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Conserved domains on  [gi|62859899|ref|NP_001017313|]
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citrate synthase, mitochondrial precursor [Xenopus tropicalis]

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 ...
35-462 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: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKT 194
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 195 KYWELIYEDSMDLIAKLPCVAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 274
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 275 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 354
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 355 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALGV 434
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 62859899 435 LAQLIWSRALGFPLERPKSMSTDGLMQL 462
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 ...
35-462 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: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKT 194
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 195 KYWELIYEDSMDLIAKLPCVAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 274
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 275 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 354
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 355 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALGV 434
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 62859899 435 LAQLIWSRALGFPLERPKSMSTDGLMQL 462
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
32-459 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: 777.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899    32 SANLKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAP 111
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   112 GGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGV 191
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   192 NKTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 271
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   272 VSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAV 351
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   352 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRA 431
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 62859899   432 LGVLAQLIWSRALGFPLERPKSMSTDGL 459
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
35-466 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 619.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEG-VNK 193
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  194 TKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 273
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  274 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVS-DEKLRDYIWNTLNSGRVVPGYGHAVL 352
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  353 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRAL 432
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 62859899  433 GVLAQLIWSRALGFPLERPKSMSTDGLMQLVGSK 466
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
73-452 8.94e-132

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


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 384.94  E-value: 8.94e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899    73 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPEcqkLLPKAPggeeplPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPS 151
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   152 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFArgyaeGVNKTKYWELIYEDsmDLIAKLPCVAAKIYRnlYREGSSIGA 231
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   232 IDSNLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 309
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   310 VLVWLtslqKDLGgevSDEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 385
Cdd:pfam00285 222 VLEML----EEIG---SPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62859899   386 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 452
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
64-453 5.92e-105

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: 317.42  E-value: 5.92e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  64 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkllpkapggEEPLPEGLFWLLVTGEAPSQEQVNWI 139
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 140 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFargYAEGVNKTKywELIYEDSMDLIAKLPCVAAKIY 219
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 220 RnlYREGSSIGAIDSNLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNG 297
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 298 LAGPLHGLANQEVLVWLtslqKDLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 374
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62859899 375 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 453
Cdd:COG0372 297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
35-462 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: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKT 194
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 195 KYWELIYEDSMDLIAKLPCVAAKIYRNLYReGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 274
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 275 HTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 354
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 355 TDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALGV 434
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*...
gi 62859899 435 LAQLIWSRALGFPLERPKSMSTDGLMQL 462
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
35-459 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: 808.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEG-VNK 193
Cdd:cd06103  81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 194 TKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVS 273
Cdd:cd06103 161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 274 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 353
Cdd:cd06103 241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 354 KTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALG 433
Cdd:cd06103 321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                       410       420
                ....*....|....*....|....*.
gi 62859899 434 VLAQLIWSRALGFPLERPKSMSTDGL 459
Cdd:cd06103 401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
32-459 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: 777.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899    32 SANLKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAP 111
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   112 GGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGV 191
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   192 NKTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 271
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   272 VSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAV 351
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   352 LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRA 431
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 62859899   432 LGVLAQLIWSRALGFPLERPKSMSTDGL 459
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
35-459 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: 627.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKT 194
Cdd:cd06106  81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 195 KYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGYTDPQ-FTELMRLYLTIHSDHEGGNVS 273
Cdd:cd06106 161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 274 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 353
Cdd:cd06106 241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 354 KTDPRYTCQREFALKH--LPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRA 431
Cdd:cd06106 321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                       410       420
                ....*....|....*....|....*...
gi 62859899 432 LGVLAQLIWSRALGFPLERPKSMSTDGL 459
Cdd:cd06106 401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
35-466 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 619.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   35 LKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGE 114
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  115 EPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEG-VNK 193
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  194 TKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIgAIDSNLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 273
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  274 AHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVS-DEKLRDYIWNTLNSGRVVPGYGHAVL 352
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  353 RKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRAL 432
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 62859899  433 GVLAQLIWSRALGFPLERPKSMSTDGLMQLVGSK 466
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
11-461 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   11 ARILGAKNSPCALIAARQASSSANLKDV--LSDLIPKEQTRIKNFrqQYGKNVIGQITVDmmyGGMRGMKGLVYETSVLD 88
Cdd:PLN02456   8 SSSLSRAAPGGGSGSLTIVDNRTGKDYEspLSELGPVQAERLKKI--KAGKDDLGLKTVD---PGYRNTAPVLSEISLID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   89 PDEGI-RFRGYSIPECQKLLPKapggeeplpEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPM 167
Cdd:PLN02456  83 GDEGIlRFRGYPIEELAEKSPF---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  168 SQLSAAITALNSESNFARGYAEGVNKTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGaiDSNLDWSHNFTNMLG 247
Cdd:PLN02456 154 TQLVSGVMALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP--DNSLDYAENFLYMLG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  248 Y-------TDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtslqKD 320
Cdd:PLN02456 232 SlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KE 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  321 LGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLVAQLYKIVpnVLLEQGKAK 397
Cdd:PLN02456 308 IG---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVR 382
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62859899  398 NPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQliWSRALGFPLER---PKSMSTDGLMQ 461
Cdd:PLN02456 383 KLYPNVDFYSGVLLRALGFPE-EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTGEWLR 446
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
72-455 8.25e-149

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: 428.17  E-value: 8.25e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  72 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQkllpkapggEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALP 150
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELA---------EKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 151 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFArgyaegvnKTKYWELIYEDSMDLIAKLPCVAAKIYRnlYREGSSIG 230
Cdd:cd06118  72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFA--------RDKSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 231 AIDSNLDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 308
Cdd:cd06118 142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 309 EVLVWLTSLQkdlggevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 385
Cdd:cd06118 221 AVLKMLLEIG-------TPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 386 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMkEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 455
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.
73-452 8.94e-132

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


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 384.94  E-value: 8.94e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899    73 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPEcqkLLPKAPggeeplPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPS 151
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   152 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFArgyaeGVNKTKYWELIYEDsmDLIAKLPCVAAKIYRnlYREGSSIGA 231
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPIY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   232 IDSNLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 309
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   310 VLVWLtslqKDLGgevSDEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYTCQREFALKHLP---NDPMFKLVAQLYKI 385
Cdd:pfam00285 222 VLEML----EEIG---SPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62859899   386 VPNVLLEQGkaKNPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 452
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
64-453 5.92e-105

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: 317.42  E-value: 5.92e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  64 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkllpkapggEEPLPEGLFWLLVTGEAPSQEQVNWI 139
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 140 SKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFargYAEGVNKTKywELIYEDSMDLIAKLPCVAAKIY 219
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 220 RnlYREGSSIGAIDSNLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNG 297
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 298 LAGPLHGLANQEVLVWLtslqKDLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDP 374
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62859899 375 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 453
Cdd:COG0372 297 LLEIAEELEEVALED--EYFIEKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
72-455 9.76e-98

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: 294.61  E-value: 9.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  72 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQkllpkapggEEPLPEGLFWLLVTGEAPsqeqvnwiskewakraalp 150
Cdd:cd06101   1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELA---------ENSSFEEVAYLLLTGELP------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 151 shvvtmldnfptnlhpmsqlsaaitalnsesnfargyaegvnktkyweliyedsmdliaklpcvaakiyrnlyregssig 230
Cdd:cd06101     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 231 aidsnlDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 308
Cdd:cd06101  53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 309 EVLVWLTSLqkdlgGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKI 385
Cdd:cd06101 126 AVLKMLEEI-----GTPKNEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 386 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMkEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 455
Cdd:cd06101 201 APEVLYE----KKLYPNVDFYSGVLYKAMGF-PTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
237-455 2.25e-90

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


Pssm-ID: 99853 [Multi-domain]  Cd Length: 213  Bit Score: 273.83  E-value: 2.25e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 237 DWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWL 314
Cdd:cd06099   1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 315 TSLqkdlgGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN---DPMFKLVAQLYKIVPNVLL 391
Cdd:cd06099  80 EEI-----GTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62859899 392 EqgkaKNPWPNVDAHSGVLLQYYGMkEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 455
Cdd:cd06099 155 E----KKLYPNVDFYSGVLYKAMGF-PTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
85-456 9.86e-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: 160.68  E-value: 9.86e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  85 SVLDPDEGI-RFRGYSIPECqkllpkapgGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTN 163
Cdd:cd06107  20 TYIDGDKGIlLYRGYPIEQL---------AESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 164 LHPMSQLSAAITALNSESNFARGYAEGVNKTKYWELIYEDSMDLIAKLPCVAAKIYRnlYREGSSIGAIDSNLDWSHNFT 243
Cdd:cd06107  91 AHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNPEVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIENFL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 244 NMLGYTD-------PQFTELMRLYLTIHSDHEgGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTS 316
Cdd:cd06107 169 YMMGYVDqepyepnPRLARALDRLWILHADHE-MNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLRE 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 317 LQkdlggevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVllEQ 393
Cdd:cd06107 248 IG-------TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED--EY 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62859899 394 GKAKNPWPNVDAHSGVLLQYYGMkEMNYYTVLFGVSRALGVLAQliWSRALGFPLE---RPKSMST 456
Cdd:cd06107 319 FVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
85-445 1.66e-44

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: 159.90  E-value: 1.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  85 SVLDPDEGI-RFRGYSIPEcqklLPKAPGGEEplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTN 163
Cdd:cd06112  16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 164 LHPMSQLSAAITALNSesnFARGYAEGVNKTKYwelIYEDSMDLIAKLPCVAAKIYRnlYREGSSIGAIDSNLDWSHNFT 243
Cdd:cd06112  87 GHPMDMLQATVAALGM---FYPKPEVLKPNPDY---IDAATVKLIAKMPTLVAMWAR--IRNGDDPIEPRPDLDYAENFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 244 NML--GYTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtslqKDL 321
Cdd:cd06112 159 YMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----EEI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 322 GgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPN-----DPMFKLVAQLYKIVPNVLLEQGKa 396
Cdd:cd06112 234 G---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKGV- 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 62859899 397 knpWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQliWSRALG 445
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 ...
75-439 4.74e-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: 158.21  E-value: 4.74e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  75 RGMKGLVYETSVL---DPDEGI-RFRGYSIPEcqklLPKAPGGEEPLpeglfWLLVTGEAPSQEQVNWISKEWAKRAALP 150
Cdd:cd06110   1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD----LAENSTFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 151 SHVVTMLDNFPTNLHPMSQLSAAITALnsesnfARGYAEGVNKTKywELIYEDSMDLIAKLPCVAAKIYRnlYREGSSIG 230
Cdd:cd06110  72 AEIIDLLKLLPKDAHPMDVLRTAVSAL------ALYDPEADDMSR--EANLRKAIRLIAKMPTIVAAFHR--IRNGLEPV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 231 AIDSNLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 308
Cdd:cd06110 142 APDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 309 EVLVWLTslqkDLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAL---KHLPNDPMFKLvaqLYKI 385
Cdd:cd06110 221 RVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRrlgKETGEPKWYEM---SEAI 290
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 62859899 386 VPNVLLEqgkaKNPWPNVDAHSGVLLQYYGMkEMNYYTVLFGVSRALGVLAQLI 439
Cdd:cd06110 291 EQAMRDE----KGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
gltA PRK05614
citrate synthase;
87-438 1.24e-39

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 147.72  E-value: 1.24e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   87 LDPDEGI-RFRGYSIpecqkllpkapggeEPLPE-GLF----WLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNF 160
Cdd:PRK05614  62 IDGDKGIlLYRGYPI--------------EQLAEkSDFlevcYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGF 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  161 PTNLHPMSQLSAAITALnseSNFargyaegvnktkyweliYEDSMD-------------LIAKLPCVAAKIYRnlYREGS 227
Cdd:PRK05614 128 RRDAHPMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQ 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  228 SIGAIDSNLDWSHNFTNML-GY------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAG 300
Cdd:PRK05614 186 PFVYPRNDLSYAENFLRMMfATpceeyeVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWG 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  301 PLHGLANQEVLVWLtslqKDLGgevSDEKLRDYIWNTL--NSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHL-PNDP 374
Cdd:PRK05614 265 PAHGGANEAVLKML----EEIG---SVDNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDP 337
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62859899  375 MFKLVAQLYKIVPNVllEQGKAKNPWPNVDAHSGVLLQYYGM-KEMnyYTVLFGVSRALGVLAQL 438
Cdd:PRK05614 338 LLEVAMELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
85-447 3.25e-36

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: 138.34  E-value: 3.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  85 SVLDPDEGI-RFRGYSIPEcqkLLPKAPGGEeplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTN 163
Cdd:cd06115  40 SYIDGDKGIlRYRGYPIEE---LAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 164 LHPMSQLSAAITALNS---ESNFARGyAEGVNKTKywELIYEDSMDLIAKLPCVAAKIYRNlyREGSSIGAIDSNLDWSH 240
Cdd:cd06115 111 AHPMGMLVSAISALSAfhpEANPALA-GQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 241 NFTNML---GYTD----PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVW 313
Cdd:cd06115 186 NFLYMLdslGERKykpnPRLARALDILFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 314 LTSLqkdlgGEVsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlpnDPMFKLVAQlykivpNVLLEQ 393
Cdd:cd06115 265 LAEI-----GTV--ENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGK------DPLIEI 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62859899 394 GKA-------------KNPWPNVDAHSGVLLQYYGMKeMNYYTVLFGVSRALGVLAQliWSRALGFP 447
Cdd:cd06115 326 AVAlekaalsdeyfvkRKLYPNVDFYSGLIYRAMGFP-TDFFPVLFAIPRMAGYLAH--WRESLDDP 389
PRK14036 PRK14036
citrate synthase; Provisional
85-445 3.42e-35

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 134.70  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   85 SVLDPDEGI-RFRGYSIPEcqklLPKAPGGEEPLpeglfWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTN 163
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  164 LHPMSQLSAAITALNSesnFargYA-EGVNKTKYwelIYEDSMDLIAKLPC-VAAkiyRNLYREGSSIGAIDSNLDWSHN 241
Cdd:PRK14036  90 GHPMDALQASAAALGL---F---YSrRALDDPEY---IRDAVVRLIAKIPTmVAA---FQLIRKGNDPIQPRDDLDYAAN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  242 FTNMLG--YTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtslqK 319
Cdd:PRK14036 158 FLYMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML----E 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  320 DLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVLLEQGKa 396
Cdd:PRK14036 233 EIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI- 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 62859899  397 knpWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQliWSRALG 445
Cdd:PRK14036 309 ---YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
87-456 1.99e-33

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: 129.95  E-value: 1.99e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  87 LDPDEGI-RFRGYSIpecQKLLPKAPGGEeplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLH 165
Cdd:cd06116  22 IDGEKGIlRYRGYPI---EQLAEQSSYLE------VAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 166 PMSQLSAAITALNSESNFARGYAEGVNKTKyweliyeDSMDLIAKLPCVAAKIYRnlYREGSSIGAIDSNLDWSHNFTNM 245
Cdd:cd06116  93 PMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNFLSM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 246 LGY-------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtslq 318
Cdd:cd06116 164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML---- 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 319 KDLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA---LKHLPNDPMFKLVAQLYKIVPNVllEQGK 395
Cdd:cd06116 239 QQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIALED--EYFI 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62859899 396 AKNPWPNVDAHSGVLLQYYGMKeMNYYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 456
Cdd:cd06116 314 SRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14032 PRK14032
citrate synthase; Provisional
89-436 2.19e-32

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 128.10  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   89 PDEG-IRFRGYSIPE----CQKllPKAPGGEEplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVV--TMLDNFP 161
Cdd:PRK14032  63 PDEGkLYYRGYDIKDlvngFLK--EKRFGFEE-----VAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrdMILKAPS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  162 TNLhpMSQLSAAITALNSesnfargYAEGVNKTKYWELIyEDSMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSNLD 237
Cdd:PRK14032 136 KDI--MNSLARSVLALYS-------YDDNPDDTSIDNVL-RQSISLIARFPTLAVYAYQayRHYHDGKSlyIHPPKPELS 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  238 WSHNFTNMLgYTDPQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVlvw 313
Cdd:PRK14032 206 TAENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKV--- 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  314 lTSLQKDLGGEVSD----EKLRDYIWNTLN------SGRVVpGYGHAVLRKTDPRYTCQREFAL-----KHLPNDpmFKL 378
Cdd:PRK14032 282 -MEMFEDIKENVKDwedeDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNL 357
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62859899  379 VAQLYKIVPNVLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----KEMnyYTVLFGVSRALGVLA 436
Cdd:PRK14032 358 YEKIEKLAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVGWSA 415
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
89-436 1.42e-31

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: 125.07  E-value: 1.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  89 PDEG-IRFRGYSIPEcqkLLPKAPGGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVV-TMLDNFPTNlHP 166
Cdd:cd06113  33 PCPGkLYYRGYDVED---LVNGAQKENRFGFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK-DI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 167 MSQLSAAITALNSesnfargYAEGVNKTKYWELIYEdSMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSNLDWSHNF 242
Cdd:cd06113 109 MNKLQRSVLALYS-------YDDKPDDISLENVLRQ-SIQLIARLPTIAVYAYQakRHYYDGESlyIHHPQPELSTAENI 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 243 TNMLgYTDPQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQ 318
Cdd:cd06113 181 LSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIK 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 319 KDLGGEVSDEKLRDYIWNTLN------SGrVVPGYGHAVLRKTDPRYTCQREFAlKHLPN----DPMFKLVAQLYKIVPN 388
Cdd:cd06113 260 ENVKDWTDEDEVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERIERLAPE 337
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 62859899 389 VLLEQ-GKAKNPWPNVDAHSGVLlqyYGM----KEMnyYTVLFGVSRALGVLA 436
Cdd:cd06113 338 VIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCA 385
PRK14034 PRK14034
citrate synthase; Provisional
75-439 2.84e-30

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 121.03  E-value: 2.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   75 RGMKGLVYETSVLDP--DEGIRFRGYSIPECqkllpkapgGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSH 152
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  153 VVTMLDNFPTN-LHPMSQLSAAITALNSESNFARGYAEGVNKTKyweliyedSMDLIAKLPCVAAKIYRnlYREGSSIGA 231
Cdd:PRK14034  76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDEEANYRK--------AVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  232 IDSNLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 309
Cdd:PRK14034 146 PRKDLSLAANFLYMLNGEEPDEVEVeaFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  310 VLVWLTSLqkdlgGEVsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFA--LKHLPNDPM-FKLVAQLYKIV 386
Cdd:PRK14034 225 VMKMLTEI-----GEE--ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 62859899  387 PNvlleqgkAKNPWPNVDAHSGVLLQYYGMKEmNYYTVLFGVSRALGVLAQLI 439
Cdd:PRK14034 298 TK-------EKGLPPNVDFYSASVYHCLGIDH-DLFTPIFAISRMSGWLAHIL 342
PRK14035 PRK14035
citrate synthase; Provisional
75-438 1.38e-26

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 110.23  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   75 RGMKGLVY-ETSVLD-PDEGIRFRGYSIPECQkllpkapggEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSH 152
Cdd:PRK14035   5 RGLEGVIAaETKISSiIDSQLTYAGYDIDDLA---------ENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  153 VVTMLDNFPT-NLHPMSQLSAAITALNSESNFARGYAEgvnktkywELIYEDSMDLIAKLPCVAAKIYRnlYREGSSIGA 231
Cdd:PRK14035  76 VYQHFEEYSTdHVHPMTALRTSVSYLAHFDPDAEEESD--------EARYERAIRIQAKVASLVTAFAR--VRQGKEPLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  232 IDSNLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 309
Cdd:PRK14035 146 PRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANER 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  310 VLVWLTSLqkdlgGEVSDekLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNV 389
Cdd:PRK14035 225 VMDMLSEI-----RSIGD--VDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMS-RKITKGTGREELFEMSVKIEKR 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 62859899  390 LLEQgkaKNPWPNVDAHSGVLlqYYGMK-EMNYYTVLFGVSRALGVLAQL 438
Cdd:PRK14035 297 MKEE---KGLIPNVDFYSATV--YHVMGiPHDLFTPIFAVSRVAGWIAHI 341
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
119-443 6.19e-26

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 108.50  E-value: 6.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  119 EGLFWLLVTGEAPSQEQVNWISK-EWAKRAALPShVVTMLDNFPTNLHPMSQLSAAITALNSESnfargyAEGVNKTKyw 197
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQrERAYRRLDRS-VLSLIDKLPTTCHPMDVVRTAVSYLGAED------PEADDSSP-- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  198 ELIYEDSMDLIAKLPCVAAKIYRNlyREGSSIGAIDSNLDWSHNFTNM-LG-YTDPQFTELMRLYLTIHSDHeGGNVSAH 275
Cdd:PRK14033 121 EANLAKALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  276 TSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLtslqKDLGgevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKT 355
Cdd:PRK14033 198 TARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTM----LEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHG 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  356 DPRYTCQREfALKHLPNDPMFKLVAQLYKIVPNVLLEqgkAKNPWPNVDAHSGVLlqYYGMK-EMNYYTVLFGVSRALGV 434
Cdd:PRK14033 271 DSRVPTMKA-ALRRVAAVRDGQRWLDIYEALEKAMAE---ATGIKPNLDFPAGPA--YYLMGfDIDFFTPIFVMSRITGW 344

                 ....*....
gi 62859899  435 LAQLIWSRA 443
Cdd:PRK14033 345 TAHIMEQRA 353
PRK14037 PRK14037
citrate synthase; Provisional
87-439 2.29e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 101.36  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   87 LDPDEGI-RFRGYSIPEcqklLPKAPGGEEplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLH 165
Cdd:PRK14037  21 IDGEKGIlRYRGYNIED----LVNYGSYEE-----TIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  166 PMSQLSAAITALnsesnfargyAEGVNKTKYWELIYEDSMDLIAKLPCVAAKIYRnlYREGSSIGAIDSNLDWSHNFTNM 245
Cdd:PRK14037  92 AIGLMEAAFAAL----------ASIDKNFKWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  246 LGYTDPQFTEL--MRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFSAAMNGLAGPLHGLANQEVLvwltsLQKDL 321
Cdd:PRK14037 160 SFAREPTAEEIkaMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAF-----KQFVE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  322 GGEVS--DEKLRDyiwNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNP 399
Cdd:PRK14037 232 IGDPNnvEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGI 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 62859899  400 WPNVDAHSGVLlqYYGMK-EMNYYTVLFGVSRALGVLAQLI 439
Cdd:PRK14037 309 YPNTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
PRK12349 PRK12349
citrate synthase;
76-439 2.79e-23

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 100.95  E-value: 2.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899   76 GMKGLVY-ET--SVLDPDEG-IRFRGYSIPEcqklLPKAPGGEEplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPS 151
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  152 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKTKyweliyedSMDLIAKLPCVAAKIYRNLyrEGSSIGA 231
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSR--------AYKLLSKVPNIVANSYHIL--NNEEPIE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  232 IDSNLDWSHNFTNMLGYTDP--QFTELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQE 309
Cdd:PRK12349 149 PLKELSYSANFLYMLTGKKPteLEEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  310 VLVWLtslqkdLGGEVSDEKLRdYIWNTLNSGRVVPGYGHAV-LRKTDPRYTCQREfALKHL---PNDpmfklvAQLYKi 385
Cdd:PRK12349 228 VMYML------LEAGTVEKFEE-LLQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcdvKGD------YTLYE- 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62859899  386 vpnvLLEQG-----KAKNPWPNVDAHSGVLLQYYGMKeMNYYTVLFGVSRALGVLAQLI 439
Cdd:PRK12349 293 ----MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
75-453 2.07e-18

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


Pssm-ID: 99862 [Multi-domain]  Cd Length: 349  Bit Score: 86.21  E-value: 2.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  75 RGMKGLV-YETSVLDPD--EG-IRFRGYSIPEcqkLLPKAPGgeeplpEGLFWLLVTGEAPSQEQVNWISKEWAKRAALP 150
Cdd:cd06109   1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED---LAGSASF------EDVAALLWNGFFPDLPELEEFRAALAAARALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 151 SHVVTMLDNFpTNLHPMSQLSAAITALNSESNFargyaegvnktkyweliyEDSMDLIAKLPCVAAKIYRnlYREGSSIG 230
Cdd:cd06109  72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDL------------------ATALRLLAAAPVITAALLR--LSRGKQPI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 231 AIDSNLDWSHNFTNML-GYTDPQ-FTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQ 308
Cdd:cd06109 131 APDPSLSHAADYLRMLtGEPPSEaHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 309 EVLVWLTSLQkdlggevSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREfALKHLPNDPMFKLVAQLYKIVPN 388
Cdd:cd06109 210 PVLDMLDAIG-------TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGAPDERLEFAEAVEQAAL 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62859899 389 VLLEQGKAKNP-WPNVDAHSGVLLQYYGMK-EMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 453
Cdd:cd06109 282 ALLREYKPGRPlETNVEFYTALLLEALGLPrEA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
92-443 5.03e-18

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: 85.43  E-value: 5.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  92 GIRFRGYSIPEcqklLPKAPGGEEplpegLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLS 171
Cdd:cd06108  22 GLTYRGYDIED----LAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 172 AAITALnsesnfarGYAEGVNKTKYWeliYEDSMDLIAKLPCVAAKIYRnLYREGSSIGAIDSNLDWSHNFTNMLGYTDP 251
Cdd:cd06108  93 TGCSML--------GCLEPENEFSQQ---YEIAIRLLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLHGKKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 252 --QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQkdlggevSDEK 329
Cdd:cd06108 161 geLEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-------SPEE 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 330 LRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN--DPMfklvaqLYKI---VPNVLLEQgkaKNPWPNVD 404
Cdd:cd06108 233 AEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEggDPL------LYQIserIEEVMWEE---KKLFPNLD 303
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 62859899 405 AHSGVLLQYYGMKeMNYYTVLFGVSRALGVLAQLIWSRA 443
Cdd:cd06108 304 FYSASAYHFCGIP-TELFTPIFVMSRVTGWAAHIMEQRA 341
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
93-442 1.42e-12

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: 68.72  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  93 IRFRGYSIPEcqklLPKAPGGEEplpegLFWLLVTGEAPSQEQV-NWISKEWAKRAaLPSHVVTMLDNFPTNLHPMSQLS 171
Cdd:cd06117  23 LHYRGYDILD----LAEKCEFEE-----VAHLLVHGKLPTKSELaAYKTKLKSLRG-LPANVKTALEQLPAAAHPMDVMR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 172 AAITALNSesnfARGYAEGVNKTKYweliyEDSMD-LIAKLPCVAAKIYrNLYREGSSIGAIDSNLDWSHNFTNMLGYTD 250
Cdd:cd06117  93 TGVSVLGC----VLPEKEDHPVSGA-----RDIADrLMASLGSILLYWY-HYSHNGKRIEVETDDDSIGGHFLHLLHGEK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 251 PQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANqEVLVWLTSLQKDlggevSDE 328
Cdd:cd06117 163 PSesWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQRYES-----ADE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899 329 KLRDyIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlKHLPNDPMFKLVAQLYKIVPNVLLEQGKAknpWPNVDAHSG 408
Cdd:cd06117 236 AEAD-IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGGDMKMFDIAERLETVMWEEKKM---FPNLDWFSA 310
                       330       340       350
                ....*....|....*....|....*....|....*
gi 62859899 409 VLLQYYGM-KEMnyYTVLFGVSRALGVLAQLIWSR 442
Cdd:cd06117 311 VSYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12350 PRK12350
citrate synthase 2; Provisional
233-453 3.02e-09

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 58.44  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  233 DSNLDWSHNFTNML-----GYTDPQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLAN 307
Cdd:PRK12350 129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  308 QEVLVWLTSLQKDlggevsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREfALKHLpNDPMFKLVAQLYKIVp 387
Cdd:PRK12350 208 ARVLPMLDAVERT-------GDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRL-GAPRYEVAEAVEQAA- 277
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62859899  388 nvlLEQGKAKNP----WPNVDAHSGVLLQYYGM-KEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 453
Cdd:PRK12350 278 ---LAELRERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
PRK12351 PRK12351
methylcitrate synthase; Provisional
124-443 1.10e-08

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 56.86  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  124 LLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITAL------NSESNF--ARGYAEgvnktk 195
Cdd:PRK12351  54 LLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFsgARDIAD------ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  196 yweliyedsmDLIAKLPCVAAKIYR--------NLYREGSSIGAidsnldwsHnFTNMLGYTDPQ--FTELMRLYLTIHS 265
Cdd:PRK12351 128 ----------RLLASLGSILLYWYHyshngrriEVETDDDSIGG--------H-FLHLLHGKKPSesWVKAMHTSLILYA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  266 DHEGgNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANqEVLVwltSLQKDLggEVSDEKLRDyIWNTLNSGRVVP 345
Cdd:PRK12351 189 EHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQRY--DTPDEAEAD-IRRRVENKEVVI 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859899  346 GYGHAVLRKTDPRYTCQREFALK---HLPNDPMFKLVAQLYKivpnVLLEQgkaKNPWPNVDAHSGVllQYYGM---KEM 419
Cdd:PRK12351 261 GFGHPVYTISDPRNKVIKEVAKKlskEAGDTKLYDIAERLET----VMWEE---KKMFPNLDWFSAV--SYHMMgvpTAM 331
                        330       340
                 ....*....|....*....|....
gi 62859899  420 nyYTVLFGVSRALGVLAQLIWSRA 443
Cdd:PRK12351 332 --FTPLFVISRTTGWAAHVIEQRQ 353
 
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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