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Conserved domains on  [gi|429242423|ref|NP_593718|]
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citrate synthase Cit1 [Schizosaccharomyces pombe]

Protein Classification

citrate synthase( domain architecture ID 10149814)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
52-479 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: 878.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANnEEFVELMRLYLTIHADHEGGNVSA 291
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTD-PQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 292 HTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRK 371
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 372 TDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGV 451
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*...
gi 429242423 452 ASQLIWDRALGLPIERPKSFSTEALKKM 479
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
52-479 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: 878.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANnEEFVELMRLYLTIHADHEGGNVSA 291
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTD-PQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 292 HTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRK 371
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 372 TDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGV 451
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*...
gi 429242423 452 ASQLIWDRALGLPIERPKSFSTEALKKM 479
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
52-476 0e+00

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


Pssm-ID: 130853  Cd Length: 427  Bit Score: 742.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423   52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:TIGR01793   4 LKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:TIGR01793  84 EPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIHKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFaNNEEFVELMRLYLTIHADHEGGNVSA 291
Cdd:TIGR01793 164 KYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGY-DSPSFQELMRLYLTIHSDHEGGNVSA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  292 HTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRK 371
Cdd:TIGR01793 243 HTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVLRK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  372 TDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGV 451
Cdd:TIGR01793 323 TDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGI 402
                         410       420
                  ....*....|....*....|....*
gi 429242423  452 ASQLIWDRALGLPIERPKSFSTEAL 476
Cdd:TIGR01793 403 LSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
52-483 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 591.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERG-MNK 210
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 211 HDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFAnnEEFVELMRLYLTIHADHEGGNVS 290
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQIPSDPELDYGANFAHMIGQP--KPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLS-EETIKSYLWKLLNSGRVVPGYGHAVL 369
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 370 RKTDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTL 449
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 429242423 450 GVASQLIWDRALGLPIERPKSFSTEALKKMVETK 483
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
90-469 3.84e-127

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: 373.76  E-value: 3.84e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423   90 GARGVRSLIWEGSVLDPNEG-IRFRGYTIPEcqkLLPSSPngkqplPESLFWLLVTGEIPTLSQVQALSADWAARSQLPK 168
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  169 FVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAkayerGMNKHDYWKYEYEDcmDLIAKTVPIAGRIYRNLYRDGVVAPi 248
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLPPIYP- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  249 QMDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEV 327
Cdd:pfam00285 144 DPDLSYAENFLYMLfGYEPDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  328 LNFLitmkKEIGddlSEETIKSYLWKLLNSG-RVVPGYGHAVLRKTDPRYTAQREFALEHLPK---DPMFQLVSRLYEIV 403
Cdd:pfam00285 223 LEML----EEIG---SPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEEVA 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429242423  404 PGVLTEHGktKNPYPNVDSHSGVLLQYYGLKEQsFYTVLFGVSRTLGVASQLIWDRALGlPIERPK 469
Cdd:pfam00285 296 PEDLYFVE--KNLYPNVDFYSGVLYHALGIPTD-MFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
102-470 1.03e-93

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: 289.30  E-value: 1.03e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 102 SVLDPNEGI-RFRGYTIPECQKllpsspngkQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPT 180
Cdd:COG0372   28 SYIDGEKGIlRYRGYPIEDLAE---------KSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGFPRD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 181 LHPMAQFSLAVTALehdSAFakaYERGMNkHDYwKYEYEDCMDLIAKTVPIAGRIYRnlYRDG--VVAPiqmDKDHSY-- 256
Cdd:COG0372   99 AHPMDVLRTAVSAL---GAF---DPDADD-IDP-EARLEKAIRLIAKLPTIAAYAYR--YRRGlpPVYP---DPDLSYae 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 257 NFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLitmk 335
Cdd:COG0372  166 NFLYMLfGEEPDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEML---- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 336 KEIGDdlsEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHLPKDPMFQLVSRLYEIVPGvlTEHGK 412
Cdd:COG0372  241 EEIGS---PDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEVALE--DEYFI 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 429242423 413 TKNPYPNVDSHSGVLLQYYGLKEqSFYTVLFGVSRTLGVASQLIWDRAlGLPIERPKS 470
Cdd:COG0372  316 EKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
52-479 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: 878.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANnEEFVELMRLYLTIHADHEGGNVSA 291
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTD-PQFTELMRLYLTIHSDHEGGNVSA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 292 HTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRK 371
Cdd:cd06105  240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 372 TDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGV 451
Cdd:cd06105  320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                        410       420
                 ....*....|....*....|....*...
gi 429242423 452 ASQLIWDRALGLPIERPKSFSTEALKKM 479
Cdd:cd06105  400 LSQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
52-476 0e+00

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


Pssm-ID: 130853  Cd Length: 427  Bit Score: 742.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423   52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:TIGR01793   4 LKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:TIGR01793  84 EPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGIHKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFaNNEEFVELMRLYLTIHADHEGGNVSA 291
Cdd:TIGR01793 164 KYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGY-DSPSFQELMRLYLTIHSDHEGGNVSA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  292 HTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRK 371
Cdd:TIGR01793 243 HTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVLRK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  372 TDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGV 451
Cdd:TIGR01793 323 TDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRALGI 402
                         410       420
                  ....*....|....*....|....*
gi 429242423  452 ASQLIWDRALGLPIERPKSFSTEAL 476
Cdd:TIGR01793 403 LSQLIWDRALGLPLERPKSVSTEWL 427
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
52-476 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: 712.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:cd06103    1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERG-MNK 210
Cdd:cd06103   81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 211 HDYWKYEYEDCMDLIAKTVPIAGRIYRNLY-RDGVVAPIQMDKDHSYNFANVLGFaNNEEFVELMRLYLTIHADHEGGNV 289
Cdd:cd06103  161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYrKGGEIGAIDSKLDWSANFAHMLGY-EDEEFTDLMRLYLTLHSDHEGGNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 290 SAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVL 369
Cdd:cd06103  240 SAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 370 RKTDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTL 449
Cdd:cd06103  320 RKTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRAL 399
                        410       420
                 ....*....|....*....|....*..
gi 429242423 450 GVASQLIWDRALGLPIERPKSFSTEAL 476
Cdd:cd06103  400 GVLAQLVWSRALGLPIERPKSMSTEGL 426
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
52-476 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: 652.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:cd06106    1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKH 211
Cdd:cd06106   81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 212 DYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAP-IQMDKDHSYNFANVLGFANNEEFVELMRLYLTIHADHEGGNVS 290
Cdd:cd06106  161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGkIDPEVDWSYNFTSMLGYGDNLDFVDLLRLYIALHGDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLR 370
Cdd:cd06106  241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 371 KTDPRYTAQREFA--LEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRT 448
Cdd:cd06106  321 KPDPRFTALMEFAqtRPELENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                        410       420
                 ....*....|....*....|....*...
gi 429242423 449 LGVASQLIWDRALGLPIERPKSFSTEAL 476
Cdd:cd06106  401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
52-483 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 591.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGK 131
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 132 QPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERG-MNK 210
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 211 HDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFAnnEEFVELMRLYLTIHADHEGGNVS 290
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQIPSDPELDYGANFAHMIGQP--KPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLS-EETIKSYLWKLLNSGRVVPGYGHAVL 369
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLGGEEPtKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 370 RKTDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTL 449
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 429242423 450 GVASQLIWDRALGLPIERPKSFSTEALKKMVETK 483
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
52-473 1.31e-170

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 487.99  E-value: 1.31e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  52 LKDRLAELIPEKQAEIKKFRAehGQDVIGEVTINqmyGGARGVRSLIWEGSVLDPNEGI-RFRGYTIPECQKLLPSspng 130
Cdd:PLN02456  34 YESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF---- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 131 kqplpESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNK 210
Cdd:PLN02456 105 -----EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLRGQHK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 211 HDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQmDKDHSYNFANVLGF------ANNEEFVELMRLYLTIHADH 284
Cdd:PLN02456 180 YKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDN-SLDYAENFLYMLGSlgdrsyKPDPRLARLLDLYFIIHADH 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 285 EGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNflitMKKEIGddlSEETIKSYLWKLLNSGRVVPGY 364
Cdd:PLN02456 259 EGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLK----MLKEIG---TVENIPEYVEGVKNSKKVLPGF 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 365 GHAVLRKTDPRYTAQREFALE---HLPKDPMFQLVSRLYEIVpgVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQsFYTV 441
Cdd:PLN02456 332 GHRVYKNYDPRAKCIREFALEvfkHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPEE-FFTV 408
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 429242423 442 LFGVSRTLGVASQliWDRALGLPIER---PKSFST 473
Cdd:PLN02456 409 LFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYT 441
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
90-469 3.84e-127

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: 373.76  E-value: 3.84e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423   90 GARGVRSLIWEGSVLDPNEG-IRFRGYTIPEcqkLLPSSPngkqplPESLFWLLVTGEIPTLSQVQALSADWAARSQLPK 168
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEE---LAERSS------FEEVAYLLLTGELPTKEELEEFSAELAAHRELPE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  169 FVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAkayerGMNKHDYWKYEYEDcmDLIAKTVPIAGRIYRNLYRDGVVAPi 248
Cdd:pfam00285  72 DVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLPPIYP- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  249 QMDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEV 327
Cdd:pfam00285 144 DPDLSYAENFLYMLfGYEPDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  328 LNFLitmkKEIGddlSEETIKSYLWKLLNSG-RVVPGYGHAVLRKTDPRYTAQREFALEHLPK---DPMFQLVSRLYEIV 403
Cdd:pfam00285 223 LEML----EEIG---SPDEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEEVA 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429242423  404 PGVLTEHGktKNPYPNVDSHSGVLLQYYGLKEQsFYTVLFGVSRTLGVASQLIWDRALGlPIERPK 469
Cdd:pfam00285 296 PEDLYFVE--KNLYPNVDFYSGVLYHALGIPTD-MFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
89-470 6.99e-119

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: 352.67  E-value: 6.99e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  89 GGARGVRSLIWEGSVLDPNEGI-RFRGYTIPECQKllpsspngkQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLP 167
Cdd:cd06118    1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAE---------KSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 168 KFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYergmnkhdYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAP 247
Cdd:cd06118   72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFARDK--------SPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 248 IQmDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQE 326
Cdd:cd06118  144 DP-DLSYAENFLYMLfGEEPDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 327 VLNFLitmkKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPK---DPMFQLVSRLYEIV 403
Cdd:cd06118  222 VLKML----LEIG---TPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEIA 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429242423 404 PGVLTEhgktKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRTLGVASQLIWDRALGLPIERPKS 470
Cdd:cd06118  295 LEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRA 356
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
102-470 1.03e-93

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: 289.30  E-value: 1.03e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 102 SVLDPNEGI-RFRGYTIPECQKllpsspngkQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPT 180
Cdd:COG0372   28 SYIDGEKGIlRYRGYPIEDLAE---------KSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGFPRD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 181 LHPMAQFSLAVTALehdSAFakaYERGMNkHDYwKYEYEDCMDLIAKTVPIAGRIYRnlYRDG--VVAPiqmDKDHSY-- 256
Cdd:COG0372   99 AHPMDVLRTAVSAL---GAF---DPDADD-IDP-EARLEKAIRLIAKLPTIAAYAYR--YRRGlpPVYP---DPDLSYae 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 257 NFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLitmk 335
Cdd:COG0372  166 NFLYMLfGEEPDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEML---- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 336 KEIGDdlsEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHLPKDPMFQLVSRLYEIVPGvlTEHGK 412
Cdd:COG0372  241 EEIGS---PDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEVALE--DEYFI 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 429242423 413 TKNPYPNVDSHSGVLLQYYGLKEqSFYTVLFGVSRTLGVASQLIWDRAlGLPIERPKS 470
Cdd:COG0372  316 EKKLYPNVDFYSGIVYHALGIPT-DMFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
89-470 1.90e-82

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: 256.09  E-value: 1.90e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  89 GGARGVRSLIWEGSVLDPNEGI-RFRGYTIPECQKllpsspngkQPLPESLFWLLVTGEIPtlsqvqalsadwaarsqlp 167
Cdd:cd06101    1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAE---------NSSFEEVAYLLLTGELP------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 168 kfveelidrcpptlhpmaqfslavtalehdsafakayergmnkhdywkyeyedcmdliaktvpiagriyrnlyrdgvvap 247
Cdd:cd06101      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 248 iqmdkDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQE 326
Cdd:cd06101   53 -----SYAENFLYMLgGEEPDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEA 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 327 VLNFLITMKKEIGDDLseetiKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPK---DPMFQLVSRLYEIV 403
Cdd:cd06101  127 VLKMLEEIGTPKNEPA-----EAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKIA 201
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429242423 404 PGVLTEhgktKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRTLGVASQLIWDRALGLPIERPKS 470
Cdd:cd06101  202 PEVLYE----KKLYPNVDFYSGVLYKAMGF-PTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRA 263
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
253-470 3.25e-77

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: 240.70  E-value: 3.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 253 DHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFL 331
Cdd:cd06099    1 SYAENFLYMLgGEEPDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 332 ITMKKEIGDDLseetiKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPK---DPMFQLVSRLYEIVPGVLT 408
Cdd:cd06099   80 EEIGTPKNEPA-----EAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429242423 409 EhgktKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRTLGVASQLIWDRALGLPIERPKS 470
Cdd:cd06099  155 E----KKLYPNVDFYSGVLYKAMGF-PTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRS 211
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
88-473 2.44e-40

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: 149.12  E-value: 2.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423  88 YGGARGVRSLIwegSVLDPNEGI-RFRGYTIPEcqkLLPSSPNgkqplpESLFWLLVTGEIPTLSQVQALSADWAARSQL 166
Cdd:cd06107    9 YLNTAVCESSI---TYIDGDKGIlLYRGYPIEQ---LAESSTY------EEVAYLLLWGELPTQEQYDEFQRRLSEHMMV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 167 PKFVEELIDRCPPTLHPMAQFSLAVTALehdSAFAKAYERGMNKHDYWKY-EYED--CMDLIAKTVPIAGRIYRnlYRDG 243
Cdd:cd06107   77 PESVHRLIQTFPRDAHPMGILCAGLSAL---SAFYPEAIPAHTGDLYQNNpEVRDkqIIRTLAKMPTIAAAAYC--HRIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 244 VvAPIQMDKDHSY--NFANVLGFANNEEF------VELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGL 315
Cdd:cd06107  152 R-PFVYPRANLSYieNFLYMMGYVDQEPYepnprlARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAAL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 316 AGPLHGLANQEVLNflitMKKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHLPKDPM 392
Cdd:cd06107  230 YGPLHGGANEAALK----MLREIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 393 FQLVSRLYEIvpGVLTEHGKTKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRTLGVASQliWDRALGLP---IERPK 469
Cdd:cd06107  303 LKVAMELERI--ALEDEYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPlqrIWRPR 377

                 ....
gi 429242423 470 SFST 473
Cdd:cd06107  378 QVYT 381
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
136-456 5.47e-38

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: 142.03  E-value: 5.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNkhdywk 215
Cdd:cd06110   40 EEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPMDVLRTAVSALALYDPEADDMSREAN------ 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 216 yeYEDCMDLIAKTVPIAGRIYRnlYRDG--VVAPiQMDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVSAH 292
Cdd:cd06110  114 --LRKAIRLIAKMPTIVAAFHR--IRNGlePVAP-DPDLSHAANFLYMLtGEKPSEEAARAFDVALILHADHEL-NASTF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 293 TGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVlnflITMKKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKT 372
Cdd:cd06110  188 AARVVASTLSDMYSAVTAAIGALKGPLHGGANERV----MKMLLEIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTG 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 373 DPRYTAQREFALEhLPKD----PMFQLVSRLYEIVpgvltehGKTKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRT 448
Cdd:cd06110  261 DPRAKHLREMSRR-LGKEtgepKWYEMSEAIEQAM-------RDEKGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRV 331

                 ....*...
gi 429242423 449 LGVASQLI 456
Cdd:cd06110  332 SGWCAHIL 339
gltA PRK05614
citrate synthase;
104-469 3.25e-34

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 133.08  E-value: 3.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 104 LDPNEGI-RFRGYTIpecqkllpsspngKQPLPESLF----WLLVTGEIPTLSQvqalSADWAARSQLPKFVEELIDRC- 177
Cdd:PRK05614  62 IDGDKGIlLYRGYPI-------------EQLAEKSDFlevcYLLLYGELPTAEQ----KAEFDTTVTRHTMVHEQLKRFf 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 178 ---PPTLHPMAQFSLAVTALehdSAFakaYERGMNKHDYWKYEYEdCMDLIAKTVPIAGRIYRnlYRDGvvAP-IQMDKD 253
Cdd:PRK05614 125 rgfRRDAHPMAVLCGVVGAL---SAF---YHDSLDINDPEHREIA-AIRLIAKMPTLAAMAYK--YSIG--QPfVYPRND 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 254 HSY--NFANVLgFAN-------NEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLAN 324
Cdd:PRK05614 194 LSYaeNFLRMM-FATpceeyevNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGAN 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 325 QEVLNflitMKKEIGDDlseETIKSYLWKLL--NSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHL-PKDPMFQLVSR 398
Cdd:PRK05614 272 EAVLK----MLEEIGSV---DNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDPLLEVAME 344
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429242423 399 LYEIvpgVLT-EHGKTKNPYPNVDSHSGVLLQYYGLKeQSFYTVLFGVSRTLGVASQliWDRALGLP---IERPK 469
Cdd:PRK05614 345 LEEI---ALNdEYFIERKLYPNVDFYSGIILKALGIP-TSMFTVIFALARTVGWIAH--WNEMHSDPeqkIGRPR 413
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
136-450 7.66e-30

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: 120.45  E-value: 7.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLP-KFVEELIDRCPpTLHPMAQFSLAVTALEH--DSAFAKAYERGMNKhd 212
Cdd:cd06113   61 EETAYLLLFGYLPNKEELEEFCEILSSYRTLPdNFVEDVILKAP-SKDIMNKLQRSVLALYSydDKPDDISLENVLRQ-- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 213 ywkyeyedCMDLIAKTVPIAGRIYR--NLYRDG---VVAPIQMDKDHSYNFANVL--GFANNEEFVELMRLYLTIHADHE 285
Cdd:cd06113  138 --------SIQLIARLPTIAVYAYQakRHYYDGeslYIHHPQPELSTAENILSMLrpDKKYTELEAKLLDLCLVLHAEHG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 286 GGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLN------SGr 359
Cdd:cd06113  210 GGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENVKDWTDEDEVRAYLRKILNkeafdkSG- 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 360 VVPGYGHAVLRKTDPRYTAQREFAlEHLPK----DPMFQLVSRLYEIVPGVLTEH-GKTKNPYPNVDSHSGVLLQYYGLK 434
Cdd:cd06113  289 LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERIERLAPEVIAEErGIGKTVCANVDFYSGFVYKMLGIP 367
                        330
                 ....*....|....*.
gi 429242423 435 eQSFYTVLFGVSRTLG 450
Cdd:cd06113  368 -QELYTPLFAVARIVG 382
PRK14036 PRK14036
citrate synthase; Provisional
102-450 3.25e-28

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 115.44  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 102 SVLDPNEGI-RFRGYTIPECQKllpsspngkqplpESLF----WLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDR 176
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEELAE-------------KSSFletaYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 177 CPPTLHPMAQFSLAVTALehdsafAKAYERgmNKHDYWKYEYEDCMDLIAK--TVPIAGRIYRNLYRdgvvaPIQMDKDH 254
Cdd:PRK14036  86 FPETGHPMDALQASAAAL------GLFYSR--RALDDPEYIRDAVVRLIAKipTMVAAFQLIRKGND-----PIQPRDDL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 255 SYNfANVLGFANNEE----FVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNf 330
Cdd:PRK14036 153 DYA-ANFLYMLTEREpdplAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLA- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 331 litMKKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHLPKDPMFQLVSRLYEIVpgvl 407
Cdd:PRK14036 230 ---MLEEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVA---- 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 429242423 408 TEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFyTVLFGVSRTLG 450
Cdd:PRK14036 300 EERLGPKGIYPNVDFYSGLVYRKLGIPRDLF-TPIFAIARVAG 341
PRK14032 PRK14032
citrate synthase; Provisional
106-450 1.87e-27

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 114.23  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 106 PNEG-IRFRGYTIpecQKLLPSSPNGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLP-KFVEELIDRCPPTlHP 183
Cdd:PRK14032  63 PDEGkLYYRGYDI---KDLVNGFLKEKRFGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPdGFTRDMILKAPSK-DI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 184 MAQFSLAVTAL-EHDSafaKAYERGMNKhdywkyEYEDCMDLIAKTVPIAGRIYR--NLYRDGVVAPIQMDKDHSYNFAN 260
Cdd:PRK14032 139 MNSLARSVLALySYDD---NPDDTSIDN------VLRQSISLIARFPTLAVYAYQayRHYHDGKSLYIHPPKPELSTAEN 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 261 VLG-FANNEEFVEL----MRLYLTIHADHEGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMK 335
Cdd:PRK14032 210 ILYmLRPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIK 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 336 KEIGDDLSEETIKSYLWKLLN------SGRVVpGYGHAVLRKTDPRYTAQREFAlEHLPKDP----MFQLVSRLYEIVPG 405
Cdd:PRK14032 290 ENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFA-EKLAKEKgreeEFNLYEKIEKLAPE 367
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 429242423 406 VLTEH-GKTKNPYPNVDSHSGVLLQYYGLKEQsFYTVLFGVSRTLG 450
Cdd:PRK14032 368 LIAEErGIYKGVSANVDFYSGFVYDMLGIPEE-LYTPLFAIARIVG 412
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
104-473 4.43e-25

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: 106.45  E-value: 4.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 104 LDPNEGI-RFRGYTIPECqkllpsspnGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLH 182
Cdd:cd06116   22 IDGEKGIlRYRGYPIEQL---------AEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 183 PMAQFSLAVTALehdSAFakaYERGMNKHDYwKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPiqmDKDHSY--NFAN 260
Cdd:cd06116   93 PMGILISSVAAL---STF---YPEAKNIGDE-EQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLP---DNDLSYtgNFLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 261 VL------GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNflitM 334
Cdd:cd06116  163 MLfkmtepKYEPNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLR----M 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 335 KKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFA---LEHLPKDPMFQLVSRLYEIvpGVLTEHG 411
Cdd:cd06116  238 LQQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKI--ALEDEYF 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429242423 412 KTKNPYPNVDSHSGVLLQYYGLKEQSFyTVLFGVSRTLGVASQliWDRALGLP---IERPKSFST 473
Cdd:cd06116  313 ISRKLYPNVDFYSGLIYQALGFPTEAF-TVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
PRK14035 PRK14035
citrate synthase; Provisional
136-450 2.92e-23

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 100.99  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELI-DRCPPTLHPMAQFSLAVTALEHDSAfaKAYERGMNKHdyw 214
Cdd:PRK14035  42 EEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFeEYSTDHVHPMTALRTSVSYLAHFDP--DAEEESDEAR--- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 215 kyeYEDCMDLIAKTVPIAGRIYRnlYRDGVVaPIQMDKDHSYNfANVLGFANNEE----FVELMRLYLTIHADHEGgNVS 290
Cdd:PRK14035 117 ---YERAIRIQAKVASLVTAFAR--VRQGKE-PLKPRPDLSYA-ANFLYMLRGELptdiEVEAFNKALVLHADHEL-NAS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNflitMKKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLR 370
Cdd:PRK14035 189 TFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMD----MLSEIR---SIGDVDAYLDEKFANKEKIMGFGHRVYK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 371 KTDPRYTAQREFALEhLPKDPMfqlVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLkEQSFYTVLFGVSRTLG 450
Cdd:PRK14035 262 DGDPRAKYLREMSRK-ITKGTG---REELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGI-PHDLFTPIFAVSRVAG 336
PRK14037 PRK14037
citrate synthase; Provisional
104-461 7.57e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 99.82  E-value: 7.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 104 LDPNEGI-RFRGYTIPECQKllpsspNGKQplpESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLH 182
Cdd:PRK14037  21 IDGEKGIlRYRGYNIEDLVN------YGSY---EETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 183 PMAQFSLAVTALEhdSAFAKAYERGMNKhdywkyeyEDCMDLIAKTVPIAGRIYRnlYRDGVVAPI-QMDKDHSYNFANV 261
Cdd:PRK14037  92 AIGLMEAAFAALA--SIDKNFKWKENDK--------EKAISIIAKMATIVANVYR--RKEGNKPRIpEPSDSFAESFLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 262 -LGFANNEEFVELMRLYLTIHADHEggnVSAHT--GHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLItmkkEI 338
Cdd:PRK14037 160 sFAREPTAEEIKAMDAALILYTDHE---VPASTtaALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFV----EI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 339 GDdlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPKDP----MFQLVSRLYEIvpGVltEHGKTK 414
Cdd:PRK14037 233 GD--PNNVEMWFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSeakkYFEIAQKLEEL--GI--KQFGSK 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 429242423 415 NPYPNVDSHSGVLlqYYGLK-EQSFYTVLFGVSRTLG--------VASQ--LIWDRAL 461
Cdd:PRK14037 307 GIYPNTDFYSGIV--FYALGfPVYMFTALFALSRTLGwlahiieyVEEQhrLIRPRAL 362
PRK14034 PRK14034
citrate synthase; Provisional
136-450 5.49e-22

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 97.14  E-value: 5.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCP-PTLHPMAQFSLAVTALEHDSAFAKAYERGMNKHDYW 214
Cdd:PRK14034  42 EEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDlKKVHPMSVLRTAISMLGLYDEEAEIMDEEANYRKAV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 215 KYEYEdcmdlIAKTVPIAGRIYRNLyrdgvvAPIQMDKDHSYNfANVLGFANNEE----FVELMRLYLTIHADHEGgNVS 290
Cdd:PRK14034 122 RLQAK-----VPTIVAAFSRIRKGL------DPVEPRKDLSLA-ANFLYMLNGEEpdevEVEAFNKALVLHADHEL-NAS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNflitMKKEIGDdlsEETIKSYLWKLLNSGRVVPGYGHAVLR 370
Cdd:PRK14034 189 TFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMK----MLTEIGE---EENVESYIHNKLQNKEKIMGFGHRVYR 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 371 KTDPRYTAQREFA--LEHLPKDPM-FQLVSRLYEIVPgvltehgKTKNPYPNVDSHSGVLLQYYGLKEQSFyTVLFGVSR 447
Cdd:PRK14034 262 QGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIVT-------KEKGLPPNVDFYSASVYHCLGIDHDLF-TPIFAISR 333

                 ...
gi 429242423 448 TLG 450
Cdd:PRK14034 334 MSG 336
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
136-450 2.29e-20

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 92.71  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTAL--EHDSAFAKAYERGMNKhdy 213
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLgaEDPEADDSSPEANLAK--- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 214 wkyeyedCMDLIAKTVPIAGRIYRNlyRDG--VVAPiQMDKDHSYNFAN-VLGFANNEEFVELMRLYLTIHADHeGGNVS 290
Cdd:PRK14033 127 -------ALRLFAVLPTIVAADQRR--RRGldPIAP-RSDLGYAENFLHmCFGEVPEPEVVRAFEVSLILYAEH-SFNAS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNflitMKKEIGDdlsEETIKSYLWKLLNSGRVVPGYGHAVLR 370
Cdd:PRK14033 196 TFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMH----TMLEIGD---PARAAEWLRDALARKEKVMGFGHRVYK 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 371 KTDPRYTAQREfALEHLPKDPMFQLVSRLYEIVPGVLTEhgkTKNPYPNVDSHSGVLlqYYGLK-EQSFYTVLFGVSRTL 449
Cdd:PRK14033 269 HGDSRVPTMKA-ALRRVAAVRDGQRWLDIYEALEKAMAE---ATGIKPNLDFPAGPA--YYLMGfDIDFFTPIFVMSRIT 342

                 .
gi 429242423 450 G 450
Cdd:PRK14033 343 G 343
PRK12349 PRK12349
citrate synthase;
141-456 6.43e-19

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 88.24  E-value: 6.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 141 LLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALehdSAFAKAYE---RGMNKhdywkye 217
Cdd:PRK12349  51 LLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKALPKETHPMDGLRTGVSAL---AGYDNDIEdrsLEVNK------- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 218 yEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQmDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGGNvSAHTGHL 296
Cdd:PRK12349 121 -SRAYKLLSKVPNIVANSYHILNNEEPIEPLK-ELSYSANFLYMLtGKKPTELEEKIFDRSLVLYSEHEMPN-STFTARV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 297 VGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGddlSEETIKSylwKLLNSGRVVpGYGHAV-LRKTDPR 375
Cdd:PRK12349 198 IASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEK---FEELLQK---KLYNKEKIM-GFGHRVyMKKMDPR 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 376 YTAQREfALEHL-PKDPMFqlvsRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLlqYYGLK-EQSFYTVLFGVSRTLGVAS 453
Cdd:PRK12349 271 ALMMKE-ALKQLcDVKGDY----TLYEMCEAGEKIMEKEKGLYPNLDYYAAPV--YWMLGiPIQLYTPIFFSSRTVGLCA 343

                 ...
gi 429242423 454 QLI 456
Cdd:PRK12349 344 HVI 346
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
141-470 8.05e-18

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


Pssm-ID: 99862 [Multi-domain]  Cd Length: 349  Bit Score: 84.66  E-value: 8.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 141 LLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPtLHPMAQFSLAVTALEHDSAFAKAyergmnkhdywkyeyed 220
Cdd:cd06109   45 LLWNGFFPDLPELEEFRAALAAARALPDVVAALLPALAG-LDPMDALRALLALLPDSPDLATA----------------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 221 cMDLIAKTVPIAGRIYRNLYRDGVVAPiQMDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHeGGNVSAHTGHLVGS 299
Cdd:cd06109  107 -LRLLAAAPVITAALLRLSRGKQPIAP-DPSLSHAADYLRMLtGEPPSEAHVRALDAYLVTVADH-GMNASTFTARVIAS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 300 ALSSPFLSMAASLNGLAGPLHGLANQEVLNflitMKKEIGddlSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQ 379
Cdd:cd06109  184 TEADLTSAVLGAIGALKGPLHGGAPGPVLD----MLDAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVL 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 380 REfALEHLPKDPMFQLVSRLYE-IVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFyTVLFGVSRTLGVASQLIWD 458
Cdd:cd06109  257 KA-AAERLGAPDERLEFAEAVEqAALALLREYKPGRPLETNVEFYTALLLEALGLPREAF-TPTFAAGRTAGWTAHVLEQ 334
                        330
                 ....*....|..
gi 429242423 459 RALGLPIeRPKS 470
Cdd:cd06109  335 ARTGRLI-RPQS 345
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
136-468 1.92e-16

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: 80.66  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALehdsafakayerGM---NKHD 212
Cdd:cd06117   40 EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVL------------GCvlpEKED 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 213 YWKYEYEDCMD-LIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVL-GFANNEEFVELMRLYLTIHADHEGgNVS 290
Cdd:cd06117  108 HPVSGARDIADrLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLhGEKPSESWEKAMHISLILYAEHEF-NAS 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 291 AHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQevLNFLITMKKEIGDDlSEETIKsylwKLLNSGRVVPGYGHAVLR 370
Cdd:cd06117  187 TFTARVIAGTGSDMYSAITGAIGALRGPKHGGANE--VAFEIQQRYESADE-AEADIR----RRVENKEVVIGFGHPVYT 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 371 KTDPRYTAQREFAlEHLPKDPMFQlvsRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFyTVLFGVSRTLG 450
Cdd:cd06117  260 IADPRNQVIKEVA-KQLSKEGGDM---KMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTAMF-TPLFVIARTTG 334
                        330
                 ....*....|....*...
gi 429242423 451 VASQLIWDRALGlPIERP 468
Cdd:cd06117  335 WSAHIIEQRQDG-KIIRP 351
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
109-460 4.22e-16

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: 79.66  E-value: 4.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 109 GIRFRGYTIPECqkllpsspnGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFS 188
Cdd:cd06108   22 GLTYRGYDIEDL---------AENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 189 LAVTAL---EHDSAFAKAYERGMNkhdywkyeyedcmdLIAKTVPIAGRIYRnlYRDGVVAPIQMDKDHSY--NFANVL- 262
Cdd:cd06108   93 TGCSMLgclEPENEFSQQYEIAIR--------------LLAIFPSILLYWYH--YSHSGKRIETETDEDSIagHFLHLLh 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 263 GFANNEEFVELMRLYLTIHADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKkeigddl 342
Cdd:cd06108  157 GKKPGELEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK------- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 343 SEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFAL---EHLPKDPMFQLVSRLYEIVPgvltehgKTKNPYPN 419
Cdd:cd06108  229 SPEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKklsEEGGDPLLYQISERIEEVMW-------EEKKLFPN 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 429242423 420 VDSHSGVLLQYYGLKEQSFyTVLFGVSRTLGVASQLIWDRA 460
Cdd:cd06108  302 LDFYSASAYHFCGIPTELF-TPIFVMSRVTGWAAHIMEQRA 341
PRK12351 PRK12351
methylcitrate synthase; Provisional
136-468 1.75e-13

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 71.88  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 136 ESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTAL------EHDSAFAKAYergmn 209
Cdd:PRK12351  49 EEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR----- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 210 khdywkyeyedcmDLIAKTVPIAGRIYRNLYR---DGVVAPIQMDKD----HsynFANVL-GFANNEEFVELMRLYLTIH 281
Cdd:PRK12351 124 -------------DIADRLLASLGSILLYWYHyshNGRRIEVETDDDsiggH---FLHLLhGKKPSESWVKAMHTSLILY 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 282 ADHEGgNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANqEVlNFLITMKKEIGDDlSEETIKsylwKLLNSGRVV 361
Cdd:PRK12351 188 AEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EV-AFEIQQRYDTPDE-AEADIR----RRVENKEVV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 362 PGYGHAVLRKTDPRYTAQREFAlEHLPKDpmfQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFyTV 441
Cdd:PRK12351 260 IGFGHPVYTISDPRNKVIKEVA-KKLSKE---AGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTAMF-TP 334
                        330       340
                 ....*....|....*....|....*..
gi 429242423 442 LFGVSRTLGVASQLIWDRALGlPIERP 468
Cdd:PRK12351 335 LFVISRTTGWAAHVIEQRQDN-KIIRP 360
PRK12350 PRK12350
citrate synthase 2; Provisional
277-470 3.59e-11

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 64.60  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 277 YLTIHADHeGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLnfliTMKKEIGddlSEETIKSYLWKLLN 356
Cdd:PRK12350 161 YWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVL----PMLDAVE---RTGDARGWVKGALD 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 357 SGRVVPGYGHAVLRKTDPRYTAQREfALEHLPKdPMFQLVSRLYEIVPGVLTEHgKTKNPY-PNVDSHSGVLLQYYGLKE 435
Cdd:PRK12350 233 RGERLMGFGHRVYRAEDPRARVLRA-TAKRLGA-PRYEVAEAVEQAALAELRER-RPDRPLeTNVEFWAAVLLDFAGVPA 309
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 429242423 436 QSFyTVLFGVSRTLGVASQLIWDRALGLPIeRPKS 470
Cdd:PRK12350 310 HMF-TAMFTCGRTAGWSAHILEQKRTGRLV-RPSA 342
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
282-467 3.18e-03

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: 39.09  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 282 ADHEGGNVSAHTGHLVGSALSSPFLS-MAASLNGlAGPLHGLAnqevLNFLITMKKEI--GDDLSEETIKSYLWKLLNSG 358
Cdd:cd06100   42 ADHGPATPSAHAARLTASAGPEDLQSaVAAGLLG-IGDRFGGA----GEGAARLFKEAvdSGDALDAAAAEFVAEYRAAK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242423 359 RVVPGYGHAVLRKTDPRYTAQREFALEHLPKDPMFqlvsRLYEIVPGVLTEhgKTKNPYP-NVDSHSGVLLQYYGLKEQS 437
Cdd:cd06100  117 KRIPGFGHPVHKNPDPRVPRLLELARELGPAGPHL----DYALAVEKALTA--AKGKPLPlNVDGAIAAILLDLGFPPGA 190
                        170       180       190
                 ....*....|....*....|....*....|
gi 429242423 438 FYTvLFGVSRTLGVASQLIWDRALGLPIER 467
Cdd:cd06100  191 LRG-LFVLGRSPGLIAHALEEKRLGQPLYR 219
 
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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