NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720360295|ref|XP_030100721|]
View 

citrate synthase, mitochondrial isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-393 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: 897.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:cd06105    35 MVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGEEPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSS 160
Cdd:cd06105   115 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKSKYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGK 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 161 IGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06105   194 IIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:cd06105   274 EVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPP 353
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMK 393
Cdd:cd06105   354 VLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVLSQLIWDRALGLPLERPKSVSTDGLEK 426
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
1-393 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: 897.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:cd06105    35 MVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGEEPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSS 160
Cdd:cd06105   115 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKSKYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGK 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 161 IGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06105   194 IIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:cd06105   274 EVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPP 353
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMK 393
Cdd:cd06105   354 VLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVLSQLIWDRALGLPLERPKSVSTDGLEK 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
1-391 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: 729.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:TIGR01793  38 MVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKGGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARAD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSS 160
Cdd:TIGR01793 118 LPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIHKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 161 IgAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:TIGR01793 198 I-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:TIGR01793 277 EVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVLRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPG 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGL 391
Cdd:TIGR01793 357 ILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
3-398 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 584.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   3 YGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:PRK09569   39 IGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSI 161
Cdd:PRK09569  119 QYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNKMDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 162 gAIDSRLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 241
Cdd:PRK09569  199 -PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQE 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 242 VLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:PRK09569  277 VLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPG 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK 398
Cdd:PRK09569  357 VLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
5-384 1.97e-130

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: 378.77  E-value: 1.97e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   5 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFArayaeGMNRAKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYK 316
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 317 IVPNILLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 384
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
7-385 1.68e-103

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 311.26  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:COG0372    15 PGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGMNRAKywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:COG0372    86 EEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR--YRRGLPPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:COG0372   156 YPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKI 317
Cdd:COG0372   235 AVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEV 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360295 318 VPNilLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 385
Cdd:COG0372   308 ALE--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 ...
1-393 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: 897.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:cd06105    35 MVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGEEPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSS 160
Cdd:cd06105   115 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKSKYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGK 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 161 IGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06105   194 IIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:cd06105   274 EVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPP 353
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMK 393
Cdd:cd06105   354 VLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVLSQLIWDRALGLPLERPKSVSTDGLEK 426
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
1-391 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: 761.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:cd06103    35 QVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGGEPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGS 159
Cdd:cd06103   115 VPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINKTTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 160 SIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLAN 239
Cdd:cd06103   195 EIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLAN 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 240 QEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVP 319
Cdd:cd06103   275 QEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIP 354
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360295 320 NILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGL 391
Cdd:cd06103   355 GVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALGVLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
1-391 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: 729.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   1 MMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAA 80
Cdd:TIGR01793  38 MVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKGGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARAD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  81 LPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSS 160
Cdd:TIGR01793 118 LPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIHKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 161 IgAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:TIGR01793 198 I-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:TIGR01793 277 EVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVLRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPG 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGL 391
Cdd:TIGR01793 357 ILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
4-391 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: 598.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   4 GGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPS 83
Cdd:cd06106    38 GGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGGEMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  84 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGA 163
Cdd:cd06106   118 YIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 164 IDSRLDWSHNFTNMLGYTDPQ-FTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEV 242
Cdd:cd06106   198 IDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEV 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 243 LVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKH--LPKDPMFKLVAQLYKIVPN 320
Cdd:cd06106   278 LRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPG 357
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGL 391
Cdd:cd06106   358 VLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRALGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
3-398 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 584.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   3 YGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:PRK09569   39 IGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSI 161
Cdd:PRK09569  119 QYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNKMDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 162 gAIDSRLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 241
Cdd:PRK09569  199 -PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQE 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 242 VLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:PRK09569  277 VLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPG 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 321 ILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK 398
Cdd:PRK09569  357 VLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
4-388 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 513.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   4 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMLPKakggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:PLN02456   66 PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIG 162
Cdd:PLN02456  137 EHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 aiDSRLDWSHNFTNMLGY-------TDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLH 235
Cdd:PLN02456  217 --DNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLH 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 236 GLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAL---KHLPKDPMFKLVA 312
Cdd:PLN02456  295 GGANEAVLKML----KEIG---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVAS 367
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360295 313 QLYKIVpnILLEQGKAKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALGFPLER---PKSMST 388
Cdd:PLN02456  368 ALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE-EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYT 441
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
4-387 3.21e-149

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


Pssm-ID: 99871 [Multi-domain]  Cd Length: 358  Bit Score: 426.63  E-value: 3.21e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   4 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:cd06118     1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAyaegmnraKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:cd06118    72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFARD--------KSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06118   142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKI 317
Cdd:cd06118   221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 318 VPNILLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 387
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.
5-384 1.97e-130

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: 378.77  E-value: 1.97e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   5 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFArayaeGMNRAKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYK 316
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 317 IVPNILLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 384
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
7-385 1.68e-103

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 311.26  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:COG0372    15 PGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGMNRAKywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:COG0372    86 EEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR--YRRGLPPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:COG0372   156 YPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKI 317
Cdd:COG0372   235 AVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEV 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360295 318 VPNilLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 385
Cdd:COG0372   308 ALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
4-387 1.32e-97

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


Pssm-ID: 99855 [Multi-domain]  Cd Length: 265  Bit Score: 291.91  E-value: 1.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   4 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQMPteeqvswlsrewakraalp 82
Cdd:cd06101     1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAEN---------SSFEEVAYLLLTGELP------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 shvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegmnrakyweliyedcmdliaklpcvaakiyrnlyregssig 162
Cdd:cd06101       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 aidsrlDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06101    53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLTQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKI 317
Cdd:cd06101   126 AVLKMLEEIGTPK-----NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 318 VPNILLEqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 387
Cdd:cd06101   201 APEVLYE----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
169-387 8.84e-90

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


Pssm-ID: 99853 [Multi-domain]  Cd Length: 213  Bit Score: 269.98  E-value: 8.84e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 169 DWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 246
Cdd:cd06099     1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 247 TQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKIVPNILL 323
Cdd:cd06099    80 EEIGTPK-----NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360295 324 EqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 387
Cdd:cd06099   155 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
17-388 1.59e-47

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: 166.46  E-value: 1.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  17 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 95
Cdd:cd06107    20 TYIDGDKGIlLYRGYPIEQ----LAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  96 LHPMSQLSAAITALNS---ESNFARAYAEGMNRAkywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSH 172
Cdd:cd06107    91 AHPMGILCAGLSALSAfypEAIPAHTGDLYQNNP---EVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 173 NFTNMLGYTD-------PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 245
Cdd:cd06107   166 NFLYMMGYVDqepyepnPRLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKM 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 246 LtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVPNIl 322
Cdd:cd06107   245 L----REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED- 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360295 323 lEQGKAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQliWSRALGFPLE---RPKSMST 388
Cdd:cd06107   317 -EYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
17-377 5.83e-47

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: 164.52  E-value: 5.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  17 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 95
Cdd:cd06112    16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  96 LHPMSQLSAAITALNSesNFARAYAEGMNRAKywelIYEDCMDLIAKLPCVAAKIYRnlYREGSSIgaIDSRLDWSH--N 173
Cdd:cd06112    87 GHPMDMLQATVAALGM--FYPKPEVLKPNPDY----IDAATVKLIAKMPTLVAMWAR--IRNGDDP--IEPRPDLDYaeN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 174 FTNML--GYTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqK 251
Cdd:cd06112   157 FLYMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----E 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 252 EVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPK-----DPMFKLVAQLYKIVPNILLEQG 326
Cdd:cd06112   232 EIG---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKG 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720360295 327 KaknpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 377
Cdd:cd06112   308 V----YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLG 351
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
7-371 1.07e-44

Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99863 [Multi-domain]  Cd Length: 356  Bit Score: 158.21  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKGLVYETSVL---DPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:cd06110     1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD----LAENSTFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFPTNLHPMSQLSAAITAL---NSEsnfarayAEGMNRakywELIYEDCMDLIAKLPCVAAKIYRnlYREGS 159
Cdd:cd06110    72 AEIIDLLKLLPKDAHPMDVLRTAVSALalyDPE-------ADDMSR----EANLRKAIRLIAKMPTIVAAFHR--IRNGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 160 SIGAIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGL 237
Cdd:cd06110   139 EPVAPDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 238 ANQEVLVWLTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKhLPKD----PMFKLVAQ 313
Cdd:cd06110   218 ANERVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRR-LGKEtgepKWYEMSEA 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 314 LYKIVPNilleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 371
Cdd:cd06110   290 IEQAMRD-------EKGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
17-379 3.60e-38

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: 141.81  E-value: 3.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  17 SVLDPDEGI-RFRGYSIPEcqkMLPKAKGGEeplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 95
Cdd:cd06115    40 SYIDGDKGIlRYRGYPIEE---LAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  96 LHPMSQLSAAITALNS---ESNFARAyaeGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSRLDWSH 172
Cdd:cd06115   111 AHPMGMLVSAISALSAfhpEANPALA---GQDIYKNKQVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 173 NFTNML---GYTD----PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 245
Cdd:cd06115   186 NFLYMLdslGERKykpnPRLARALDILFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 246 LTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVpnIL 322
Cdd:cd06115   265 LA----EIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLAdevFEIVGKDPLIEIAVALEKAA--LS 335
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 323 LEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQliWSRALGFP 379
Cdd:cd06115   336 DEYFVKRKLYPNVDFYSGLIYRAMGFpTDF--FPVLFAIPRMAGYLAH--WRESLDDP 389
gltA PRK05614
citrate synthase;
19-370 5.36e-38

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 141.55  E-value: 5.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  19 LDPDEGI-RFRGYSIpecqkmlpkakggeEPLPE-GLF----WLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNF 92
Cdd:PRK05614   62 IDGDKGIlLYRGYPI--------------EQLAEkSDFlevcYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  93 PTNLHPMSQLSAAITALnseSNFarayaegmnrakyweliYEDCMD-------------LIAKLPCVAAKIYRnlYREGS 159
Cdd:PRK05614  128 RRDAHPMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQ 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 160 SIGAIDSRLDWSHNFTNML-GY------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAG 232
Cdd:PRK05614  186 PFVYPRNDLSYAENFLRMMfATpceeyeVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWG 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 233 PLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTL--NSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHL-PKDP 306
Cdd:PRK05614  265 PAHGGANEAVLKML----EEIG---SVDNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDP 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360295 307 MFKLVAQLYKIVPNIllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQL 370
Cdd:PRK05614  338 LLEVAMELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
19-388 1.11e-36

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: 137.27  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  19 LDPDEGI-RFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLH 97
Cdd:cd06116    22 IDGEKGIlRYRGYPIEQL---------AEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  98 PMSQLSAAITALNSESNFARAYAEGMNRAKyweliyeDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSHNFTNM 177
Cdd:cd06116    93 PMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNFLSM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 178 LGY-------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 250
Cdd:cd06116   164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML---- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 251 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVpnILLEQGK 327
Cdd:cd06116   239 QQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIA--LEDEYFI 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360295 328 AKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 388
Cdd:cd06116   314 SRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14036 PRK14036
citrate synthase; Provisional
17-377 1.47e-35

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 134.31  E-value: 1.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  17 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 95
Cdd:PRK14036   19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  96 LHPMSQLSAAITALNSesNFARAyaeGMNRAKYwelIYEDCMDLIAKLPC-VAAkiyRNLYREGSSigAIDSR--LDWSH 172
Cdd:PRK14036   90 GHPMDALQASAAALGL--FYSRR---ALDDPEY---IRDAVVRLIAKIPTmVAA---FQLIRKGND--PIQPRddLDYAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 173 NFTNMLG--YTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 250
Cdd:PRK14036  157 NFLYMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML---- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 251 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVPNILLEQGK 327
Cdd:PRK14036  232 EEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720360295 328 aknpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 377
Cdd:PRK14036  309 ----YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
21-371 1.57e-35

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: 134.70  E-value: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  21 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVV-TMLDNFPTNl 96
Cdd:cd06113    33 PCPGkLYYRGYDVEDLVNGAQKENrfGFEE-----TAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  97 HPMSQLSAAITALNSesnfaraY---AEGMNRakywELIYEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSRLD 169
Cdd:cd06113   107 DIMNKLQRSVLALYS-------YddkPDDISL----ENVLRQSIQLIARLPTIAVYAYQakRHYYDGESlyIHHPQPELS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 170 WSHNFTNMLgYTDPQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 245
Cdd:cd06113   176 TAENILSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEM 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 246 LTQLQKEVgKDVSDEK-LRDYIWNTLN------SGrVVPGYGHAVLRKTDPRYSCQREFAlKHLPK----DPMFKLVAQL 314
Cdd:cd06113   255 LEDIKENV-KDWTDEDeVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERI 331
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360295 315 YKIVPNILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLAQLI 371
Cdd:cd06113   332 ERLAPEVIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCAHRI 388
PRK14032 PRK14032
citrate synthase; Provisional
21-368 3.29e-33

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 128.87  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  21 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVV--TMLDNFPTN 95
Cdd:PRK14032   63 PDEGkLYYRGYDIKDLVNGFLKEKrfGFEE-----VAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrdMILKAPSKD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  96 LhpMSQLSAAITALNS-ESNfarayAEGMNRakywELIYEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSRLDW 170
Cdd:PRK14032  138 I--MNSLARSVLALYSyDDN-----PDDTSI----DNVLRQSISLIARFPTLAVYAYQayRHYHDGKSlyIHPPKPELST 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 171 SHNFTNMLgYTDPQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 246
Cdd:PRK14032  207 AENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMF 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 247 TQLQKEVGKDVSDEKLRDYIWNTLN------SGRVVpGYGHAVLRKTDPRYSCQREFAL-----KHLPKDpmFKLVAQLY 315
Cdd:PRK14032  286 EDIKENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNLYEKIE 362
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 316 KIVPNILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 368
Cdd:PRK14032  363 KLAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVGWSA 415
PRK14034 PRK14034
citrate synthase; Provisional
7-371 2.76e-31

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 122.57  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKGLVYETSVLDP--DEGIRFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSH 84
Cdd:PRK14034    5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  85 VVTMLDNFPTN-LHPMSQLSAAITALNSESNFARAYAEGMNRAKyweliyedCMDLIAKLPCVAAKIYRnlYREGSSIGA 163
Cdd:PRK14034   76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDEEANYRK--------AVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 164 IDSRLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 241
Cdd:PRK14034  146 PRKDLSLAANFLYMLNGEEPDEVEVeaFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 242 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA--LKHLPKDPM-FKLVAQLYKIV 318
Cdd:PRK14034  225 VMKMLTEIGEE-------ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720360295 319 PNilleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 371
Cdd:PRK14034  298 TK-------EKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHIL 342
PRK14035 PRK14035
citrate synthase; Provisional
7-370 2.20e-27

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 111.39  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKGLVY-ETSVLD-PDEGIRFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSH 84
Cdd:PRK14035    5 RGLEGVIAaETKISSiIDSQLTYAGYDIDDLA---------ENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  85 VVTMLDNFPT-NLHPMSQLSAAITALNSESNFARAYAEgmnrakywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGA 163
Cdd:PRK14035   76 VYQHFEEYSTdHVHPMTALRTSVSYLAHFDPDAEEESD--------EARYERAIRIQAKVASLVTAFAR--VRQGKEPLK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 164 IDSRLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 241
Cdd:PRK14035  146 PRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANER 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 242 VLVWLTQLqKEVGkDVSdeklrDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDPMFKlvaQLYKIVPNI 321
Cdd:PRK14035  225 VMDMLSEI-RSIG-DVD-----AYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMS-RKITKGTGRE---ELFEMSVKI 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720360295 322 LLEQGKAKNPWPNVDAHSGVLlqYYGM-TEMNYYTVLFGVSRALGVLAQL 370
Cdd:PRK14035  294 EKRMKEEKGLIPNVDFYSATV--YHVMgIPHDLFTPIFAVSRVAGWIAHI 341
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
51-375 2.56e-27

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 111.58  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  51 EGLFWLLVTGQMPTEEQVSWLS-REWAKRAALPShVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKyw 129
Cdd:PRK14033   50 EEVAYLLWNGELPTDAELALFSqRERAYRRLDRS-VLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADDSSPEANLAK-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 130 eliyedCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSRLDWSHNFTNM-LG-YTDPQFTELMRLYLTIHSDHeGGNVSAH 207
Cdd:PRK14033  127 ------ALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTF 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 208 TSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKT 287
Cdd:PRK14033  198 TARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHG 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 288 DPRYSCQREfALKHLPKDPMFKLVAQLYKIvpnilLEQG--KAKNPWPNVDAHSGVLlqYYGM---TEMnyYTVLFGVSR 362
Cdd:PRK14033  271 DSRVPTMKA-ALRRVAAVRDGQRWLDIYEA-----LEKAmaEATGIKPNLDFPAGPA--YYLMgfdIDF--FTPIFVMSR 340
                         330
                  ....*....|...
gi 1720360295 363 ALGVLAQLIWSRA 375
Cdd:PRK14033  341 ITGWTAHIMEQRA 353
PRK12349 PRK12349
citrate synthase;
8-371 6.41e-26

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 107.50  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   8 GMKGLVY-ET--SVLDPDEG-IRFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPS 83
Cdd:PRK12349    8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  84 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKyweliyedCMDLIAKLPCVAAKIYRNLyrEGSSIGA 163
Cdd:PRK12349   79 GVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSR--------AYKLLSKVPNIVANSYHIL--NNEEPIE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 164 IDSRLDWSHNFTNMLGYTDP--QFTELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 241
Cdd:PRK12349  149 PLKELSYSANFLYMLTGKKPteLEEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 242 VLVWLTQlqkevGKDVSD-EKLrdyIWNTLNSGRVVPGYGHAV-LRKTDPRYSCQREfALKHL-PKDPMFKLVAqlykiv 318
Cdd:PRK12349  228 VMYMLLE-----AGTVEKfEEL---LQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcDVKGDYTLYE------ 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360295 319 pniLLEQG-----KAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLI 371
Cdd:PRK12349  293 ---MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
PRK14037 PRK14037
citrate synthase; Provisional
19-371 1.86e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 100.59  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  19 LDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLH 97
Cdd:PRK14037   21 IDGEKGIlRYRGYNIED----LVNYGSYEE-----TIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  98 PMSQLSAAITALNS-ESNFarayaegmnraKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSHNFTN 176
Cdd:PRK14037   92 AIGLMEAAFAALASiDKNF-----------KWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 177 MLGYTDPQFTEL--MRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVLvwlTQLQkE 252
Cdd:PRK14037  159 ASFAREPTAEEIkaMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAF---KQFV-E 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 253 VGK-DVSDEKLRDyiwNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNP 331
Cdd:PRK14037  232 IGDpNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGI 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1720360295 332 WPNVDAHSGVLlqYYGMT-EMNYYTVLFGVSRALGVLAQLI 371
Cdd:PRK14037  309 YPNTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
24-375 4.12e-20

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


Pssm-ID: 99861 [Multi-domain]  Cd Length: 363  Bit Score: 90.83  E-value: 4.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  24 GIRFRGYSIpecqKMLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQL- 102
Cdd:cd06108    22 GLTYRGYDI----EDLAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMr 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 103 --SAAITALNSESNFARAYaEGMNRakyweliyedcmdLIAKLPCVAAKIYRnLYREGSSIGAIDSRLDWSHNFTNMLGY 180
Cdd:cd06108    93 tgCSMLGCLEPENEFSQQY-EIAIR-------------LLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLHG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 181 TDP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQkevgkdvS 258
Cdd:cd06108   158 KKPgeLEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-------S 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 259 DEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDPMFKLvaqLYKIVPNILLEQGKAKNPWPNVDAH 338
Cdd:cd06108   230 PEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPL---LYQISERIEEVMWEEKKLFPNLDFY 305
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1720360295 339 SGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRA 375
Cdd:cd06108   306 SASAYHFCGIpTEL--FTPIFVMSRVTGWAAHIMEQRA 341
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
7-385 2.33e-19

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


Pssm-ID: 99862 [Multi-domain]  Cd Length: 349  Bit Score: 88.52  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295   7 RGMKGLV-YETSVLDPD--EG-IRFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALP 82
Cdd:cd06109     1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED----LAGSASFEDVA-----ALLWNGFFPDLPELEEFRAALAAARALP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  83 SHVVTMLDNFpTNLHPMSQLSAAITALNSESNFARAyaegmnrakyweliyedcMDLIAKLPCVAAKIYRnlYREGSSIG 162
Cdd:cd06109    72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDLATA------------------LRLLAAAPVITAALLR--LSRGKQPI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 163 AIDSRLDWSHNFTNML-GYTDPQ-FTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 240
Cdd:cd06109   131 APDPSLSHAADYLRMLtGEPPSEaHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 241 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLPKDPMFKLVAQLYKIVPN 320
Cdd:cd06109   210 PVLDML----DAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGAPDERLEFAEAVEQAAL 281
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360295 321 ILLEQGKAKNP-WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 385
Cdd:cd06109   282 ALLREYKPGRPlETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
25-374 7.60e-15

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


Pssm-ID: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 75.27  E-value: 7.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  25 IRFRGYSIpecqkmLPKAKGGEEplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSA 104
Cdd:cd06117    23 LHYRGYDI------LDLAEKCEF---EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 105 AITALNSesnfARAYAEGMNRAKYweliyEDCMD-LIAKLPCVAAKIY---RNLYR-----EGSSIGAidsrldwshNFT 175
Cdd:cd06117    94 GVSVLGC----VLPEKEDHPVSGA-----RDIADrLMASLGSILLYWYhysHNGKRievetDDDSIGG---------HFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 176 NMLGYTDPQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEV 253
Cdd:cd06117   156 HLLHGEKPSesWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAF----EIQQRY 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 254 GKdvSDEKLRDyIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDP----MFKLVAQLYKIVPNIlleqgkaK 329
Cdd:cd06117   231 ES--ADEAEAD-IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGgdmkMFDIAERLETVMWEE-------K 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720360295 330 NPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSR 374
Cdd:cd06117   300 KMFPNLDWFSAVSYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12351 PRK12351
methylcitrate synthase; Provisional
56-375 2.42e-10

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 61.48  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295  56 LLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITAL------NSESNFARAYaegmnrakyw 129
Cdd:PRK12351   54 LLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR---------- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 130 eliyeDCMD-LIAKLPCVAAKIYR--------NLYREGSSIGAidsrldwsHnFTNMLGYTDPQ--FTELMRLYLTIHSD 198
Cdd:PRK12351  124 -----DIADrLLASLGSILLYWYHyshngrriEVETDDDSIGG--------H-FLHLLHGKKPSesWVKAMHTSLILYAE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 199 HEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANqEVLVwltQLQKevGKDVSDEKLRDyIWNTLNSGRVVPG 278
Cdd:PRK12351  190 HEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQ--RYDTPDEAEAD-IRRRVENKEVVIG 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 279 YGHAVLRKTDPRYSCQREFAlKHLPKDPMFKlvaQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVL 357
Cdd:PRK12351  262 FGHPVYTISDPRNKVIKEVA-KKLSKEAGDT---KLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVpTAM--FTPL 335
                         330
                  ....*....|....*...
gi 1720360295 358 FGVSRALGVLAQLIWSRA 375
Cdd:PRK12351  336 FVISRTTGWAAHVIEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
165-385 5.73e-10

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 60.36  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 165 DSRLDWSHNFTNML-----GYTDPQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLAN 239
Cdd:PRK12350  129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 240 QEVLVWLTqlqkEVGKDvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLPKdPMFKLVAQLYKIVP 319
Cdd:PRK12350  208 ARVLPMLD----AVERT---GDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRLGA-PRYEVAEAVEQAAL 278
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360295 320 NILleqgKAKNP----WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 385
Cdd:PRK12350  279 AEL----RERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
144-382 2.25e-03

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 40.19  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 144 PCVAAKIYRNLYREGSSIGAIDSRLdWshnFTNMLgytdPQF-TELMRLYLTIHSDHeGGNVS-AHTSHLVGSALSDPYL 221
Cdd:PLN02522  365 PCYAGVPMSSIIEKDYGVGDVISLL-W---FKRSL----PRYcTKFIEMCIMLCADH-GPCVSgAHNTIVTARAGKDLVS 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 222 SFAAAMNGLaGPLHGLANQEVLVWLtqlqkevgKDVSDEKL--RDYIWNTLNSGRVVPGYGHAVLRKT--DPRYSCQREF 297
Cdd:PLN02522  436 SLVSGLLTI-GPRFGGAIDDAARYF--------KDAYDRGLtpYEFVEGMKKKGIRVPGIGHRIKSRDnrDKRVELLQKY 506
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360295 298 ALKHLPKDPMFKLVAQlykiVPNILLEqgKAKNPWPNVDAHSGV----LLQYYGM---------TEMNYYTVLFGVSRAL 364
Cdd:PLN02522  507 ARTHFPSVKYMEYAVQ----VETYTLS--KANNLVLNVDGAIGSlfldLLAGSGMftkqeideiVEIGYLNGLFVLARSI 580
                         250
                  ....*....|....*...
gi 1720360295 365 GVLAQLIWSRALGFPLER 382
Cdd:PLN02522  581 GLIGHTFDQKRLKQPLYR 598
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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