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Conserved domains on  [gi|6325257|ref|NP_015325|]
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citrate (Si)-synthase CIT3 [Saccharomyces cerevisiae S288C]

Protein Classification

citrate synthase family protein; citrate/2-methylcitrate synthase( domain architecture ID 10149816)

citrate synthase family protein similar to citrate synthase that 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| citrate/2-methylcitrate synthase, citrate synthase forms citrate from oxaloacetate and acetyl-CoA; methylcitrate synthase catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also has minor citrate synthase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
29-474 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: 824.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   29 LKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGIDG 108
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  109 dNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGlI 188
Cdd:cd06106  81 -EMLPESMLWLLLTGKVPTFEQARGLSKELAERG-KLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKG-I 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  189 GKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLGQYSEEVDWCTNICSLLGMTNgtnssntcnltsqqSLDFINL 268
Cdd:cd06106 158 KKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGD--------------NLDFVDL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  269 MRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWK 348
Cdd:cd06106 224 LRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWK 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  349 ILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEfENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYH 428
Cdd:cd06106 304 TLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPEL-ENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYH 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 6325257  429 YGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:cd06106 383 YGIREFLYYTVIFGVSRALGPLTQLVWDRILGLPIERPKSLSLEGL 428
 
Name Accession Description Interval E-value
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
29-474 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: 824.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   29 LKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGIDG 108
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  109 dNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGlI 188
Cdd:cd06106  81 -EMLPESMLWLLLTGKVPTFEQARGLSKELAERG-KLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKG-I 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  189 GKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLGQYSEEVDWCTNICSLLGMTNgtnssntcnltsqqSLDFINL 268
Cdd:cd06106 158 KKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGD--------------NLDFVDL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  269 MRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWK 348
Cdd:cd06106 224 LRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWK 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  349 ILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEfENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYH 428
Cdd:cd06106 304 TLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPEL-ENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYH 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 6325257  429 YGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:cd06106 383 YGIREFLYYTVIFGVSRALGPLTQLVWDRILGLPIERPKSLSLEGL 428
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
27-474 3.23e-169

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: 483.63  E-value: 3.23e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257     27 LTLKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGi 106
Cdd:TIGR01793   2 LDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    107 DGDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKG 186
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARA-DLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    187 lIGKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLgQYSEEVDWCTNICSLLGMTNGtnssntcnltsqqslDFI 266
Cdd:TIGR01793 160 -IHKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSP---------------SFQ 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    267 NLMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYL 346
Cdd:TIGR01793 223 ELMRLYLTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    347 WKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRpieFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILF 426
Cdd:TIGR01793 303 WKTLNSGKVVPGYGHAVLRKTDPRYICQREFALKH---LPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLL 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 6325257    427 YHYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:TIGR01793 380 QYYGLTEARYYTVLFGVSRALGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
28-475 7.54e-147

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 426.86  E-value: 7.54e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    28 TLKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGiD 107
Cdd:PRK09569   2 QLKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAP-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   108 GDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRgRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGL 187
Cdd:PRK09569  81 SEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKR-QNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   188 IGKMEFWKDTLEDSLNLIASLPLLTGRIYsNITNEGHPLGQYSEEVDWCTNICSLLGmtngtnssntcnltsqQSLDFIN 267
Cdd:PRK09569 160 FNKMDAWEYMYEDASDLVARIPVIAAYIY-NLKYKGDKQIPSDPELDYGANFAHMIG----------------QPKPYKD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   268 LMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNIS-SIAREQEIKDYL 346
Cdd:PRK09569 223 VARMYFILHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGgEEPTKEQVEQAL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   347 WKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpiEFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILF 426
Cdd:PRK09569 303 WDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLK---HLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQ 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 6325257   427 YHYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGLE 475
Cdd:PRK09569 380 WYYGVKEWDFYTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLE 428
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
67-467 1.18e-114

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: 341.79  E-value: 1.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257     67 GMRGNQSMFWQGTSLDPEHG-IKFQGLTIEE-CQNrlpntgidgdnFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRK 144
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAER-----------SSFEEVAYLLLTGELPTKEELEEFSAELA-AHRE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    145 LPHYTEKVLSSLPKDMHPMTQLAIGLasmnkgSLFATNYQKGLIGKMEFWKDTLEDslNLIASLPLLTGRIYSNItnEGH 224
Cdd:pfam00285  69 LPEDVLELLRALPRDAHPMAVLRAAV------SALAAFDPEAISDKADYWENALRD--DLIAKLPTIAAYIYRHR--RGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    225 PLGQYSEEVDWCTNIcslLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYS 304
Cdd:pfam00285 139 PPIYPDPDLSYAENF---LYMLFGYEPDP----------EEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIA 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    305 SGIMGLAGPLHGLAAQEVVRFLIEmnsnissIAREQEIKDYLWKILNSN-RVIPGYGHAVLRKPDPRFTAMLEFAQKRPI 383
Cdd:pfam00285 205 AAIGALKGPLHGGANEAVLEMLEE-------IGSPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAE 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    384 EFENDKNVLLMQKLAEIAPKVLLEHgkSKNPFPNVDSASGILFYHYGIRELLfFTVIFGCSRAMGPLTQLVWDRILGlPI 463
Cdd:pfam00285 278 EGGDDPLLELAEELEEVAPEDLYFV--EKNLYPNVDFYSGVLYHALGIPTDM-FTPLFAISRTAGWLAHWIEQLADN-RI 353

                  ....
gi 6325257    464 ERPK 467
Cdd:pfam00285 354 IRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
79-469 4.08e-71

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: 230.75  E-value: 4.08e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   79 TSLDPEHGI-KFQGLTIEECQNrlpntgidgdNFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLP 157
Cdd:COG0372  28 SYIDGEKGIlRYRGYPIEDLAE----------KSSFEEVAYLLLYGELPTKEELAEFKAELA-RHRELPEEVKEFLDGFP 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  158 KDMHPMTQLAIGLASMnkgslfATNYQKGLIGKMEfwkDTLEDSLNLIASLPLLTGRIYsNITNeGHPLGQYSEEVDWCT 237
Cdd:COG0372  97 RDAHPMDVLRTAVSAL------GAFDPDADDIDPE---ARLEKAIRLIAKLPTIAAYAY-RYRR-GLPPVYPDPDLSYAE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  238 NIcslLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGL 317
Cdd:COG0372 166 NF---LYMLFGEEPDP----------EEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  318 AAQEVVRFLIEMNSnissiarEQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKL 397
Cdd:COG0372 232 ANEAVLEMLEEIGS-------PDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEEL 304
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325257  398 AEIAPKVllEHGKSKNPFPNVDSASGILFYHYGI-RELlfFTVIFGCSRAMGPLTQLVWDRIlGLPIERPKSL 469
Cdd:COG0372 305 EEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQI 372
 
Name Accession Description Interval E-value
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
29-474 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: 824.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   29 LKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGIDG 108
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  109 dNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGlI 188
Cdd:cd06106  81 -EMLPESMLWLLLTGKVPTFEQARGLSKELAERG-KLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKG-I 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  189 GKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLGQYSEEVDWCTNICSLLGMTNgtnssntcnltsqqSLDFINL 268
Cdd:cd06106 158 KKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGD--------------NLDFVDL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  269 MRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWK 348
Cdd:cd06106 224 LRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWK 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  349 ILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEfENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYH 428
Cdd:cd06106 304 TLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPEL-ENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYH 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 6325257  429 YGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:cd06106 383 YGIREFLYYTVIFGVSRALGPLTQLVWDRILGLPIERPKSLSLEGL 428
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
29-474 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: 559.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   29 LKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPntGIDG 108
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLP--KADG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  109 DNF-LPESMLWLLMTGGVPTFQQAASFRKELAIRGRkLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGL 187
Cdd:cd06103  79 GGEpLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAE-VPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  188 IGKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLGQYSEEVDWCTNICSLLGmtngtnssntcnltsQQSLDFIN 267
Cdd:cd06103 158 INKTTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLG---------------YEDEEFTD 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  268 LMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLW 347
Cdd:cd06103 223 LMRLYLTLHSDHEGGNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIW 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  348 KILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRpieFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFY 427
Cdd:cd06103 303 DTLNSGRVVPGYGHAVLRKTDPRFTCQREFALKH---LPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQ 379
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 6325257  428 HYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:cd06103 380 HYGMTEPQYYTVLFGVSRALGVLAQLVWSRALGLPIERPKSMSTEGL 426
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
29-477 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: 551.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   29 LKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNtGIDG 108
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPK-APGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  109 DNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGlI 188
Cdd:cd06105  80 EEPLPEGLFWLLLTGEVPTKEQVSALSKEWAARA-ALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEG-I 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  189 GKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHpLGQYSEEVDWCTNICSLLGMTNGtnssntcnltsqqslDFINL 268
Cdd:cd06105 158 HKSKYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGK-IIAIDSNLDWSANFANMLGYTDP---------------QFTEL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  269 MRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWK 348
Cdd:cd06105 222 MRLYLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWK 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  349 ILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpiEFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYH 428
Cdd:cd06105 302 TLNSGRVVPGYGHAVLRKTDPRYTCQREFALK---HLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQY 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 6325257  429 YGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGLEAL 477
Cdd:cd06105 379 YGLTEMNYYTVLFGVSRALGVLSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
27-474 3.23e-169

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: 483.63  E-value: 3.23e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257     27 LTLKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGi 106
Cdd:TIGR01793   2 LDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    107 DGDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGrKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKG 186
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARA-DLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    187 lIGKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLgQYSEEVDWCTNICSLLGMTNGtnssntcnltsqqslDFI 266
Cdd:TIGR01793 160 -IHKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSP---------------SFQ 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    267 NLMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYL 346
Cdd:TIGR01793 223 ELMRLYLTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    347 WKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRpieFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILF 426
Cdd:TIGR01793 303 WKTLNSGKVVPGYGHAVLRKTDPRYICQREFALKH---LPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLL 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 6325257    427 YHYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGL 474
Cdd:TIGR01793 380 QYYGLTEARYYTVLFGVSRALGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
28-475 7.54e-147

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 426.86  E-value: 7.54e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    28 TLKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGiD 107
Cdd:PRK09569   2 QLKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAP-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   108 GDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRgRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGL 187
Cdd:PRK09569  81 SEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKR-QNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   188 IGKMEFWKDTLEDSLNLIASLPLLTGRIYsNITNEGHPLGQYSEEVDWCTNICSLLGmtngtnssntcnltsqQSLDFIN 267
Cdd:PRK09569 160 FNKMDAWEYMYEDASDLVARIPVIAAYIY-NLKYKGDKQIPSDPELDYGANFAHMIG----------------QPKPYKD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   268 LMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNIS-SIAREQEIKDYL 346
Cdd:PRK09569 223 VARMYFILHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGgEEPTKEQVEQAL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   347 WKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpiEFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILF 426
Cdd:PRK09569 303 WDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLK---HLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQ 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 6325257   427 YHYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGLE 475
Cdd:PRK09569 380 WYYGVKEWDFYTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLE 428
PLN02456 PLN02456
citrate synthase
24-482 4.90e-123

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 367.04  E-value: 4.90e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    24 SSALTLKEALENVIPKKRDAVKKLKAcyGSTFVGPITISsvlGGMRGNQSMFWQGTSLDPEHGI-KFQGLTIEECQNRLP 102
Cdd:PLN02456  29 RTGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   103 NTGIdgdnflpesmLWLLMTGGVPTFQQAASFRKELAIRgRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATN 182
Cdd:PLN02456 104 FEEV----------AYLLLYGNLPTKEQLADWEAELRQH-SAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   183 YQKGlIGKMEFWKDTLEDSLNLIASLPLLTGRIYsnITNEGHPLGQYSEEVDWCTNICSLLGmtngtnSSNTCNLTSQQS 262
Cdd:PLN02456 173 YLRG-QHKYKSWEVRDEDIVRLIGKLPTLAAAIY--RRMYGRGPVIPDNSLDYAENFLYMLG------SLGDRSYKPDPR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   263 LDfiNLMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLiemnsniSSIAREQEI 342
Cdd:PLN02456 244 LA--RLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML-------KEIGTVENI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   343 KDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIApkVLLEHGKSKNPFPNVDSAS 422
Cdd:PLN02456 315 PEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYS 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325257   423 GILFYHYGIRElLFFTVIFGCSRAMGPLTQlvWDRILGLPIER---PKSLNL-EGLEALTKASN 482
Cdd:PLN02456 393 GVLLRALGFPE-EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYTgEWLRHYCPKAE 453
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
67-467 1.18e-114

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: 341.79  E-value: 1.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257     67 GMRGNQSMFWQGTSLDPEHG-IKFQGLTIEE-CQNrlpntgidgdnFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRK 144
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAER-----------SSFEEVAYLLLTGELPTKEELEEFSAELA-AHRE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    145 LPHYTEKVLSSLPKDMHPMTQLAIGLasmnkgSLFATNYQKGLIGKMEFWKDTLEDslNLIASLPLLTGRIYSNItnEGH 224
Cdd:pfam00285  69 LPEDVLELLRALPRDAHPMAVLRAAV------SALAAFDPEAISDKADYWENALRD--DLIAKLPTIAAYIYRHR--RGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    225 PLGQYSEEVDWCTNIcslLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYS 304
Cdd:pfam00285 139 PPIYPDPDLSYAENF---LYMLFGYEPDP----------EEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIA 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    305 SGIMGLAGPLHGLAAQEVVRFLIEmnsnissIAREQEIKDYLWKILNSN-RVIPGYGHAVLRKPDPRFTAMLEFAQKRPI 383
Cdd:pfam00285 205 AAIGALKGPLHGGANEAVLEMLEE-------IGSPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAE 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    384 EFENDKNVLLMQKLAEIAPKVLLEHgkSKNPFPNVDSASGILFYHYGIRELLfFTVIFGCSRAMGPLTQLVWDRILGlPI 463
Cdd:pfam00285 278 EGGDDPLLELAEELEEVAPEDLYFV--EKNLYPNVDFYSGVLYHALGIPTDM-FTPLFAISRTAGWLAHWIEQLADN-RI 353

                  ....
gi 6325257    464 ERPK 467
Cdd:pfam00285 354 IRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
66-469 3.24e-92

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: 284.49  E-value: 3.24e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   66 GGMRGNQSMFWQGTSLDPEHGI-KFQGLTIEECQNrlpntgidgdNFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRK 144
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAE----------KSSFEEVAYLLLYGKLPTKEELAEFKKKLA-SHRA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  145 LPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFAtnyqkgligKMEFWKDTLEDSLNLIASLPLLTGRIYSNItnEGH 224
Cdd:cd06118  70 LPEHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFA---------RDKSPEARYEKAIRLIAKLPTIAANIYRNR--EGL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  225 PLGQYSEEVDWCTNIcslLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYS 304
Cdd:cd06118 139 EIIAPDPDLSYAENF---LYMLFGEEPDP----------EEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIA 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  305 SGIMGLAGPLHGLAAQEVVRFLIEMNSNIssiareqEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIE 384
Cdd:cd06118 205 AAIAALKGPLHGGANEAVLKMLLEIGTPE-------NVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEE 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  385 FENDKNVLLMQKLAEIAPKVLLEhgksKNPFPNVDSASGILFYHYGIrELLFFTVIFGCSRAMGPLTQLVWDRILGLPIE 464
Cdd:cd06118 278 KGDDKLFEIAEELEEIALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLI 352

                ....*
gi 6325257  465 RPKSL 469
Cdd:cd06118 353 RPRAE 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
79-469 4.08e-71

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: 230.75  E-value: 4.08e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   79 TSLDPEHGI-KFQGLTIEECQNrlpntgidgdNFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLP 157
Cdd:COG0372  28 SYIDGEKGIlRYRGYPIEDLAE----------KSSFEEVAYLLLYGELPTKEELAEFKAELA-RHRELPEEVKEFLDGFP 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  158 KDMHPMTQLAIGLASMnkgslfATNYQKGLIGKMEfwkDTLEDSLNLIASLPLLTGRIYsNITNeGHPLGQYSEEVDWCT 237
Cdd:COG0372  97 RDAHPMDVLRTAVSAL------GAFDPDADDIDPE---ARLEKAIRLIAKLPTIAAYAY-RYRR-GLPPVYPDPDLSYAE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  238 NIcslLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGL 317
Cdd:COG0372 166 NF---LYMLFGEEPDP----------EEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  318 AAQEVVRFLIEMNSnissiarEQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKL 397
Cdd:COG0372 232 ANEAVLEMLEEIGS-------PDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEEL 304
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325257  398 AEIAPKVllEHGKSKNPFPNVDSASGILFYHYGI-RELlfFTVIFGCSRAMGPLTQLVWDRIlGLPIERPKSL 469
Cdd:COG0372 305 EEVALED--EYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQI 372
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
264-469 6.79e-67

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: 215.64  E-value: 6.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  264 DFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREqeik 343
Cdd:cd06101  70 EFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKNEPAEA---- 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  344 dYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPKVLLEhgksKNPFPNVDSASG 423
Cdd:cd06101 145 -YIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYE----KKLYPNVDFYSG 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6325257  424 ILFYHYGIrELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSL 469
Cdd:cd06101 220 VLYKAMGF-PTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAE 264
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
268-469 2.52e-66

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: 212.58  E-value: 2.52e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  268 LMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAReqeikDYLW 347
Cdd:cd06099  22 AMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLEEIGTPKNEPAE-----AYIR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  348 KILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPKVLLEhgksKNPFPNVDSASGILFY 427
Cdd:cd06099  96 KKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVLYE----KKLYPNVDFYSGVLYK 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6325257  428 HYGIrELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSL 469
Cdd:cd06099 172 AMGF-PTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSE 212
PRK14032 PRK14032
citrate synthase; Provisional
56-448 1.16e-34

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 135.03  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    56 VGPITISSVLGGMRGNQSMFwqgtsldPEHG-IKFQGLTIEEcqnrLPNTGIDGDNFLPESMLWLLMTGGVPTFQQAASF 134
Cdd:PRK14032  43 VGLTNIGDVHGYEIDDGEKI-------PDEGkLYYRGYDIKD----LVNGFLKEKRFGFEEVAYLLLFGELPTKEELAEF 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   135 RKELAIRgRKLPH-YTEKVLSSLP-KDMhpMTQLA---IGLASMNKG----SLfatnyqkgligkmefwKDTLEDSLNLI 205
Cdd:PRK14032 112 TELLGDY-RELPDgFTRDMILKAPsKDI--MNSLArsvLALYSYDDNpddtSI----------------DNVLRQSISLI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   206 ASLPLL---TGRIYSNITNEG-----HPLGQYS--EevdwctNICSLLgmtngtnsSNTCNLTSQQS--LDfINLMrlyt 273
Cdd:PRK14032 173 ARFPTLavyAYQAYRHYHDGKslyihPPKPELStaE------NILYML--------RPDNKYTELEArlLD-LALV---- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   274 gIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWKILNS- 352
Cdd:PRK14032 234 -LHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNKe 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   353 --NR--VIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPKVLLEH-GKSKNPFPNVDSASGILFY 427
Cdd:PRK14032 313 afDKsgLIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEKLAPELIAEErGIYKGVSANVDFYSGFVYD 392
                        410       420
                 ....*....|....*....|..
gi 6325257   428 HYGI-RELlfFTVIFGCSRAMG 448
Cdd:PRK14032 393 MLGIpEEL--YTPLFAIARIVG 412
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
108-448 1.29e-34

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: 133.93  E-value: 1.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  108 GDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRgRKLP-HYTEKVLSSLP-KD-MHPMTQLAIGLASMNKG----SLfa 180
Cdd:cd06113  55 ENRFGFEETAYLLLFGYLPNKEELEEFCEILSSY-RTLPdNFVEDVILKAPsKDiMNKLQRSVLALYSYDDKpddiSL-- 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  181 tnyqkgligkmefwKDTLEDSLNLIASLPLLTGRIYSNITnegHPLGQYS-------EEVDWCTNICSLLgmtngtNSSN 253
Cdd:cd06113 132 --------------ENVLRQSIQLIARLPTIAVYAYQAKR---HYYDGESlyihhpqPELSTAENILSML------RPDK 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  254 TCNLTSQQSLDFInLMrlytgIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNI 333
Cdd:cd06113 189 KYTELEAKLLDLC-LV-----LHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENV 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  334 SSIAREQEIKDYLWKILNSNR-----VIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPKVLLEH 408
Cdd:cd06113 263 KDWTDEDEVRAYLRKILNKEAfdksgLIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERIERLAPEVIAEE 342
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 6325257  409 -GKSKNPFPNVDSASGILFYHYGI-RELlfFTVIFGCSRAMG 448
Cdd:cd06113 343 rGIGKTVCANVDFYSGFVYKMLGIpQEL--YTPLFAVARIVG 382
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
81-458 1.99e-32

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: 127.15  E-value: 1.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   81 LDPEHGI-KFQGLTIEECQNRlpntgidgDNFlpESMLWLLMTGGVPTFQQAASFRKELAIRgRKLPHYTEKVLSSLPKD 159
Cdd:cd06112  18 IDGKNGIlEYRGYDIEELAEY--------SSF--EEVALLLLDGDLPTAAELEEFDKELRQH-RRVKYNIRDMMKCFPET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  160 MHPMTQLAIGLASMnkGSLFA-TNYQKGLigkmefwKDTLEDSL-NLIASLPLLTGrIYSNITNEGHPLgQYSEEVDWCT 237
Cdd:cd06112  87 GHPMDMLQATVAAL--GMFYPkPEVLKPN-------PDYIDAATvKLIAKMPTLVA-MWARIRNGDDPI-EPRPDLDYAE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  238 NicsLLGMTNGtnssntcnltSQQSLDFINLMRLYTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGL 317
Cdd:cd06112 156 N---FLYMLFG----------EEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGG 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  318 AAQEVVRFLIEmnsnissIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENdknvllMQKL 397
Cdd:cd06112 222 ANEDVLEMLEE-------IGSPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGE------LSKL 288
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325257  398 AEIA---PKVLLEHGKSKNPFPNVDSASGILFYHYGIRELLfFTVIFGCSRAMGPLT----QLVWDRI 458
Cdd:cd06112 289 YEIAlevERLCEELLGHKGVYPNVDFYSGIVYKELGIPADL-FTPIFAVARVAGWLAhwkeQLGDNRI 355
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
79-469 4.58e-31

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: 123.70  E-value: 4.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   79 TSLDPEHGI-KFQGLTIEECqnrlpntgIDGDNFlpESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLP 157
Cdd:cd06107  20 TYIDGDKGIlLYRGYPIEQL--------AESSTY--EEVAYLLLWGELPTQEQYDEFQRRLS-EHMMVPESVHRLIQTFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  158 KDMHPMTQLAIGLASMnkgSLFATNYQKGLIGKMEFWKDTLEDS--LNLIASLPLLTGRIYSNitNEGHPLGQYSEEVDW 235
Cdd:cd06107  89 RDAHPMGILCAGLSAL---SAFYPEAIPAHTGDLYQNNPEVRDKqiIRTLAKMPTIAAAAYCH--RIGRPFVYPRANLSY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  236 CTNICSLLGMTNgtNSSNTCNLTSQQSLDfinlmRLYTgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLH 315
Cdd:cd06107 164 IENFLYMMGYVD--QEPYEPNPRLARALD-----RLWI-LHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLH 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  316 GlAAQEVVrfliemNSNISSIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpIEFENDKNVLLmq 395
Cdd:cd06107 235 G-GANEAA------LKMLREIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHE--VLTEVEKDPLL-- 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325257  396 KLAEIAPKVLLEHG--KSKNPFPNVDSASGILFYHYGIrELLFFTVIFGCSRAMGPLTQlvWDRILGLP---IERPKSL 469
Cdd:cd06107 304 KVAMELERIALEDEyfVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPlqrIWRPRQV 379
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
114-448 2.53e-28

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: 115.45  E-value: 2.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  114 ESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLPKDMHPMTQLAIGLasmnkgSLFATNYQKGLIGKMEf 193
Cdd:cd06110  40 EEVAYLLWNGELPTAEELDAFKAQLA-AERELPAEIIDLLKLLPKDAHPMDVLRTAV------SALALYDPEADDMSRE- 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  194 wkDTLEDSLNLIASLPLLTGRIysnitnegHPLGQYSEEVDWCTNIC---SLLGMTNGtnssntcNLTSQQSLDFINLMR 270
Cdd:cd06110 112 --ANLRKAIRLIAKMPTIVAAF--------HRIRNGLEPVAPDPDLShaaNFLYMLTG-------EKPSEEAARAFDVAL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  271 LytgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSnissiarEQEIKDYLWKIL 350
Cdd:cd06110 175 I---LHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGS-------VDNVAAYVKDKL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  351 NSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIApkvllehGKSKNPFPNVDSASGILFYHYG 430
Cdd:cd06110 244 ANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAM-------RDEKGLNPNVDFYSASVYYMLG 316
                       330
                ....*....|....*...
gi 6325257  431 IRELLfFTVIFGCSRAMG 448
Cdd:cd06110 317 IPVDL-FTPIFAISRVSG 333
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
79-469 1.38e-24

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: 105.60  E-value: 1.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   79 TSLDPEHGI-KFQGLTIEECQNRlpntgidgDNFLPESmlWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLP 157
Cdd:cd06115  40 SYIDGDKGIlRYRGYPIEELAEK--------STFLEVA--YLLIYGNLPTKSQLSDWEFAVS-QHTAVPTGVLDMIKSFP 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  158 KDMHPMTQLAIGLASMnkgSLFATNYQKGLIGKMEFWKDTLEDS--LNLIASLPLLTGRIYSNITneGHPLGQYSEEVDW 235
Cdd:cd06115 109 HDAHPMGMLVSAISAL---SAFHPEANPALAGQDIYKNKQVRDKqiVRILGKAPTIAAAAYRRRA--GRPPNLPSQDLSY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  236 CTNICSLLGMTNGTNSSNTCNLTSQQSLDFInlmrlytgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLH 315
Cdd:cd06115 184 TENFLYMLDSLGERKYKPNPRLARALDILFI--------LHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLH 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  316 GLAAQEVVRFLIEmnsnissIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpiEFEndknVLLMQ 395
Cdd:cd06115 255 GGANEAVLRMLAE-------IGTVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADE---VFE----IVGKD 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  396 KLAEIA---PKVLL--EHGKSKNPFPNVDSASGILFYHYGIrELLFFTVIFGCSRAMGPLTQlvWDRIL---GLPIERPK 467
Cdd:cd06115 321 PLIEIAvalEKAALsdEYFVKRKLYPNVDFYSGLIYRAMGF-PTDFFPVLFAIPRMAGYLAH--WRESLddpDTKIMRPQ 397

                ..
gi 6325257  468 SL 469
Cdd:cd06115 398 QL 399
PRK14036 PRK14036
citrate synthase; Provisional
81-458 1.03e-23

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 102.34  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    81 LDPEHGI-KFQGLTIEECQNRlpntgidgDNFLPESmlWLLMTGGVPTFQQAASFRKELAIRgRKLPHYTEKVLSSLPKD 159
Cdd:PRK14036  21 VDGQKGIlEYRGYPIEELAEK--------SSFLETA--YLLIWGELPTAEELEEFEQEVRMH-RRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   160 MHPMTQLAIGLASMnkgSLFatnYQKGLIGKMEFWKDTLedsLNLIASLPLLTGrIYSNITNEGHPLgQYSEEVDWCTNi 239
Cdd:PRK14036  90 GHPMDALQASAAAL---GLF---YSRRALDDPEYIRDAV---VRLIAKIPTMVA-AFQLIRKGNDPI-QPRDDLDYAAN- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   240 csLLGMTNGTNSSNTcnltSQQSLDfINLMrlytgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAA 319
Cdd:PRK14036 158 --FLYMLTEREPDPL----AARIFD-RCLI-----LHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGAN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   320 QEVVRFLIEmnsnissIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDknvllmqKLAE 399
Cdd:PRK14036 225 EDVLAMLEE-------IGSVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHD-------EYYE 290
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325257   400 IA---PKVLLEHGKSKNPFPNVDSASGILFYHYGIRELLfFTVIFGCSRAMGPLT----QLVWDRI 458
Cdd:PRK14036 291 IAlelERVAEERLGPKGIYPNVDFYSGLVYRKLGIPRDL-FTPIFAIARVAGWLAhwreQLGANRI 355
PRK14037 PRK14037
citrate synthase; Provisional
79-448 2.41e-22

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 98.28  E-value: 2.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257    79 TSLDPEHGI-KFQGLTIEEcqnrLPNTGIDgdnflpESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLP 157
Cdd:PRK14037  19 TFIDGEKGIlRYRGYNIED----LVNYGSY------EETIYLMLYGELPTKKELNDLKEKLN-EEYEVPQEVIDSIYLMP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   158 KDMHpmtqlAIGLASMNKGSLFAtnyqkglIGKMEFWKDTLED-SLNLIASLPLLTGRIYSNITNEG----HPLGQYSEe 232
Cdd:PRK14037  88 RDSD-----AIGLMEAAFAALAS-------IDKNFKWKENDKEkAISIIAKMATIVANVYRRKEGNKpripEPSDSFAE- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   233 vdwctnicSLLGMTNGTNSSNtcnltsqqslDFINLMRLYTGIHVDHEggnVSAHTTH-LVG-SALSDPYLSYSSGIMGL 310
Cdd:PRK14037 155 --------SFLLASFAREPTA----------EEIKAMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAAL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   311 AGPLHGLAAQEVVRFLIEmnsnISSIAREQEikdylW---KILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPiefEN 387
Cdd:PRK14037 214 KGPLHGGAAEEAFKQFVE----IGDPNNVEM-----WfndKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLI---ER 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325257   388 DKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYHYGIrELLFFTVIFGCSRAMG 448
Cdd:PRK14037 282 NSEAKKYFEIAQKLEELGIKQFGSKGIYPNTDFYSGIVFYALGF-PVYMFTALFALSRTLG 341
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
114-448 5.75e-22

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: 96.99  E-value: 5.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  114 ESMLWLLMTGGVPTFQQAASFRKELaIRGRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMnkGSLFATNYQKgligkmef 193
Cdd:cd06108  40 EEVAYLLLYGKLPTRKQLDAYKTKL-VALRRLPAALKTVLELIPKDSHPMDVMRTGCSML--GCLEPENEFS-------- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  194 wkDTLEDSLNLIASLP--LLTGRIYSnitnegHPLGQYSEEVDWCTNICSLLGMTNGTNSSNtcnltsqqslDFINLMRL 271
Cdd:cd06108 109 --QQYEIAIRLLAIFPsiLLYWYHYS------HSGKRIETETDEDSIAGHFLHLLHGKKPGE----------LEIKAMDV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  272 YTGIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGlAAQEVVRFLIEmnsNISSIareQEIKDYLWKILN 351
Cdd:cd06108 171 SLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHG-GANEAAMELIE---RFKSP---EEAEQGLLEKLE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  352 SNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKnvllMQKLAEIAPKVLLEhgkSKNPFPNVD--SASGilfYHY 429
Cdd:cd06108 243 RKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPL----LYQISERIEEVMWE---EKKLFPNLDfySASA---YHF 312
                       330       340
                ....*....|....*....|
gi 6325257  430 -GIRELLfFTVIFGCSRAMG 448
Cdd:cd06108 313 cGIPTEL-FTPIFVMSRVTG 331
gltA PRK05614
citrate synthase;
118-469 6.22e-20

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 91.86  E-value: 6.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   118 WLLMTGGVPTFQQAASFRKElaIRGRKLPHytEKV---LSSLPKDMHPMTQLAIGLASMnkgslfATNYQkgligkmefw 194
Cdd:PRK05614  90 YLLLYGELPTAEQKAEFDTT--VTRHTMVH--EQLkrfFRGFRRDAHPMAVLCGVVGAL------SAFYH---------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   195 kdtleDSLN-------------LIASLPLLTGRIYSNitNEGHPLGQYSEEVDWCTNIcslLGMTNGTNSSN-TCNLTSQ 260
Cdd:PRK05614 150 -----DSLDindpehreiaairLIAKMPTLAAMAYKY--SIGQPFVYPRNDLSYAENF---LRMMFATPCEEyEVNPVLV 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   261 QSLDfinlmRLYTgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNS--NISS-IA 337
Cdd:PRK05614 220 RALD-----RIFI-LHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSvdNIPEfIA 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   338 ReqeIKDylwKilNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVL-LMQKLAEIAPKVllEHGKSKNPFP 416
Cdd:PRK05614 293 R---AKD---K--NDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLeVAMELEEIALND--EYFIERKLYP 362
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325257   417 NVDSASGILFYHYGIrELLFFTVIFGCSRAMGPLTQlvWDRILGLP---IERPKSL 469
Cdd:PRK05614 363 NVDFYSGIILKALGI-PTSMFTVIFALARTVGWIAH--WNEMHSDPeqkIGRPRQL 415
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
79-469 1.65e-19

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: 90.27  E-value: 1.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   79 TSLDPEHGI-KFQGLTIEECQNRlpntgidgDNFLpeSMLWLLMTGGVPTFQQAASFrkELAIRGRKLPHYT-EKVLSSL 156
Cdd:cd06116  20 TYIDGEKGIlRYRGYPIEQLAEQ--------SSYL--EVAYLLLHGELPTKERLAQW--VYDITRHTMTHENlKKFMDGF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  157 PKDMHPMTQLAIGLASMNKGSLFATNYQKGLIGKMEFWKdtledslnLIASLPLLTGRIYSNitNEGHPLGQYSEEVDWC 236
Cdd:cd06116  88 RYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIR--------LIGKMPTIAAFAYRH--RLGLPYVLPDNDLSYT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  237 TNICSLLGMTNGTNSSNTCNLTSQQSLDFInlmrlytgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHG 316
Cdd:cd06116 158 GNFLSMLFKMTEPKYEPNPVLAKALDVLFI--------LHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  317 LAAQEVVRFLIEmnsnissIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpIEFENDKNVLLmqK 396
Cdd:cd06116 229 GANEAVLRMLQQ-------IGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADE--VFEATGRNPLL--D 297
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325257  397 LAEIAPKVLL--EHGKSKNPFPNVDSASGILFYHYGIrELLFFTVIFGCSRAMGPLTQlvWDRILGLP---IERPKSL 469
Cdd:cd06116 298 IAVELEKIALedEYFISRKLYPNVDFYSGLIYQALGF-PTEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQV 372
PRK14035 PRK14035
citrate synthase; Provisional
109-448 2.49e-18

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 86.35  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   109 DNFLPESMLWLLMTGGVPTFQQAASFRKEL----AIRGRKLPHYTEKVLSSLpkdmHPMTQLAIGLASMNKGSLFATNyq 184
Cdd:PRK14035  37 ENASFEEVIFLLWNYRLPTEEELAHLKGKLrkymTLNDRVYQHFEEYSTDHV----HPMTALRTSVSYLAHFDPDAEE-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   185 kgligkmEFWKDTLEDSLNLIASLPLLTGRiYSNITNEGHPLgQYSEEVDWCTNicsLLGMTNGTNSSNTcnltsqQSLD 264
Cdd:PRK14035 111 -------ESDEARYERAIRIQAKVASLVTA-FARVRQGKEPL-KPRPDLSYAAN---FLYMLRGELPTDI------EVEA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   265 FINLMRLytgiHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSnissiarEQEIKD 344
Cdd:PRK14035 173 FNKALVL----HADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRS-------IGDVDA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   345 YLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpIEFENDKNVLLmqklaEIAPKVLLEHGKSKNPFPNVDSASGI 424
Cdd:PRK14035 241 YLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRK--ITKGTGREELF-----EMSVKIEKRMKEEKGLIPNVDFYSAT 313
                        330       340
                 ....*....|....*....|....
gi 6325257   425 LFYHYGIRELLfFTVIFGCSRAMG 448
Cdd:PRK14035 314 VYHVMGIPHDL-FTPIFAVSRVAG 336
PRK12349 PRK12349
citrate synthase;
116-448 1.52e-16

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 80.92  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   116 MLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMnkgslfaTNYQKGLIGKMEfwK 195
Cdd:PRK12349  48 IVHLLLEEHLPNEDEKATLEKKLK-EEYAVPEGVFNILKALPKETHPMDGLRTGVSAL-------AGYDNDIEDRSL--E 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   196 DTLEDSLNLIASLPLLTGRIYSNITNEG--HPLGQ--YSEevdwctnicSLLGMTNGTNSsntcnlTSQQSLDFINLMRL 271
Cdd:PRK12349 118 VNKSRAYKLLSKVPNIVANSYHILNNEEpiEPLKElsYSA---------NFLYMLTGKKP------TELEEKIFDRSLVL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   272 YTgihvDHEGGNvSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSnissiarEQEIKDYLWKILN 351
Cdd:PRK12349 183 YS----EHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGT-------VEKFEELLQKKLY 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   352 SNRVIPGYGHAV-LRKPDPRfTAMLEFAQKRPIEFENDKNVLLMqklAEIAPKVLLEhgkSKNPFPNVDSASGILFYHYG 430
Cdd:PRK12349 251 NKEKIMGFGHRVyMKKMDPR-ALMMKEALKQLCDVKGDYTLYEM---CEAGEKIMEK---EKGLYPNLDYYAAPVYWMLG 323
                        330
                 ....*....|....*...
gi 6325257   431 IRELLfFTVIFGCSRAMG 448
Cdd:PRK12349 324 IPIQL-YTPIFFSSRTVG 340
PRK14034 PRK14034
citrate synthase; Provisional
105-448 2.62e-15

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 77.50  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   105 GID--GDNFLPESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLPKD-MHPMTQL--AIGLAS------- 172
Cdd:PRK14034  31 NIDdlAENASFEEVVYLLWHRKLPNKQELAEFKEQLS-ENAKVPGEIIEHLKQYDLKkVHPMSVLrtAISMLGlydeeae 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   173 -MNKgslfATNYQKGLigkmefwkdtledslNLIASLPLLTGrIYSNITNEGHPLgQYSEEVDWCTNicsLLGMTNGTNS 251
Cdd:PRK14034 110 iMDE----EANYRKAV---------------RLQAKVPTIVA-AFSRIRKGLDPV-EPRKDLSLAAN---FLYMLNGEEP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   252 SNTcnltsqqSLDFINLMRLytgIHVDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEmns 331
Cdd:PRK14034 166 DEV-------EVEAFNKALV---LHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTE--- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   332 nissIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPkvllehgKS 411
Cdd:PRK14034 232 ----IGEEENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVT-------KE 300
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 6325257   412 KNPFPNVDSASGILFYHYGIRELLfFTVIFGCSRAMG 448
Cdd:PRK14034 301 KGLPPNVDFYSASVYHCLGIDHDL-FTPIFAISRMSG 336
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
114-448 1.56e-13

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 71.91  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   114 ESMLWLLMTGGVPTFQQAASFRKelaiRGRKLPHYTEKVLS---SLPKDMHPMTQL--AIGLASMNKGSLF----ATNYQ 184
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQ----RERAYRRLDRSVLSlidKLPTTCHPMDVVrtAVSYLGAEDPEADdsspEANLA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   185 KgligkmefwkdtledSLNLIASLPLLTGRIYSNitNEGHPLGQYSEEVDWCTNicsLLGMTNGTNSSNTCNLTSQQSld 264
Cdd:PRK14033 126 K---------------ALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAEN---FLHMCFGEVPEPEVVRAFEVS-- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   265 finlMRLYTgihvDHeGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEmnsnissIAREQEIKD 344
Cdd:PRK14033 184 ----LILYA----EH-SFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLE-------IGDPARAAE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   345 YLWKILNSNRVIPGYGHAVLRKPDPRFTAMlEFAQKRPIEFENDKNVLlmqKLAEIAPKVLLEhgkSKNPFPNVDSASGI 424
Cdd:PRK14033 248 WLRDALARKEKVMGFGHRVYKHGDSRVPTM-KAALRRVAAVRDGQRWL---DIYEALEKAMAE---ATGIKPNLDFPAGP 320
                        330       340
                 ....*....|....*....|....
gi 6325257   425 LFYHYGIrELLFFTVIFGCSRAMG 448
Cdd:PRK14033 321 AYYLMGF-DIDFFTPIFVMSRITG 343
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
114-448 1.12e-11

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: 66.17  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  114 ESMLWLLMTGGVPTFQQAASFRKELAiRGRKLPHYTEKVLSSLpKDMHPMTQLAIGLASMNKGslfatnyqkgligkmef 193
Cdd:cd06109  40 EDVAALLWNGFFPDLPELEEFRAALA-AARALPDVVAALLPAL-AGLDPMDALRALLALLPDS----------------- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  194 wkDTLEDSLNLIASLPLLT------GRIYSNItnegHPLGQYSEEVDwctnicsLLGMTNGTNSSNTCnltsQQSLDfin 267
Cdd:cd06109 101 --PDLATALRLLAAAPVITaallrlSRGKQPI----APDPSLSHAAD-------YLRMLTGEPPSEAH----VRALD--- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  268 lmrLYTGIHVDHeGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVvrflIEMnsnISSIAREQEIKDYLW 347
Cdd:cd06109 161 ---AYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPV----LDM---LDAIGTPENAEAWLR 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  348 KILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQkrpiEFENDKNVLLMQKLAEIAPKVLLEHGKSKNPF-PNVDSASGILF 426
Cdd:cd06109 230 EALARGERLMGFGHRVYRVRDPRADVLKAAAE----RLGAPDERLEFAEAVEQAALALLREYKPGRPLeTNVEFYTALLL 305
                       330       340
                ....*....|....*....|...
gi 6325257  427 YHYGI-RELlfFTVIFGCSRAMG 448
Cdd:cd06109 306 EALGLpREA--FTPTFAAGRTAG 326
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
114-477 6.69e-11

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: 63.71  E-value: 6.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  114 ESMLWLLMTGGVPTFQQAASFRKEL-AIRGrkLPHYTEKVLSSLPKDMHPMTQLAIGLASMnkGSLFATNYQKGLIGKme 192
Cdd:cd06117  40 EEVAHLLVHGKLPTKSELAAYKTKLkSLRG--LPANVKTALEQLPAAAHPMDVMRTGVSVL--GCVLPEKEDHPVSGA-- 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  193 fwKDTLEdslNLIASLP--LLTGRIYSnitnegHPLGQYSEEVDWCTNICSLLGMTNGTNSSNTCNLTSQQSLDfinlmr 270
Cdd:cd06117 114 --RDIAD---RLMASLGsiLLYWYHYS------HNGKRIEVETDDDSIGGHFLHLLHGEKPSESWEKAMHISLI------ 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  271 LYTgihvDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGlAAQEVVrFLIEMNSNISSIArEQEIKdylwKIL 350
Cdd:cd06117 177 LYA----EHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHG-GANEVA-FEIQQRYESADEA-EADIR----RRV 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  351 NSNRVIPGYGHAVLRKPDPRFTAMLEFAQKrpieFENDKNVLLMQKLAEIAPKVLLEhgkSKNPFPNVDSASGILFYHYG 430
Cdd:cd06117 245 ENKEVVIGFGHPVYTIADPRNQVIKEVAKQ----LSKEGGDMKMFDIAERLETVMWE---EKKMFPNLDWFSAVSYHMMG 317
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6325257  431 IRELLfFTVIFGCSRAMGPLTQLVWDRILGlPIERPkSLNLEGLEAL 477
Cdd:cd06117 318 VPTAM-FTPLFVIARTTGWSAHIIEQRQDG-KIIRP-SANYTGPEDL 361
PRK12351 PRK12351
methylcitrate synthase; Provisional
114-448 5.71e-10

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 61.09  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   114 ESMLWLLMTGGVPTFQQAASFRKEL-AIRGrkLPHYTEKVLSSLPKDMHPMTQLAIGlASMnkgslfatnyqkglIGKME 192
Cdd:PRK12351  49 EEVAHLLVHGKLPTQAELAAYKTKLkALRG--LPAAVKTVLEAIPAAAHPMDVMRTG-VSV--------------LGCLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   193 FWKD--TLEDSLN----LIASLP--LL-------TGRIYSNITNE----GHplgqyseevdwctnicsLLGMTNGTNSSN 253
Cdd:PRK12351 112 PEKEdhNFSGARDiadrLLASLGsiLLywyhyshNGRRIEVETDDdsigGH-----------------FLHLLHGKKPSE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   254 TCNLTSQQSLDfinlmrLYTgihvDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGlAAQEVVrflIEMNSNI 333
Cdd:PRK12351 175 SWVKAMHTSLI------LYA----EHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHG-GANEVA---FEIQQRY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   334 SSiarEQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKnvllMQKLAEIAPKVLLEhgkSKN 413
Cdd:PRK12351 240 DT---PDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTK----LYDIAERLETVMWE---EKK 309
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 6325257   414 PFPNVD--SASGilfYHY-GIRELLfFTVIFGCSRAMG 448
Cdd:PRK12351 310 MFPNLDwfSAVS---YHMmGVPTAM-FTPLFVISRTTG 343
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
277-421 7.58e-10

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. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 59.97  E-value: 7.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  277 VDHEGgNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMnsnissiAREQEIKDYLWKILNSNRVI 356
Cdd:cd06102 109 ADHEL-NASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEA-------LRAGDAEAAVRERLRRGEAL 180
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325257  357 PGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDknvllMQKLAEIAPKVLLEHgksknpfPNVDSA 421
Cdd:cd06102 181 PGFGHPLYPDGDPRAAALLAALRPLGPAAPPA-----ARALIEAARALTGAR-------PNIDFA 233
PRK12350 PRK12350
citrate synthase 2; Provisional
278-448 4.95e-07

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 51.50  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   278 DHeGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVvrflIEMnsnISSIAREQEIKDYLWKILNSNRVIP 357
Cdd:PRK12350 167 EH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARV----LPM---LDAVERTGDARGWVKGALDRGERLM 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   358 GYGHAVLRKPDPRFTAM-----------LEFAQKrpIEfendKNVLlmQKLAEIAPKVLLEhgksknpfPNVDSASGILF 426
Cdd:PRK12350 239 GFGHRVYRAEDPRARVLratakrlgaprYEVAEA--VE----QAAL--AELRERRPDRPLE--------TNVEFWAAVLL 302
                        170       180
                 ....*....|....*....|...
gi 6325257   427 YHYGI-RELlfFTVIFGCSRAMG 448
Cdd:PRK12350 303 DFAGVpAHM--FTAMFTCGRTAG 323
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
277-459 4.97e-06

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. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. 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; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.


Pssm-ID: 99854 [Multi-domain]  Cd Length: 227  Bit Score: 47.56  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  277 VDHEGGNVSAHTTHLVGSALSDPYLS-YSSGIMGlAGPLHGLAAQEVVRFLIEMNSNISSIARE-QEIKDYLWKilnSNR 354
Cdd:cd06100  42 ADHGPATPSAHAARLTASAGPEDLQSaVAAGLLG-IGDRFGGAGEGAARLFKEAVDSGDALDAAaAEFVAEYRA---AKK 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257  355 VIPGYGHAVLRKPDPRFTAMLEFAQKRPIEfendkNVLLmqKLAEIAPKVLLEhgKSKNPFP-NVDSASGILFYHYGI-R 432
Cdd:cd06100 118 RIPGFGHPVHKNPDPRVPRLLELARELGPA-----GPHL--DYALAVEKALTA--AKGKPLPlNVDGAIAAILLDLGFpP 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6325257  433 ELLFFTVIFGcsRAMG-------------PLTQLVWDRIL 459
Cdd:cd06100 189 GALRGLFVLG--RSPGliahaleekrlgqPLYRHPWDDIE 226
PRK06224 PRK06224
citryl-CoA lyase;
304-448 2.34e-03

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 39.85  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325257   304 SSGIMGLaGPLHGLAAQEVVRFLIEMNSNISS-IAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRP 382
Cdd:PRK06224  92 AAGLLAL-GSVHGGAGEQAAELLQEIAAAADAgADLDAAARAIVAEYRAAGKRVPGFGHPLHKPVDPRAPRLLALAREAG 170
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325257   383 IefeNDKNVLLMQKLAEIAPKVlleHGKsknPFP-NVDSASGILFYHYGI--RELLFFTVIfgcSRAMG 448
Cdd:PRK06224 171 V---AGRHCRLAEALEAALAAA---KGK---PLPlNVDGAIAAILADLGFppALARGLFVI---SRAAG 227
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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