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Conserved domains on  [gi|269973935|ref|NP_082221|]
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citrate synthase-like protein [Mus musculus]

Protein Classification

citrate synthase( domain architecture ID 10149814)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


:

Pssm-ID: 99858  Cd Length: 427  Bit Score: 939.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 193 KYWELTYEDCMDLLAKLPCVAAKIYRNLYReDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 273 HTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 353 TDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 269973935 433 LSQLIWSRALGFPLERPKSMSTDALMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99858  Cd Length: 427  Bit Score: 939.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 193 KYWELTYEDCMDLLAKLPCVAAKIYRNLYReDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 273 HTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 353 TDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 269973935 433 LSQLIWSRALGFPLERPKSMSTDALMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 0e+00

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


Pssm-ID: 130853  Cd Length: 427  Bit Score: 770.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935   30 STNLKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  110 GGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGM 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  190 NRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYReDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYK-DGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  270 VSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  350 LRKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 269973935  430 LGVLSQLIWSRALGFPLERPKSMSTDAL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
33-461 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 605.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQG-MNR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 192 TKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIeAIDSKLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 272 AHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEV-GEDASDEKLKNYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 351 RKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 269973935 431 GVLSQLIWSRALGFPLERPKSMSTDALMKFV 461
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWA 431
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
71-450 7.59e-125

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: 367.22  E-value: 7.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935   71 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPEcqkLLpkakgGKEPLPEgLFWLLVTGQMPTEEQVSWLSQEWVKRAALPS 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LA-----ERSSFEE-VAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  150 HVVTMLDNFPTKLHPMSQLSAAITVLNNESNFArayaqGMNRTKYWELTYEDcmDLLAKLPCVAAKIYRNLYREDRNieA 229
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLPPI--Y 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  230 IDSKLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 307
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  308 VLVWLTQLQKEvgedasdEKLKNYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVGQLYKI 383
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935  384 VPDILLEQGkaKNPWPNVDAHSGVLLQYYGMREmNYYTVLFGVSRALGVLSQLIWSRALGfPLERPK 450
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 8.20e-100

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: 304.33  E-value: 8.20e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPEcqkLLPKAkggkepLPEGLFWLLVTGQMPTEEQVSWL 137
Cdd:COG0372    4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIED---LAEKS------SFEEVAYLLLYGELPTKEELAEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 138 SQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLnneSNFaraYAQGMNRTKywELTYEDCMDLLAKLPCVAAKIY 217
Cdd:COG0372   75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 218 RnlYREDRNIEAIDSKLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNG 295
Cdd:COG0372  147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 296 LAGPLHGLANQEVLVWLtqlqKEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDP 372
Cdd:COG0372  224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 373 MFKLVGQLYKIVPDilLEQGKAKNPWPNVDAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQLIWSRAlGFPLERPKS 451
Cdd:COG0372  297 LLEIAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99858  Cd Length: 427  Bit Score: 939.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRT 192
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 193 KYWELTYEDCMDLLAKLPCVAAKIYRNLYReDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 273 HTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 353 TDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALGV 432
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*..
gi 269973935 433 LSQLIWSRALGFPLERPKSMSTDALMK 459
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
33-457 0e+00

Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99857  Cd Length: 426  Bit Score: 793.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:cd06103    1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQG-MNR 191
Cdd:cd06103   81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 192 TKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06103  161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 272 AHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06103  241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 352 KTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALG 431
Cdd:cd06103  321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                        410       420
                 ....*....|....*....|....*.
gi 269973935 432 VLSQLIWSRALGFPLERPKSMSTDAL 457
Cdd:cd06103  401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 0e+00

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


Pssm-ID: 130853  Cd Length: 427  Bit Score: 770.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935   30 STNLKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  110 GGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGM 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  190 NRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYReDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYK-DGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  270 VSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  350 LRKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 269973935  430 LGVLSQLIWSRALGFPLERPKSMSTDAL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
33-457 0e+00

Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99859  Cd Length: 428  Bit Score: 624.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:cd06106    1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRT 192
Cdd:cd06106   81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 193 KYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIEAIDSKLDWSHNFTNMLGYTDPQ-FTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06106  161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 272 AHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06106  241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 352 KTDPRYSCQREFALKH--LPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRA 429
Cdd:cd06106  321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                        410       420
                 ....*....|....*....|....*...
gi 269973935 430 LGVLSQLIWSRALGFPLERPKSMSTDAL 457
Cdd:cd06106  401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
33-461 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 605.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  33 LKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGK 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 113 EPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQG-MNR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 192 TKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIeAIDSKLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 272 AHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEV-GEDASDEKLKNYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 351 RKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 269973935 431 GVLSQLIWSRALGFPLERPKSMSTDALMKFV 461
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWA 431
PLN02456 PLN02456
citrate synthase
29-459 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 517.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  29 SSTNLKDVLRNLIPKEQARIKtfRKKHGKTVVGQITVDmmyGGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKLLPK 107
Cdd:PLN02456  30 TGKDYESPLSELGPVQAERLK--KIKAGKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 108 akggkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQ 187
Cdd:PLN02456 105 ---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 188 GMNRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYRedRNIEAIDSKLDWSHNFTNMLGY-------TDPQFTELMRLYLT 260
Cdd:PLN02456 176 GQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYG--RGPVIPDNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFI 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 261 IHSDHEGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLtqlqKEVGedaSDEKLKNYIWNTLNSGR 340
Cdd:PLN02456 254 IHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KEIG---TVENIPEYVEGVKNSKK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 341 VVPGYGHAVLRKTDPRYSCQREFAL---KHLPKDPMFKLVGQLYKIVpdILLEQGKAKNPWPNVDAHSGVLLQYYGMREm 417
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE- 403
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 269973935 418 NYYTVLFGVSRALGVLSQliWSRALGFPLER---PKSMSTDALMK 459
Cdd:PLN02456 404 EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTGEWLR 446
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 5.28e-143

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: 413.54  E-value: 5.28e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  70 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKLlpkakggkePLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALP 148
Cdd:cd06118    1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 149 SHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARayaqgmnrTKYWELTYEDCMDLLAKLPCVAAKIYRnlYREDRNIE 228
Cdd:cd06118   72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFAR--------DKSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 229 AIDSKLDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 306
Cdd:cd06118  142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 307 EVLVWLTQLQKEvgedasdEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVGQLYKI 383
Cdd:cd06118  221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 384 VPDILLEqgkaKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLIWSRALGFPLERPKSMS 453
Cdd:cd06118  294 ALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
71-450 7.59e-125

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: 367.22  E-value: 7.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935   71 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPEcqkLLpkakgGKEPLPEgLFWLLVTGQMPTEEQVSWLSQEWVKRAALPS 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LA-----ERSSFEE-VAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  150 HVVTMLDNFPTKLHPMSQLSAAITVLNNESNFArayaqGMNRTKYWELTYEDcmDLLAKLPCVAAKIYRNLYREDRNieA 229
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLPPI--Y 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  230 IDSKLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 307
Cdd:pfam00285 143 PDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  308 VLVWLTQLQKEvgedasdEKLKNYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVGQLYKI 383
Cdd:pfam00285 222 VLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEEV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935  384 VPDILLEQGkaKNPWPNVDAHSGVLLQYYGMREmNYYTVLFGVSRALGVLSQLIWSRALGfPLERPK 450
Cdd:pfam00285 295 APEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 8.20e-100

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: 304.33  E-value: 8.20e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPEcqkLLPKAkggkepLPEGLFWLLVTGQMPTEEQVSWL 137
Cdd:COG0372    4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIED---LAEKS------SFEEVAYLLLYGELPTKEELAEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 138 SQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLnneSNFaraYAQGMNRTKywELTYEDCMDLLAKLPCVAAKIY 217
Cdd:COG0372   75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 218 RnlYREDRNIEAIDSKLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNG 295
Cdd:COG0372  147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 296 LAGPLHGLANQEVLVWLtqlqKEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDP 372
Cdd:COG0372  224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 373 MFKLVGQLYKIVPDilLEQGKAKNPWPNVDAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQLIWSRAlGFPLERPKS 451
Cdd:COG0372  297 LLEIAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 3.52e-94

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: 285.36  E-value: 3.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  70 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKLlpkakggkePLPEGLFWLLVTGQMPteeqvswlsqewvkraalp 148
Cdd:cd06101    1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAEN---------SSFEEVAYLLLTGELP------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 149 shvvtmldnfptklhpmsqlsaaitvlnnesnfarayaqgmnrtkyweltyedcmdllaklpcvaakiyrnlyredrnie 228
Cdd:cd06101      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 229 aidsklDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 306
Cdd:cd06101   53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 307 EVLVWLTQLQKEVgedasDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVGQLYKI 383
Cdd:cd06101  126 AVLKMLEEIGTPK-----NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 384 VPDILLEqgkaKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLIWSRALGFPLERPKSMS 453
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 ...
235-453 1.25e-86

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: 264.20  E-value: 1.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 235 DWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWL 312
Cdd:cd06099    1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 313 TQLQKEVGEDASDeklknYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVGQLYKIVPDILL 389
Cdd:cd06099   80 EEIGTPKNEPAEA-----YIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269973935 390 EqgkaKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLIWSRALGFPLERPKSMS 453
Cdd:cd06099  155 E----KKLYPNVDFYSGVLYKAMGF-PTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
73-437 2.64e-43

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: 155.90  E-value: 2.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  73 RGMKGLVYETSVL---DPDEGI-RFRGYSIPEcqkLLPKAKGgkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALP 148
Cdd:cd06110    1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD---LAENSTF------EEVAYLLWNGELPTAEELDAFKAQLAAERELP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 149 SHVVTMLDNFPTKLHPMSQLSAAITVLnnesnfARAYAQGMNRTKywELTYEDCMDLLAKLPCVAAKIYRnlYREDRNIE 228
Cdd:cd06110   72 AEIIDLLKLLPKDAHPMDVLRTAVSAL------ALYDPEADDMSR--EANLRKAIRLIAKMPTIVAAFHR--IRNGLEPV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 229 AIDSKLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 306
Cdd:cd06110  142 APDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 307 EVLVWLTqlqkEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKhlpkdpMFKLVGQ--LYKIV 384
Cdd:cd06110  221 RVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRR------LGKETGEpkWYEMS 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269973935 385 PDILLEQGKAKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLI 437
Cdd:cd06110  288 EAIEQAMRDEKGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
83-443 5.27e-43

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


Pssm-ID: 99865  Cd Length: 373  Bit Score: 155.66  E-value: 5.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  83 SVLDPDEGI-RFRGYSIPECqkllpkAKGGKEplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTK 161
Cdd:cd06112   16 SYIDGKNGIlEYRGYDIEEL------AEYSSF---EEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 162 LHPMSQLSAAITVLNneSNFARAYAQGMNRTKYWELtyedCMDLLAKLPCVAAKIYRnlYREDRNIEAIDSKLDWSHNFT 241
Cdd:cd06112   87 GHPMDMLQATVAALG--MFYPKPEVLKPNPDYIDAA----TVKLIAKMPTLVAMWAR--IRNGDDPIEPRPDLDYAENFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 242 NML--GYTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLtqlqKEV 319
Cdd:cd06112  159 YMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----EEI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 320 GedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPK-----DPMFKLVGQLYKIVPDILLEQGKa 394
Cdd:cd06112  234 G---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKGV- 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 269973935 395 knpWPNVDAHSGVLLQYYGMREmNYYTVLFGVSRALGVLSQliWSRALG 443
Cdd:cd06112  309 ---YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLG 351
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
83-454 2.82e-42

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: 154.13  E-value: 2.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  83 SVLDPDEGI-RFRGYSIPECqkllpkakGGKEPLPEGLFwLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTK 161
Cdd:cd06107   20 TYIDGDKGIlLYRGYPIEQL--------AESSTYEEVAY-LLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 162 LHPMSQLSAAITVLNN---ESNFARAYAQGMNRTkywELTYEDCMDLLAKLPCVAAKIYRnlYREDRNIEAIDSKLDWSH 238
Cdd:cd06107   91 AHPMGILCAGLSALSAfypEAIPAHTGDLYQNNP---EVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 239 NFTNMLGYTD-------PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVW 311
Cdd:cd06107  166 NFLYMMGYVDqepyepnPRLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 312 LtqlqKEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVGQLYKIVpdil 388
Cdd:cd06107  245 L----REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIA---- 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269973935 389 LEQG--KAKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQliWSRALGFPLE---RPKSMST 454
Cdd:cd06107  314 LEDEyfVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
83-445 3.01e-37

Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99868  Cd Length: 410  Bit Score: 141.04  E-value: 3.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  83 SVLDPDEGI-RFRGYSIPECQKllpkakggKEPLPEGLFwLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTK 161
Cdd:cd06115   40 SYIDGDKGIlRYRGYPIEELAE--------KSTFLEVAY-LLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 162 LHPMSQLSAAITVLNN---ESNFARAyAQGMNRTKywELTYEDCMDLLAKLPCVAAKIYRNlyREDRNIEAIDSKLDWSH 238
Cdd:cd06115  111 AHPMGMLVSAISALSAfhpEANPALA-GQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 239 NFTNML---GYTD----PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVW 311
Cdd:cd06115  186 NFLYMLdslGERKykpnPRLARALDILFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 312 LTQLqkevgedASDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlkhlpkDPMFKLVGQlykivpDILLEQ 391
Cdd:cd06115  265 LAEI-------GTVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGK------DPLIEI 325
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935 392 GKA-------------KNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQliWSRALGFP 445
Cdd:cd06115  326 AVAlekaalsdeyfvkRKLYPNVDFYSGLIYRAMGF-PTDFFPVLFAIPRMAGYLAH--WRESLDDP 389
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
87-431 2.00e-33

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: 130.47  E-value: 2.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  87 PDEG-IRFRGYSIPEcqkLLPKAKGGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVV-TMLDNFPTKlHP 164
Cdd:cd06113   33 PCPGkLYYRGYDVED---LVNGAQKENRFGFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK-DI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 165 MSQLSAAITVLnnesnfaRAYAQGMNRTKYwELTYEDCMDLLAKLPCVAAKIY----RNLYREDRNIEAIDSKLDWSHNF 240
Cdd:cd06113  109 MNKLQRSVLAL-------YSYDDKPDDISL-ENVLRQSIQLIARLPTIAVYAYqakrHYYDGESLYIHHPQPELSTAENI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 241 TNMLgYTDPQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQ 316
Cdd:cd06113  181 LSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIK 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 317 KEVgEDASDEK-LKNYIWNTLN------SGrVVPGYGHAVLRKTDPRYSCQREFAlKHLPK----DPMFKLVGQLYKIVP 385
Cdd:cd06113  260 ENV-KDWTDEDeVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERIERLAP 336
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 269973935 386 DILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----REMnyYTVLFGVSRALG 431
Cdd:cd06113  337 EVIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVG 382
gltA PRK05614
citrate synthase;
85-436 8.41e-33

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 128.84  E-value: 8.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  85 LDPDEGI-RFRGYSIpecQKLLPKAKggkeplpeglF----WLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFP 159
Cdd:PRK05614  62 IDGDKGIlLYRGYPI---EQLAEKSD----------FlevcYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 160 TKLHPMSQLSAAITVLnneSNFarayaqgmnrtkyweltYEDCMD-------------LLAKLPCVAAKIYRnlYREDRN 226
Cdd:PRK05614 129 RDAHPMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 227 IEAIDSKLDWSHNFTNML-GY------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGP 299
Cdd:PRK05614 187 FVYPRNDLSYAENFLRMMfATpceeyeVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGP 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 300 LHGLANQEVLVWLtqlqKEVG--EDASD--EKLKNYiwntlNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHL-PKD 371
Cdd:PRK05614 266 AHGGANEAVLKML----EEIGsvDNIPEfiARAKDK-----NDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLND 336
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269973935 372 PMFKLVGQLYKIV--PDILLEqgkaKNPWPNVDAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQL 436
Cdd:PRK05614 337 PLLEVAMELEEIAlnDEYFIE----RKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
85-454 1.03e-32

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: 128.02  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  85 LDPDEGI-RFRGYSIPE-CQK--LLPKAkggkeplpeglfWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPT 160
Cdd:cd06116   22 IDGEKGIlRYRGYPIEQlAEQssYLEVA------------YLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 161 KLHPMSQLSAAITVLNNESNFARAYAQGMNRTKyweltyeDCMDLLAKLPCVAAKIYRnlYREDRNIEAIDSKLDWSHNF 240
Cdd:cd06116   90 DAHPMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 241 TNMLGY-------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLT 313
Cdd:cd06116  161 LSMLFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 314 QLqkevgedASDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVGQLYKIVPDIllE 390
Cdd:cd06116  240 QI-------GSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIALED--E 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935 391 QGKAKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQliWSRALGFP---LERPKSMST 454
Cdd:cd06116  311 YFISRKLYPNVDFYSGLIYQALGF-PTEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14036 PRK14036
citrate synthase; Provisional
83-443 1.88e-31

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 124.30  E-value: 1.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  83 SVLDPDEGI-RFRGYSIPECQK---LLPKAkggkeplpeglfWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNF 158
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEELAEkssFLETA------------YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 159 PTKLHPMSQLSAAITVLnnesnfARAYA-QGMNRTKYwelTYEDCMDLLAKLPC-VAAkiYRNLYREDRNIEAIDSkLDW 236
Cdd:PRK14036  87 PETGHPMDALQASAAAL------GLFYSrRALDDPEY---IRDAVVRLIAKIPTmVAA--FQLIRKGNDPIQPRDD-LDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 237 SHNFTNMLG--YTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLtq 314
Cdd:PRK14036 155 AANFLYMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML-- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 315 lqKEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVGQLYKIVPDILLEQ 391
Cdd:PRK14036 232 --EEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPK 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 269973935 392 GKaknpWPNVDAHSGVLlqYygmREM----NYYTVLFGVSRALGVLSQliWSRALG 443
Cdd:PRK14036 307 GI----YPNVDFYSGLV--Y---RKLgiprDLFTPIFAIARVAGWLAH--WREQLG 351
PRK14032 PRK14032
citrate synthase; Provisional
87-431 2.67e-31

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 125.02  E-value: 2.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  87 PDEG-IRFRGYSIpecQKLLPKAKGGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVtmlDNFPTKLHP- 164
Cdd:PRK14032  63 PDEGkLYYRGYDI---KDLVNGFLKEKRFGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFT---RDMILKAPSk 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 165 --MSQLSAAITVLnnesnfaraYA---QGMNRTKYWELtyEDCMDLLAKLPCVAAKIYRNL-YREDRN---IEAIDSKLD 235
Cdd:PRK14032 137 diMNSLARSVLAL---------YSyddNPDDTSIDNVL--RQSISLIARFPTLAVYAYQAYrHYHDGKslyIHPPKPELS 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 236 WSHNFTNMLgYTDPQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVW 311
Cdd:PRK14032 206 TAENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEM 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 312 LTQLQKEVGEDASDEKLKNYIWNTLN------SGRVVpGYGHAVLRKTDPRYSCQREFAL-----KHLPKDpmFKLVGQL 380
Cdd:PRK14032 285 FEDIKENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNLYEKI 361
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 269973935 381 YKIVPDILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----REMnyYTVLFGVSRALG 431
Cdd:PRK14032 362 EKLAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVG 412
PRK14034 PRK14034
citrate synthase; Provisional
73-437 1.85e-30

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 121.41  E-value: 1.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  73 RGMKGLVYETSVLDP--DEGIRFRGYSIPEcqkLLPKAKGgkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSH 150
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDD---LAENASF------EEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 151 VVTMLDNFP-TKLHPMSQLSAAITVLN--NESnfarayAQGMNRtkywELTYEDCMDLLAKLPCVAAKIYRnlYREDRNI 227
Cdd:PRK14034  76 IIEHLKQYDlKKVHPMSVLRTAISMLGlyDEE------AEIMDE----EANYRKAVRLQAKVPTIVAAFSR--IRKGLDP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 228 EAIDSKLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLAN 305
Cdd:PRK14034 144 VEPRKDLSLAANFLYMLNGEEPDEVEVeaFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGAN 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 306 QEVLVWLTqlqkEVGEdasDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKhlpkdpMFKLVGQ--LYKI 383
Cdd:PRK14034 223 ENVMKMLT----EIGE---EENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKR------LTVLLGEekWYNM 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935 384 ---VPDILLEQgkaKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLI 437
Cdd:PRK14034 290 sikIEEIVTKE---KGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHIL 342
PRK14035 PRK14035
citrate synthase; Provisional
73-431 1.00e-26

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 110.62  E-value: 1.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  73 RGMKGLVY-ETSVLD-PDEGIRFRGYSIPEcqkLLPKAKggkepLPEGLFwLLVTGQMPTEEQVSWLSQEWVKRAALPSH 150
Cdd:PRK14035   5 RGLEGVIAaETKISSiIDSQLTYAGYDIDD---LAENAS-----FEEVIF-LLWNYRLPTEEELAHLKGKLRKYMTLNDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 151 VVTMLDNFPTK-LHPMSQLSAAITVLNNESNFARayaqgmNRTKywELTYEDCMDLLAKLPCVAAKIYRnlYREDRNIEA 229
Cdd:PRK14035  76 VYQHFEEYSTDhVHPMTALRTSVSYLAHFDPDAE------EESD--EARYERAIRIQAKVASLVTAFAR--VRQGKEPLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 230 IDSKLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 307
Cdd:PRK14035 146 PRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANER 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 308 VLVWLTQLqKEVGEdasdekLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDPMFKLVGQLYKIVPDI 387
Cdd:PRK14035 225 VMDMLSEI-RSIGD------VDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMS-RKITKGTGREELFEMSVKIEKR 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 269973935 388 LLEQgkaKNPWPNVDAHSGVLlqYYGMR-EMNYYTVLFGVSRALG 431
Cdd:PRK14035 297 MKEE---KGLIPNVDFYSATV--YHVMGiPHDLFTPIFAVSRVAG 336
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
117-431 1.92e-25

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 107.34  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 117 EGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRTKywe 196
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADDSSPEANLAK--- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 197 ltyedCMDLLAKLPCVAAKIYRNlyREDRNIEAIDSKLDWSHNFTNM-LG-YTDPQFTELMRLYLTIHSDHeGGNVSAHT 274
Cdd:PRK14033 127 -----ALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTFT 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 275 SHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLvwltQLQKEVGedaSDEKLKNYIWNTLNSGRVVPGYGHAVLRKTD 354
Cdd:PRK14033 199 ARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHGD 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269973935 355 PRYSCQREfALKHLPKDPMFKLVGQLYKIVPDILLEqgkAKNPWPNVDAHSGVLlqYYGMR-EMNYYTVLFGVSRALG 431
Cdd:PRK14033 272 SRVPTMKA-ALRRVAAVRDGQRWLDIYEALEKAMAE---ATGIKPNLDFPAGPA--YYLMGfDIDFFTPIFVMSRITG 343
PRK12349 PRK12349
citrate synthase;
74-437 4.08e-24

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 103.26  E-value: 4.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  74 GMKGLVY-ET--SVLDPDEG-IRFRGYSIPEcqklLPKAKGGKEplpegLFWLLVTGQMPTEEQVSWLSQEWVKRAALPS 149
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 150 HVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRTKyweltyedCMDLLAKLPCVAAKIYRNLyrEDRNIEA 229
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSR--------AYKLLSKVPNIVANSYHIL--NNEEPIE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 230 IDSKLDWSHNFTNMLGYTDP--QFTELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 307
Cdd:PRK12349 149 PLKELSYSANFLYMLTGKKPteLEEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 308 VLVWLTQlqkevGEDASD-EKLknyIWNTLNSGRVVPGYGHAV-LRKTDPRYSCQREfALKHL-PKDPMFKlvgqLYKiv 384
Cdd:PRK12349 228 VMYMLLE-----AGTVEKfEEL---LQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcDVKGDYT----LYE-- 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 269973935 385 pdiLLEQG-----KAKNPWPNVDAHSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLI 437
Cdd:PRK12349 293 ---MCEAGekimeKEKGLYPNLDYYAAPVYWMLGI-PIQLYTPIFFSSRTVGLCAHVI 346
PRK14037 PRK14037
citrate synthase; Provisional
85-437 3.20e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 100.98  E-value: 3.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  85 LDPDEGI-RFRGYSIpecQKLLpkAKGGKEPLpeglFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLH 163
Cdd:PRK14037  21 IDGEKGIlRYRGYNI---EDLV--NYGSYEET----IYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 164 PMSQLSAAITVLnnesnfarayAQGMNRTKYWELTYEDCMDLLAKLPCVAAKIYRnlYREDRNIEAIDSKLDWSHNFTNM 243
Cdd:PRK14037  92 AIGLMEAAFAAL----------ASIDKNFKWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 244 LGYTDPQFTEL--MRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFAAALNGLAGPLHGLANQEVLvwlTQLQkEV 319
Cdd:PRK14037 160 SFAREPTAEEIkaMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAF---KQFV-EI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 320 GEDASDEKLKNYiwNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWP 399
Cdd:PRK14037 233 GDPNNVEMWFND--KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGIYP 310
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 269973935 400 NVDAHSGVLlqYYGMR-EMNYYTVLFGVSRALGVLSQLI 437
Cdd:PRK14037 311 NTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
90-441 1.03e-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: 87.36  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  90 GIRFRGYSIPEcqkLLPKAKGgkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLS 169
Cdd:cd06108   22 GLTYRGYDIED---LAENATF------EEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 170 AAITVLNN---ESNFARAYAQGmNRtkyweltyedcmdLLAKLPCVAAKIYRnlYRED-RNIEAIDSKLDWSHNFTNMLG 245
Cdd:cd06108   93 TGCSMLGClepENEFSQQYEIA-IR-------------LLAIFPSILLYWYH--YSHSgKRIETETDEDSIAGHFLHLLH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 246 YTDP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEvgEDA 323
Cdd:cd06108  157 GKKPgeLEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSP--EEA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 324 SDEKLKnyiwnTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDpmfKLVGQLYKIVPDILLEQGKAKNPWPNVDA 403
Cdd:cd06108  234 EQGLLE-----KLERKELIMGFGHRVYKEGDPRSDIIKKWS-KKLSEE---GGDPLLYQISERIEEVMWEEKKLFPNLDF 304
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 269973935 404 HSGVLLQYYGMrEMNYYTVLFGVSRALGVLSQLIWSRA 441
Cdd:cd06108  305 YSASAYHFCGI-PTELFTPIFVMSRVTGWAAHIMEQRA 341
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
73-451 2.33e-17

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: 83.12  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  73 RGMKGLV-YETSVLDPD--EG-IRFRGYSIPEcqkLLPKAKGgkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALP 148
Cdd:cd06109    1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED---LAGSASF------EDVAALLWNGFFPDLPELEEFRAALAAARALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 149 SHVVTMLDNFpTKLHPMSQLSAAITVLNNESNFARAyaqgmnrtkyweltyedcMDLLAKLPCVAAKIYRnLYREDRNIE 228
Cdd:cd06109   72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDLATA------------------LRLLAAAPVITAALLR-LSRGKQPIA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 229 AiDSKLDWSHNFTNML-GYTDPQ-FTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 306
Cdd:cd06109  132 P-DPSLSHAADYLRMLtGEPPSEaHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 307 EVLVWLtqlqKEVGEDASDEKlknYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLP-KDPMFKLVGQLYKIVP 385
Cdd:cd06109  210 PVLDML----DAIGTPENAEA---WLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGaPDERLEFAEAVEQAAL 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269973935 386 DILLEQGKAKNPWPNVDAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQLIWSRALGfPLERPKS 451
Cdd:cd06109  282 ALLREYKPGRPLETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
91-440 1.49e-13

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


Pssm-ID: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 71.80  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935  91 IRFRGYSIPEcqkLLPKAKGgkeplpEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSA 170
Cdd:cd06117   23 LHYRGYDILD---LAEKCEF------EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 171 AITVLnnesnfarayaqGMNRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIEAIDSKLD---WSHNFTNMLGYT 247
Cdd:cd06117   94 GVSVL------------GCVLPEKEDHPVSGARDIADRLMASLGSILLYWYHYSHNGKRIEVETDddsIGGHFLHLLHGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 248 DPQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANqEVLVWLTQLQKEVGEDASD 325
Cdd:cd06117  162 KPSesWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQRYESADEAEAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 326 eklknyIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDP----MFKLVGQLYKIVPDIlleqgkaKNPWPNV 401
Cdd:cd06117  240 ------IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGgdmkMFDIAERLETVMWEE-------KKMFPNL 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 269973935 402 DAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQLIWSR 440
Cdd:cd06117  306 DWFSAVSYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12350 PRK12350
citrate synthase 2; Provisional
231-451 6.36e-10

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 60.36  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 231 DSKLDWSHNFTNML-----GYTDPQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLAN 305
Cdd:PRK12350 129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 306 QEVLVWLTQLqkEVGEDAsdeklKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLPKdPMFKLVGQLYKIVP 385
Cdd:PRK12350 208 ARVLPMLDAV--ERTGDA-----RGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRLGA-PRYEVAEAVEQAAL 278
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269973935 386 DILleqgKAKNP----WPNVDAHSGVLLQYYGM-REMnyYTVLFGVSRALGVLSQLIWSRALGfPLERPKS 451
Cdd:PRK12350 279 AEL----RERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
PRK12351 PRK12351
methylcitrate synthase; Provisional
122-431 3.29e-09

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 58.40  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 122 LLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNN------ESNFARAYaqgmnrtkyw 195
Cdd:PRK12351  54 LLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCllpekeDHNFSGAR---------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 196 eltyeDCMD-LLAKLPcvAAKIYrnLYREDRNIEAIDSKLD----WSHnFTNMLGYTDPQ--FTELMRLYLTIHSDHEGg 268
Cdd:PRK12351 124 -----DIADrLLASLG--SILLY--WYHYSHNGRRIEVETDddsiGGH-FLHLLHGKKPSesWVKAMHTSLILYAEHEF- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 269 NVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANqEVLVwltQLQKevGEDASDEKLKNyIWNTLNSGRVVPGYGHA 348
Cdd:PRK12351 193 NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQ--RYDTPDEAEAD-IRRRVENKEVVIGFGHP 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973935 349 VLRKTDPRYSCQREFAlKHLPKDpmfklVG--QLYKIVPDILLEQGKAKNPWPNVDAHSGVllQYYGM---REMnyYTVL 423
Cdd:PRK12351 266 VYTISDPRNKVIKEVA-KKLSKE-----AGdtKLYDIAERLETVMWEEKKMFPNLDWFSAV--SYHMMgvpTAM--FTPL 335

                 ....*...
gi 269973935 424 FGVSRALG 431
Cdd:PRK12351 336 FVISRTTG 343
 
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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