 TYIDGDKGIlLYRGYPIEQ----LAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      135 LHPMSQLSAAITALNS---ESNFARAYAEGIHRTkywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSKLDWSH 211
Cdd:cd06107  91 AHPMGILCAGLSALSAfypEAIPAHTGDLYQNNP---EVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      212 NFTNMLGYTDAQ-------FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 284
Cdd:cd06107 166 NFLYMMGYVDQEpyepnprLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKM 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      285 LtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPHDPMFKLVAQLYKIVPNVl 361
Cdd:cd06107 245 L----REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED- 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4CTS_B      362 lEQGKAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQliWSRALGFPLE---RPKSMST 427
Cdd:cd06107 317 -EYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
56-416 1.81e-45

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


Pssm-ID: 99865  Cd Length: 373  Bit Score: 161.82  E-value: 1.81e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       56 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 134
Cdd:cd06112  16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      135 LHPMSQLSAAITALNSESNFARAYAEGihrTKYwelIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSKLDWSHNFT 214
Cdd:cd06112  87 GHPMDMLQATVAALGMFYPKPEVLKPN---PDY---IDAATVKLIAKMPTLVAMWAR--IRNGDDPIEPRPDLDYAENFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      215 NML--GYTDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEV 292
Cdd:cd06112 159 YMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----EEI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      293 GkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLP-----HDPMFKLVAQLYKIVPNVLLEQGKa 367
Cdd:cd06112 234 G---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFakmgeLSKLYEIALEVERLCEELLGHKGV- 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
4CTS_B      368 knpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 416
Cdd:cd06112 309 ---YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLG 351
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
46-410 1.30e-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: 1.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       46 RGMKGLVYETSVL---DPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALP 121
Cdd:cd06110   1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD----LAENSTFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      122 SHVVTMLDNFPTNLHPMSQLSAAITAL----------NSESNFARAyaegihrtkyweliyedcMDLIAKLPCVAAKIYR 191
Cdd:cd06110  72 AEIIDLLKLLPKDAHPMDVLRTAVSALalydpeaddmSREANLRKA------------------IRLIAKMPTIVAAFHR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      192 nlYREGSSIGAIDSKLDWSHNFTNMLGYT--DAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGL 269
Cdd:cd06110 134 --IRNGLEPVAPDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGAL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      270 AGPLHGLANQEVLVWLTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAL---KHLPHDPM 346
Cdd:cd06110 211 KGPLHGGANERVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRrlgKETGEPKW 283
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4CTS_B      347 FKLvaqLYKIVPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 410
Cdd:cd06110 284 YEM---SEAIEQAMRDE----KGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
56-418 2.90e-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: 140.27  E-value: 2.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       56 SVLDPDEGI-RFRGYSIPEcqkMLPKAKGGEeplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 134
Cdd:cd06115  40 SYIDGDKGIlRYRGYPIEE---LAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      135 LHPMSQLSAAITALNS---ESNFARAyAEGIHRTKywELIYEDCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSKLDWSH 211
Cdd:cd06115 111 AHPMGMLVSAISALSAfhpEANPALA-GQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      212 NFTNML-GYTDAQFTELMRL------YLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 284
Cdd:cd06115 186 NFLYMLdSLGERKYKPNPRLaraldiLFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      285 LTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlphDPMFKLVAQlykivpNVLLEQ 364
Cdd:cd06115 265 LA----EIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGK------DPLIEI 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4CTS_B      365 GKA-------------KNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQliWSRALGFP 418
Cdd:cd06115 326 AVAlekaalsdeyfvkRKLYPNVDFYSGLIYRAMGFpTDF--FPVLFAIPRMAGYLAH--WRESLDDP 389
gltA PRK05614
citrate synthase;
58-409 3.45e-37

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 140.40  E-value: 3.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        58 LDPDEGI-RFRGYSIpecqkmlpkakggeEPLPE-GLF----WLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNF 131
Cdd:PRK05614  62 IDGDKGIlLYRGYPI--------------EQLAEkSDFlevcYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGF 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       132 PTNLHPMSQLSAAITALnseSNFarayaegihrtkyweliYEDCMD-------------LIAKLPCVAAKIYRnlYREGS 198
Cdd:PRK05614 128 RRDAHPMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQ 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       199 SIGAIDSKLDWSHNFTNML-GY------TDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAG 271
Cdd:PRK05614 186 PFVYPRNDLSYAENFLRMMfATpceeyeVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWG 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       272 PLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTL--NSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPH-DP 345
Cdd:PRK05614 265 PAHGGANEAVLKML----EEIG---SVDNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELGLnDP 337
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
4CTS_B       346 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQL 409
Cdd:PRK05614 338 LLEVAMELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
60-407 4.91e-37

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: 139.71  E-value: 4.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       60 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVV-TMLDNFPTNl 135
Cdd:cd06113  33 PCPGkLYYRGYDVEDLVNGAQKENrfGFEE-----TAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      136 HPMSQLSAAITALNSesnfaraY---AEGIHRtkywELIYEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSKLD 208
Cdd:cd06113 107 DIMNKLQRSVLALYS-------YddkPDDISL----ENVLRQSIQLIARLPTIAVYAYQakRHYYDGESlyIHHPQPELS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      209 WSHNFTNMLgYTDAQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 284
Cdd:cd06113 176 TAENILSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEM 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      285 LTQLQKEVgKDVSDEK-LRDYIWNTLN------SGrVVPGYGHAVLRKTDPRYTCQREFAlKHLPH----DPMFKLVAQL 353
Cdd:cd06113 255 LEDIKENV-KDWTDEDeVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERI 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
4CTS_B      354 YKIVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 407
Cdd:cd06113 332 ERLAPEVIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCA 385
PRK14036 PRK14036
citrate synthase; Provisional
56-416 3.04e-36

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 137.01  E-value: 3.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        56 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTN 134
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       135 LHPMSQLSAAITALNSesNFARAyaeGIHRTKYwelIYEDCMDLIAKLPC-VAAkiyRNLYREGSSIGAIDSKLDWSHNF 213
Cdd:PRK14036  90 GHPMDALQASAAALGL--FYSRR---ALDDPEY---IRDAVVRLIAKIPTmVAA---FQLIRKGNDPIQPRDDLDYAANF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       214 TNMLG--YTDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKE 291
Cdd:PRK14036 159 LYMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML----EE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       292 VGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPHDPMFKLVAQLYKIVPNVLLEQGKak 368
Cdd:PRK14036 234 IG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI-- 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
4CTS_B       369 npWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 416
Cdd:PRK14036 309 --YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
58-427 1.46e-34

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


Pssm-ID: 99869  Cd Length: 384  Bit Score: 132.64  E-value: 1.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       58 LDPDEGI-RFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLH 136
Cdd:cd06116  22 IDGEKGIlRYRGYPIEQL---------AEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      137 PMSQLSAAITALNSESNFARAYAEGIHRTKyweliyeDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSKLDWSHNFTNM 216
Cdd:cd06116  93 PMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNFLSM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      217 LGY-------TDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 289
Cdd:cd06116 164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML---- 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      290 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPHDPMFKLVAQLYKIVPNVllEQGK 366
Cdd:cd06116 239 QQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIALED--EYFI 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4CTS_B      367 AKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 427
Cdd:cd06116 314 SRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14032 PRK14032
citrate synthase; Provisional
60-407 1.45e-33

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 130.79  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        60 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVV--TMLDNFPTN 134
Cdd:PRK14032  63 PDEGkLYYRGYDIKDLVNGFLKEKrfGFEE-----VAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrdMILKAPSKD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       135 LhpMSQLSAAITALNS-ESNfarayAEGIHRtkywELIYEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSKLDW 209
Cdd:PRK14032 138 I--MNSLARSVLALYSyDDN-----PDDTSI----DNVLRQSISLIARFPTLAVYAYQayRHYHDGKSlyIHPPKPELST 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       210 SHNFTNMLgYTDAQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 285
Cdd:PRK14032 207 AENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMF 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       286 TQLQKEVGKDVSDEKLRDYIWNTLN------SGRVVpGYGHAVLRKTDPRYTCQREFAlKHLPHDP----MFKLVAQLYK 355
Cdd:PRK14032 286 EDIKENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFA-EKLAKEKgreeEFNLYEKIEK 363
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
4CTS_B       356 IVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 407
Cdd:PRK14032 364 LAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVGWSA 415
PRK14034 PRK14034
citrate synthase; Provisional
46-410 1.81e-29

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 117.94  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        46 RGMKGLVYETSVLDP--DEGIRFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSH 123
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       124 VVTMLDNFPTN-LHPMSQLSAAITALNSESNFARAYAEgihrtkywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGA 202
Cdd:PRK14034  76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDE--------EANYRKAVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       203 IDSKLDWSHNFTNMLG--YTDAQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 280
Cdd:PRK14034 146 PRKDLSLAANFLYMLNgeEPDEVEVEAFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       281 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA--LKHLPHDPM-FKLVAQLYKIV 357
Cdd:PRK14034 225 VMKMLTEIGEE-------ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
4CTS_B       358 PNvlleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 410
Cdd:PRK14034 298 TK-------EKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHIL 342
PRK14035 PRK14035
citrate synthase; Provisional
46-409 2.89e-26

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 109.08  E-value: 2.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        46 RGMKGLVY-ETSVLD-PDEGIRFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSH 123
Cdd:PRK14035   5 RGLEGVIAaETKISSiIDSQLTYAGYDIDDLA---------ENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       124 VVTMLDNFPT-NLHPMSQLSAAITALNSESNFARAYAEgihrtkywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGA 202
Cdd:PRK14035  76 VYQHFEEYSTdHVHPMTALRTSVSYLAHFDPDAEEESD--------EARYERAIRIQAKVASLVTAFAR--VRQGKEPLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       203 IDSKLDWSHNFTNMLG---YTDAQfTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:PRK14035 146 PRPDLSYAANFLYMLRgelPTDIE-VEAFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       280 EVLVWLTQLqKEVGkDVSdeklrDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALK---HLPHDPMFKLVAQLYKI 356
Cdd:PRK14035 224 RVMDMLSEI-RSIG-DVD-----AYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKitkGTGREELFEMSVKIEKR 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
4CTS_B       357 VPnvlleqgKAKNPWPNVDAHSGVLlqYYGM-TEMNYYTVLFGVSRALGVLAQL 409
Cdd:PRK14035 297 MK-------EEKGLIPNVDFYSATV--YHVMgIPHDLFTPIFAVSRVAGWIAHI 341
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
90-414 4.55e-26

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 108.50  E-value: 4.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        90 EGLFWLLVTGQIPTEEQVSWLSK-EWAKRAALPShVVTMLDNFPTNLHPMSQLSAAITALNSESnfarAYAEGIHRtkyw 168
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQrERAYRRLDRS-VLSLIDKLPTTCHPMDVVRTAVSYLGAED----PEADDSSP---- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       169 ELIYEDCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSKLDWSHNFTNMLgYTDAQFTELMRLY---LTIHSDHeGGNVSA 245
Cdd:PRK14033 121 EANLAKALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMC-FGEVPEPEVVRAFevsLILYAEH-SFNAST 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       246 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 325
Cdd:PRK14033 197 FTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKH 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       326 TDPRYTCQREfALKHLPHDPMFKLVAQLYKIVPNVLLEqgkAKNPWPNVDAHSGVLlqYYGM---TEMnyYTVLFGVSRA 402
Cdd:PRK14033 270 GDSRVPTMKA-ALRRVAAVRDGQRWLDIYEALEKAMAE---ATGIKPNLDFPAGPA--YYLMgfdIDF--FTPIFVMSRI 341
                        330
                 ....*....|..
4CTS_B       403 LGVLAQLIWSRA 414
Cdd:PRK14033 342 TGWTAHIMEQRA 353
PRK12349 PRK12349
citrate synthase;
47-410 2.11e-25

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 106.73  E-value: 2.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        47 GMKGLVY-ET--SVLDPDEG-IRFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPS 122
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       123 HVVTMLDNFPTNLHPMSQLSAAITAL----------NSESNFARAYaegihrtkyweliyedcmDLIAKLPCVAAKIYRN 192
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALagydndiedrSLEVNKSRAY------------------KLLSKVPNIVANSYHI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       193 LyrEGSSIGAIDSKLDWSHNFTNML-GYTDAQF-TELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFAAAMNGLA 270
Cdd:PRK12349 141 L--NNEEPIEPLKELSYSANFLYMLtGKKPTELeEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       271 GPLHGLANQEVLVWLTQlqkevGKDVSD-EKLrdyIWNTLNSGRVVPGYGHAV-LRKTDPRYTCQREfALKHLPHDpmfK 348
Cdd:PRK12349 218 GSLHGGANEAVMYMLLE-----AGTVEKfEEL---LQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLCDV---K 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4CTS_B       349 LVAQLYKivpnvLLEQG-----KAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLI 410
Cdd:PRK12349 286 GDYTLYE-----MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
PRK14037 PRK14037
citrate synthase; Provisional
58-410 3.65e-22

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 97.51  E-value: 3.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        58 LDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLH 136
Cdd:PRK14037  21 IDGEKGIlRYRGYNIED----LVNYGSYEE-----TIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       137 PMSQLSAAITALNSESNfarayaegihRTKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSKLDWSHNFTN- 215
Cdd:PRK14037  92 AIGLMEAAFAALASIDK----------NFKWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLLa 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       216 -MLGYTDAQFTELMRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVlvwLTQLQkEV 292
Cdd:PRK14037 160 sFAREPTAEEIKAMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEA---FKQFV-EI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       293 GK-DVSDEKLRDyiwNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPW 371
Cdd:PRK14037 233 GDpNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGIY 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
4CTS_B       372 PNVDAHSGVLlqYYGMT-EMNYYTVLFGVSRALGVLAQLI 410
Cdd:PRK14037 310 PNTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
63-414 2.30e-20

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: 91.98  E-value: 2.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       63 GIRFRGYSIpecqKMLPKAKGGEEplpegLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQL- 141
Cdd:cd06108  22 GLTYRGYDI----EDLAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMr 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      142 --SAAITALNSESNFARAYAEGIHrtkyweliyedcmdLIAKLPCVAAKIYRnLYREGSSIGAIDSKLDWSHNFTNML-G 218
Cdd:cd06108  93 tgCSMLGCLEPENEFSQQYEIAIR--------------LLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLhG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      219 YTDAQ-FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQkevgkdvS 297
Cdd:cd06108 158 KKPGElEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-------S 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      298 DEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPHDPMFKLvaqLYKI---VPNVLLEQgkaKNPWPNV 374
Cdd:cd06108 230 PEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPL---LYQIserIEEVMWEE---KKLFPNL 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
4CTS_B      375 DAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRA 414
Cdd:cd06108 303 DFYSASAYHFCGIpTEL--FTPIFVMSRVTGWAAHIMEQRA 341
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
46-424 4.86e-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: 87.75  E-value: 4.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       46 RGMKGLV-YETSVLDPD--EG-IRFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQIPTEEQVSWLSKEWAKRAALP 121
Cdd:cd06109   1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED----LAGSASFEDVA-----ALLWNGFFPDLPELEEFRAALAAARALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      122 SHVVTMLDNFpTNLHPMSQLSAAITALNSESNFARAyaegihrtkyweliyedcMDLIAKLPCVAAKIYRnlYREGSSIG 201
Cdd:cd06109  72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDLATA------------------LRLLAAAPVITAALLR--LSRGKQPI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      202 AIDSKLDWSHNFTNML--GYTDAQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 279
Cdd:cd06109 131 APDPSLSHAADYLRMLtgEPPSEAHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      280 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREfALKHLP-HDPMFKLVAQLYKIVP 358
Cdd:cd06109 210 PVLDML----DAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGaPDERLEFAEAVEQAAL 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4CTS_B      359 NVLLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 424
Cdd:cd06109 282 ALLREYKPGRPLETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
64-413 2.52e-13

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


Pssm-ID: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 71.03  E-value: 2.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       64 IRFRGYSIpecqkmLPKAKGGEEplpEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSA 143
Cdd:cd06117  23 LHYRGYDI------LDLAEKCEF---EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      144 AITALNSESNFARAYAEGIHRtkyweliyeDCMD-LIAKLPCVAAKIYrNLYREGSSIGAIDSKLDWSHNFTNML-GYTD 221
Cdd:cd06117  94 GVSVLGCVLPEKEDHPVSGAR---------DIADrLMASLGSILLYWY-HYSHNGKRIEVETDDDSIGGHFLHLLhGEKP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      222 AQ-FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGKdvSDEK 300
Cdd:cd06117 164 SEsWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAF----EIQQRYES--ADEA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B      301 LRDyIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPHDPMFKLVAQLYKIVPNVLLEQGKAknpWPNVDAHSGV 380
Cdd:cd06117 237 EAD-IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGGDMKMFDIAERLETVMWEEKKM---FPNLDWFSAV 311
                       330       340       350
                ....*....|....*....|....*....|....
4CTS_B      381 LLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSR 413
Cdd:cd06117 312 SYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12351 PRK12351
methylcitrate synthase; Provisional
95-414 4.69e-10

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 61.09  E-value: 4.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B        95 LLVTGQIPTEEQV-SWLSKEWAKRAaLPSHVVTMLDNFPTNLHPMSQLSAAITAL------NSESNFARAYaegihrtky 167
Cdd:PRK12351  54 LLVHGKLPTQAELaAYKTKLKALRG-LPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR--------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       168 weliyeDCMD-LIAKLPCVAAKIYR--------NLYREGSSIGAidskldwsHnFTNMLgyTDAQFTEL----MRLYLTI 234
Cdd:PRK12351 124 ------DIADrLLASLGSILLYWYHyshngrriEVETDDDSIGG--------H-FLHLL--HGKKPSESwvkaMHTSLIL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       235 HSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANqEVLVwltQLQKevGKDVSDEKLRDyIWNTLNSGRV 314
Cdd:PRK12351 187 YAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQ--RYDTPDEAEAD-IRRRVENKEV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       315 VPGYGHAVLRKTDPRYTCQREFALkhlphdpmfKLVA-----QLYKI---VPNVLLEQgkaKNPWPNVDAHSGVllQYYG 386
Cdd:PRK12351 259 VIGFGHPVYTISDPRNKVIKEVAK---------KLSKeagdtKLYDIaerLETVMWEE---KKMFPNLDWFSAV--SYHM 324
                        330       340       350
                 ....*....|....*....|....*....|.
4CTS_B       387 M---TEMnyYTVLFGVSRALGVLAQLIWSRA 414
Cdd:PRK12351 325 MgvpTAM--FTPLFVISRTTGWAAHVIEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
204-424 7.84e-09

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 56.90  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       204 DSKLDWSHNFTNML-----GYTDAQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLAN 278
Cdd:PRK12350 129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4CTS_B       279 QEVLVWLTqlqkEVGKDvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREfALKHLPhDPMFKLVAQLYKIVp 358
Cdd:PRK12350 208 ARVLPMLD----AVERT---GDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRLG-APRYEVAEAVEQAA- 277
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4CTS_B       359 nvlLEQGKAKNP----WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 424
Cdd:PRK12350 278 ---LAELRERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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