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Conserved domains on  [gi|508704881|gb|EOX96777|]
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Citrate synthase family protein [Theobroma cacao]

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 ...
40-466 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: 858.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKS 199
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 200 KYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNVSAH 279
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 280 TGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVLRKT 359
Cdd:cd06105  241 TTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 360 DPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSIGIC 439
Cdd:cd06105  321 DPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVL 400
                        410       420
                 ....*....|....*....|....*..
gi 508704881 440 SQLIWDRALGLPLERPKSVTMEWLENY 466
Cdd:cd06105  401 SQLIWDRALGLPLERPKSVSTDGLEKL 427
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
40-466 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: 858.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKS 199
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 200 KYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNVSAH 279
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 280 TGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVLRKT 359
Cdd:cd06105  241 TTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 360 DPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSIGIC 439
Cdd:cd06105  321 DPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVL 400
                        410       420
                 ....*....|....*....|....*..
gi 508704881 440 SQLIWDRALGLPLERPKSVTMEWLENY 466
Cdd:cd06105  401 SQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
37-463 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: 794.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   37 DLDLHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAK 116
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  117 PDGEPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGI 196
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  197 PKSKYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNV 276
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  277 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVL 356
Cdd:TIGR01793 241 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  357 RKTDPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSI 436
Cdd:TIGR01793 321 RKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRAL 400
                         410       420
                  ....*....|....*....|....*..
gi 508704881  437 GICSQLIWDRALGLPLERPKSVTMEWL 463
Cdd:TIGR01793 401 GILSQLIWDRALGLPLERPKSVSTEWL 427
PLN02456 PLN02456
citrate synthase
7-470 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 634.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   7 VAALSRLRSRVSQQSSLSNSVRWLQTQSSSDLDLHSQLKELVPEQQERLKKLKAehGKVQLGNITVDmvlGGMRGMTGLL 86
Cdd:PLN02456   1 AAAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  87 WETSLLDPDEGI-RFRGLSIPECQKLLPAakpdgeplpEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDAL 165
Cdd:PLN02456  76 SEISLIDGDEGIlRFRGYPIEELAEKSPF---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDAL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 166 PVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKSKYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAmDDSLDYGGN 245
Cdd:PLN02456 147 PHDAHPMTQLVSGVMALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP-DNSLDYAEN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 246 FSHMLGF-------KSPQMQELMRLYVTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 318
Cdd:PLN02456 226 FLYMLGSlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 319 KSVvdecGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFAL---KHLPDDPLFQLVSKLYEVVppILT 395
Cdd:PLN02456 306 KEI----G---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLD 376
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508704881 396 ELGKVKNPWPNVDAHSGVLLNYFGLTEaRYYTVLFGVSRSIGICSQliWDRALGLPLER---PKSV-TMEWLENYCKKR 470
Cdd:PLN02456 377 EYFKVRKLYPNVDFYSGVLLRALGFPE-EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVyTGEWLRHYCPKA 452
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
78-456 1.27e-126

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: 371.84  E-value: 1.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   78 GMRGMTGLLWETSLLDPDEG-IRFRGLSIPE-CQK--------LLpaakpdgeplpegllwllLTGKVPSKAQVDALSQE 147
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERssfeevayLL------------------LTGELPTKEELEEFSAE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  148 LRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEfqkayEKGIPKSKYWEPTYEDalSLIARVPLVASYVYRRI 227
Cdd:pfam00285  63 LAAHRELPEDVLELLRALPRDAHPMAVLRAAVSALAAFDP-----EAISDKADYWENALRD--DLIAKLPTIAAYIYRHR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  228 YKDGnFIAMDDSLDYGGNFSHML-GFK-SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGP 305
Cdd:pfam00285 136 RGLP-PIYPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  306 LHGLANQEVLLWIKSVvdecgenITKEQLKDYVWKTLNSGK-VVPGFGHGVLRKTDPRYTCQREFALKHLP---DDPLFQ 381
Cdd:pfam00285 214 LHGGANEAVLEMLEEI-------GSPDEVEEYIRKVLNKGKeRIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLE 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508704881  382 LVSKLYEVVPPILTELGkvKNPWPNVDAHSGVLLNYFGLTEaRYYTVLFGVSRSIGICSQLIWDRALGlPLERPK 456
Cdd:pfam00285 287 LAEELEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
78-458 1.61e-99

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: 303.56  E-value: 1.61e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  78 GMRGMTGLLWETSLLDPDEGI-RFRGLSIPECqkllpAAKPDgeplPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPD 156
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGIlRYRGYPIEDL-----AEKSS----FEEVAYLLLYGELPTKEELAEFKAELARHRELPE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 157 YVFKAIDALPVSAHPMTQFATGVMALQVqsefqkAYEKGIPKSKywEPTYEDALSLIARVPLVASYVYRriYKDGN-FIA 235
Cdd:COG0372   87 EVKEFLDGFPRDAHPMDVLRTAVSALGA------FDPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR--YRRGLpPVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 236 MDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 313
Cdd:COG0372  157 PDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 314 VLLWIksvvdecgENI-TKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFA---LKHLPDDPLFQLVSKLYEV 389
Cdd:COG0372  236 VLEML--------EEIgSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 390 VPPilTELGKVKNPWPNVDAHSGVLLNYFGL-TEarYYTVLFGVSRSIGICSQLIWDRAlGLPLERPKSV 458
Cdd:COG0372  308 ALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTD--MFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQI 372
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
40-466 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: 858.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:cd06105    1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKS 199
Cdd:cd06105   81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 200 KYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNVSAH 279
Cdd:cd06105  161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 280 TGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVLRKT 359
Cdd:cd06105  241 TTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRKT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 360 DPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSIGIC 439
Cdd:cd06105  321 DPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGVL 400
                        410       420
                 ....*....|....*....|....*..
gi 508704881 440 SQLIWDRALGLPLERPKSVTMEWLENY 466
Cdd:cd06105  401 SQLIWDRALGLPLERPKSVSTDGLEKL 427
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
37-463 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: 794.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   37 DLDLHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAK 116
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  117 PDGEPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGI 196
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  197 PKSKYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNV 276
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  277 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVL 356
Cdd:TIGR01793 241 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  357 RKTDPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSI 436
Cdd:TIGR01793 321 RKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRAL 400
                         410       420
                  ....*....|....*....|....*..
gi 508704881  437 GICSQLIWDRALGLPLERPKSVTMEWL 463
Cdd:TIGR01793 401 GILSQLIWDRALGLPLERPKSVSTEWL 427
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
40-463 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: 710.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:cd06103    1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKG-IPK 198
Cdd:cd06103   81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 199 SKYWEPTYEDALSLIARVPLVASYVYRRIY-KDGNFIAMDDSLDYGGNFSHMLGFKSPQMQELMRLYVTIHSDHEGGNVS 277
Cdd:cd06103  161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYrKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 278 AHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVLR 357
Cdd:cd06103  241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 358 KTDPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSIG 437
Cdd:cd06103  321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                        410       420
                 ....*....|....*....|....*.
gi 508704881 438 ICSQLIWDRALGLPLERPKSVTMEWL 463
Cdd:cd06103  401 VLAQLVWSRALGLPIERPKSMSTEGL 426
PLN02456 PLN02456
citrate synthase
7-470 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 634.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   7 VAALSRLRSRVSQQSSLSNSVRWLQTQSSSDLDLHSQLKELVPEQQERLKKLKAehGKVQLGNITVDmvlGGMRGMTGLL 86
Cdd:PLN02456   1 AAAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  87 WETSLLDPDEGI-RFRGLSIPECQKLLPAakpdgeplpEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDAL 165
Cdd:PLN02456  76 SEISLIDGDEGIlRFRGYPIEELAEKSPF---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDAL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 166 PVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKSKYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAmDDSLDYGGN 245
Cdd:PLN02456 147 PHDAHPMTQLVSGVMALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP-DNSLDYAEN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 246 FSHMLGF-------KSPQMQELMRLYVTIHSDHEGGNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 318
Cdd:PLN02456 226 FLYMLGSlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 319 KSVvdecGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFAL---KHLPDDPLFQLVSKLYEVVppILT 395
Cdd:PLN02456 306 KEI----G---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLD 376
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508704881 396 ELGKVKNPWPNVDAHSGVLLNYFGLTEaRYYTVLFGVSRSIGICSQliWDRALGLPLER---PKSV-TMEWLENYCKKR 470
Cdd:PLN02456 377 EYFKVRKLYPNVDFYSGVLLRALGFPE-EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVyTGEWLRHYCPKA 452
PRK09569 PRK09569
citrate (Si)-synthase;
40-466 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 614.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKG-IPK 198
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 199 SKYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHMLGfKSPQMQELMRLYVTIHSDHEGGNVSA 278
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQIPSDPELDYGANFAHMIG-QPKPYKDVARMYFILHSDHESGNVSA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 279 HTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDE-CGENITKEQLKDYVWKTLNSGKVVPGFGHGVLR 357
Cdd:PRK09569 242 HTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKlGGEEPTKEQVEQALWDTLNAGQVIPGYGHAVLR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 358 KTDPRYTCQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRSIG 437
Cdd:PRK09569 322 KTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRALG 401
                        410       420
                 ....*....|....*....|....*....
gi 508704881 438 ICSQLIWDRALGLPLERPKSVTMEWLENY 466
Cdd:PRK09569 402 VMANITWDRGLGYAIERPKSVTTEMLEKW 430
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
40-463 0e+00

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


Pssm-ID: 99859  Cd Length: 428  Bit Score: 598.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  40 LHSQLKELVPEQQERLKKLKAEHGKVQLGNITVDMVLGGMRGMTGLLWETSLLDPDEGIRFRGLSIPECQKLLPAAKPDG 119
Cdd:cd06106    1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 120 EPLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEFQKAYEKGIPKS 199
Cdd:cd06106   81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 200 KYWEPTYEDALSLIARVPLVASYVYRRIYKDGNFI-AMDDSLDYGGNFSHMLGFKSPQ-MQELMRLYVTIHSDHEGGNVS 277
Cdd:cd06106  161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLgKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 278 AHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLNSGKVVPGFGHGVLR 357
Cdd:cd06106  241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 358 KTDPRYTCQREFALKH--LPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEARYYTVLFGVSRS 435
Cdd:cd06106  321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                        410       420
                 ....*....|....*....|....*...
gi 508704881 436 IGICSQLIWDRALGLPLERPKSVTMEWL 463
Cdd:cd06106  401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
78-456 1.27e-126

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: 371.84  E-value: 1.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881   78 GMRGMTGLLWETSLLDPDEG-IRFRGLSIPE-CQK--------LLpaakpdgeplpegllwllLTGKVPSKAQVDALSQE 147
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERssfeevayLL------------------LTGELPTKEELEEFSAE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  148 LRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVQSEfqkayEKGIPKSKYWEPTYEDalSLIARVPLVASYVYRRI 227
Cdd:pfam00285  63 LAAHRELPEDVLELLRALPRDAHPMAVLRAAVSALAAFDP-----EAISDKADYWENALRD--DLIAKLPTIAAYIYRHR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  228 YKDGnFIAMDDSLDYGGNFSHML-GFK-SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGP 305
Cdd:pfam00285 136 RGLP-PIYPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  306 LHGLANQEVLLWIKSVvdecgenITKEQLKDYVWKTLNSGK-VVPGFGHGVLRKTDPRYTCQREFALKHLP---DDPLFQ 381
Cdd:pfam00285 214 LHGGANEAVLEMLEEI-------GSPDEVEEYIRKVLNKGKeRIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLE 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508704881  382 LVSKLYEVVPPILTELGkvKNPWPNVDAHSGVLLNYFGLTEaRYYTVLFGVSRSIGICSQLIWDRALGlPLERPK 456
Cdd:pfam00285 287 LAEELEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
77-458 2.22e-117

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: 348.44  E-value: 2.22e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  77 GGMRGMTGLLWETSLLDPDEGI-RFRGLSIPECQKLlpaakpdgePLPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVP 155
Cdd:cd06118    1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 156 DYVFKAIDALPVSAHPMTQFATGVMALqvqSEFQKAYEKgipksKYWEPTYEDALSLIARVPLVASYVYRriYKDGN-FI 234
Cdd:cd06118   72 EHVVEILDLLPKNAHPMDVLRTAVSAL---GSFDPFARD-----KSPEARYEKAIRLIAKLPTIAANIYR--NREGLeII 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 235 AMDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQ 312
Cdd:cd06118  142 APDPDLSYAENFLYMLFGEepDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 313 EVLLWIksvvDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFALKHLP---DDPLFQLVSKLYEV 389
Cdd:cd06118  221 AVLKML----LEIG---TPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEekgDDKLFEIAEELEEI 293
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508704881 390 VPPILTElgkvKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIGICSQLIWDRALGLPLERPKSV 458
Cdd:cd06118  294 ALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAE 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
78-458 1.61e-99

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: 303.56  E-value: 1.61e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  78 GMRGMTGLLWETSLLDPDEGI-RFRGLSIPECqkllpAAKPDgeplPEGLLWLLLTGKVPSKAQVDALSQELRSRAVVPD 156
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGIlRYRGYPIEDL-----AEKSS----FEEVAYLLLYGELPTKEELAEFKAELARHRELPE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 157 YVFKAIDALPVSAHPMTQFATGVMALQVqsefqkAYEKGIPKSKywEPTYEDALSLIARVPLVASYVYRriYKDGN-FIA 235
Cdd:COG0372   87 EVKEFLDGFPRDAHPMDVLRTAVSALGA------FDPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR--YRRGLpPVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 236 MDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 313
Cdd:COG0372  157 PDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 314 VLLWIksvvdecgENI-TKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFA---LKHLPDDPLFQLVSKLYEV 389
Cdd:COG0372  236 VLEML--------EEIgSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLEIAEELEEV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 390 VPPilTELGKVKNPWPNVDAHSGVLLNYFGL-TEarYYTVLFGVSRSIGICSQLIWDRAlGLPLERPKSV 458
Cdd:COG0372  308 ALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTD--MFTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQI 372
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
241-458 4.48e-79

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: 246.84  E-value: 4.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 241 DYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 318
Cdd:cd06101   53 SYAENFLYMLGGEepDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKML 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 319 ksvvDECGENItKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFALKHLP---DDPLFQLVSKLYEVVPPILT 395
Cdd:cd06101  132 ----EEIGTPK-NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKekgLDPMFELAAELEKIAPEVLY 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508704881 396 ElgkvKNPWPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIGICSQLIWDRALGLPLERPKSV 458
Cdd:cd06101  207 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAE 264
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
241-457 2.09e-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: 2.09e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 241 DYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 318
Cdd:cd06099    1 SYAENFLYMLGGEepDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 319 ksvvDECGENItKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFALKHLP---DDPLFQLVSKLYEVVPpilt 395
Cdd:cd06099   80 ----EEIGTPK-NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKedgDDPMFELAAELEKIAE---- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508704881 396 ELGKVKNPWPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIGICSQLIWDRALGLPLERPKS 457
Cdd:cd06099  151 EVLYEKKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRS 211
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
133-443 1.04e-45

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: 162.44  E-value: 1.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQV-QSEFQKAYEkgipkskywEPTYEDALS 211
Cdd:cd06110   49 GELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPMDVLRTAVSALALyDPEADDMSR---------EANLRKAIR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 LIARVP-LVASYvyRRIYKDGNFIAMDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSAL 288
Cdd:cd06110  120 LIAKMPtIVAAF--HRIRNGLEPVAPDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTL 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 289 SDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDEcgENITkeqlkDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQRE 368
Cdd:cd06110  197 SDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSV--DNVA-----AYVKDKLANKEKIMGFGHRVYKTGDPRAKHLRE 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 508704881 369 FA--LKHLPDDPlfqlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIGICSQLI 443
Cdd:cd06110  270 MSrrLGKETGEP------KWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
133-443 1.48e-43

2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.


Pssm-ID: 130859  Cd Length: 368  Bit Score: 157.14  E-value: 1.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALqvqSEFQKAYEKGIPkskywEPTYEDALSL 212
Cdd:TIGR01800  49 GKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHPMDVLRTAVSYL---GALDPEKFGHTP-----EEARDIAIRL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  213 IARVPLVASYVYRRIyKDGNFIAMDDSLDYGGNFSHML-GFKSPQMQE-LMRLYVTIHSDHEGgNVSAHTGHLVGSALSD 290
Cdd:TIGR01800 121 LAKLPTIVAYWYRIR-HGGEIIAPKDDDSIAGNFLYMLhGEEPTKEWEkAMDIALILYAEHEF-NASTFAARVIASTLSD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  291 PYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFA 370
Cdd:TIGR01800 199 MYSAITAAIGALKGPLHGGANEAVM----AMLDEIG---DPDKAEAWIRKALENKERIMGFGHRVYKTYDPRAKILKEYA 271
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508704881  371 lKHLPDDplfQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIGICSQLI 443
Cdd:TIGR01800 272 -KKLSAK---EGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGI-PTDLFTPIFAMSRVTGWTAHII 339
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
133-437 3.40e-42

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


Pssm-ID: 99865  Cd Length: 373  Bit Score: 153.73  E-value: 3.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVqseFQKAYEKGIPKSKYwepTYEDALSL 212
Cdd:cd06112   51 GDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPETGHPMDMLQATVAALGM---FYPKPEVLKPNPDY---IDAATVKL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVP-LVASYvyRRIYKDGNFIAMDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALS 289
Cdd:cd06112  125 IAKMPtLVAMW--ARIRNGDDPIEPRPDLDYAENFLYMLFGEepDPATAKILDACLILHAEHTM-NASTFSALVTGSTLA 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 290 DPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREF 369
Cdd:cd06112  202 DPYAVISSAIGTLSGPLHGGANEDVL----EMLEEIG---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKL 274
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508704881 370 ALKHLPDDPLFqlvSKLYEV---VPPILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIG 437
Cdd:cd06112  275 AEDLFAKMGEL---SKLYEIaleVERLCEELLGHKGVYPNVDFYSGIVYKELGI-PADLFTPIFAVARVAG 341
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
133-441 4.40e-41

Escherichia coli (Ec) citrate synthase (CS) GltA_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.


Pssm-ID: 99867  Cd Length: 400  Bit Score: 151.19  E-value: 4.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQvqSEFQKAYEKGIPkskywEPTYEDALSL 212
Cdd:cd06114   77 GELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALS--AFYPDSLDVNDP-----EQRELAAIRL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVPLVASYVYRriYKDGN-FIAMDDSLDYGGNFSHMLgF--------KSPQMQELMRLYVTIHSDHEGgNVSAHTGHL 283
Cdd:cd06114  150 IAKVPTIAAMAYR--YSIGQpFIYPDNDLSYVENFLHMM-FavpyepyeVDPVVVKALDTILILHADHEQ-NASTSTVRM 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 284 VGSALSDPYLSFAAALNGLAGPLHGLANQEVLLW---IKSVvdecgENITK--EQLKDYvwktlNSGKVVPGFGHGVLRK 358
Cdd:cd06114  226 VGSSGANLFASISAGIAALWGPLHGGANEAVLEMleeIGSV-----GNVDKyiAKAKDK-----NDPFRLMGFGHRVYKN 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 359 TDPRYTCQREFA---LKHLP-DDPLFQLVSKLYEVVppiLT-ELGKVKNPWPNVDAHSGVLLNYFGLTEaRYYTVLFGVS 433
Cdd:cd06114  296 YDPRAKILKKTCdevLAELGkDDPLLEIAMELEEIA---LKdDYFIERKLYPNVDFYSGIILRALGIPT-EMFTVLFALG 371

                 ....*...
gi 508704881 434 RSIGICSQ 441
Cdd:cd06114  372 RTPGWIAQ 379
gltA PRK05614
citrate synthase;
133-442 1.13e-36

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 139.63  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALqvqSEFqkayekgipkskyweptYEDALS- 211
Cdd:PRK05614  95 GELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGAL---SAF-----------------YHDSLDi 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 ------------LIARVPLVASYVYRriYKDGN-FIAMDDSLDYGGNFSHMLgFK--------SPQMQELMRLYVTIHSD 270
Cdd:PRK05614 155 ndpehreiaairLIAKMPTLAAMAYK--YSIGQpFVYPRNDLSYAENFLRMM-FAtpceeyevNPVLVRALDRIFILHAD 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 271 HEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDecGENITK--EQLKDyvwKtlNSGKVV 348
Cdd:PRK05614 232 HEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGS--VDNIPEfiARAKD---K--NDGFRL 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 349 PGFGHGVLRKTDPRYTCQREFA---LKHL-PDDPLFQLVSKLYEVVppiLT-ELGKVKNPWPNVDAHSGVLLNYFGLTeA 423
Cdd:PRK05614 304 MGFGHRVYKNYDPRAKIMRETChevLKELgLNDPLLEVAMELEEIA---LNdEYFIERKLYPNVDFYSGIILKALGIP-T 379
                        330
                 ....*....|....*....
gi 508704881 424 RYYTVLFGVSRSIGICSQL 442
Cdd:PRK05614 380 SMFTVIFALARTVGWIAHW 398
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
133-454 2.07e-35

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: 135.26  E-value: 2.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQV-QSEFQKAYEKGIPKSKywePTYED--A 209
Cdd:cd06107   55 GELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRDAHPMGILCAGLSALSAfYPEAIPAHTGDLYQNN---PEVRDkqI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 210 LSLIARVPLVASYVYRRiYKDGNFIAMDDSLDYGGNFSHMLGFK-------SPQMQELMRLYVTIHSDHEGgNVSAHTGH 282
Cdd:cd06107  132 IRTLAKMPTIAAAAYCH-RIGRPFVYPRANLSYIENFLYMMGYVdqepyepNPRLARALDRLWILHADHEM-NCSTSAAR 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 283 LVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVdecgeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPR 362
Cdd:cd06107  210 HTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREIG-------TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPR 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 363 YTCQREFA---LKHLPDDPLFQLVSKLYEVVppILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIGIC 439
Cdd:cd06107  283 AKVIREILhevLTEVEKDPLLKVAMELERIA--LEDEYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWM 359
                        330
                 ....*....|....*
gi 508704881 440 SQliWDRALGLPLER 454
Cdd:cd06107  360 AH--WREMMEDPLQR 372
PRK14036 PRK14036
citrate synthase; Provisional
133-437 2.40e-32

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 126.61  E-value: 2.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQVqseFqkaY-EKGIPKSKYwepTYEDALS 211
Cdd:PRK14036  54 GELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPETGHPMDALQASAAALGL---F---YsRRALDDPEY---IRDAVVR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 LIARVP-LVASYvyRRIYKDGNFIAMDDSLDYGGNFSHMLGFK--SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSAL 288
Cdd:PRK14036 125 LIAKIPtMVAAF--QLIRKGNDPIQPRDDLDYAANFLYMLTERepDPLAARIFDRCLILHAEHTI-NASTFSARVTASTL 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 289 SDPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQRE 368
Cdd:PRK14036 202 TDPYAVIASAVGTLAGPLHGGANEDVL----AMLEEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQK 274
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508704881 369 FA---LKHLPDDPLFQLVSKLYEVVPPILTElgkvKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIG 437
Cdd:PRK14036 275 LAeelFARFGHDEYYEIALELERVAEERLGP----KGIYPNVDFYSGLVYRKLGI-PRDLFTPIFAIARVAG 341
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
133-456 3.63e-31

citrate synthase I (hexameric type); This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes. [Energy metabolism, TCA cycle]


Pssm-ID: 273811  Cd Length: 412  Bit Score: 124.12  E-value: 3.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALqvqSEFqkaYEKG--IPKSKYWEPTyedAL 210
Cdd:TIGR01798  82 GELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGAL---SAF---YHDAldINDPRHREIS---AI 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  211 SLIARVPLVASYVYRriYKDGN-FIAMDDSLDYGGNFSHMLgFKSP--------QMQELMRLYVTIHSDHEGgNVSAHTG 281
Cdd:TIGR01798 153 RLIAKIPTLAAMSYK--YSIGQpFVYPRNNLSYAENFLHMM-FATPcedykvnpVLARAMDRIFILHADHEQ-NASTSTV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  282 HLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSV--VDECGENItkEQLKDYvwktlNSGKVVPGFGHGVLRKT 359
Cdd:TIGR01798 229 RLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIgsVKNIDEFI--KKVKDK-----NDPFRLMGFGHRVYKNY 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  360 DPRYTCQREF---ALKHL--PDDPLFQLVSKLYEVV--PPILTElgkvKNPWPNVDAHSGVLLNYFGLTeARYYTVLFGV 432
Cdd:TIGR01798 302 DPRAKVMRETcheVLKELglHDDPLFKLAMELEKIAlnDPYFIE----RKLYPNVDFYSGIILKAMGIP-TSMFTVIFAL 376
                         330       340
                  ....*....|....*....|....*..
gi 508704881  433 SRSIGICSQliWDRAL---GLPLERPK 456
Cdd:TIGR01798 377 ARTVGWISH--WSEMIsdpGQKIGRPR 401
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
90-466 3.08e-29

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


Pssm-ID: 99868  Cd Length: 410  Bit Score: 118.70  E-value: 3.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881  90 SLLDPDEGI-RFRGLSIPECqkllpAAKPDgepLPEgLLWLLLTGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVS 168
Cdd:cd06115   40 SYIDGDKGIlRYRGYPIEEL-----AEKST---FLE-VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 169 AHPMTQFATGVMALQV-QSEFQKAYE-KGIPKSKywEPTYEDALSLIARVPLVASYVYRRiyKDG-NFIAMDDSLDYGGN 245
Cdd:cd06115  111 AHPMGMLVSAISALSAfHPEANPALAgQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRR--RAGrPPNLPSQDLSYTEN 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 246 FSHMLGFKS-------PQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLlwi 318
Cdd:cd06115  187 FLYMLDSLGerkykpnPRLARALDILFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVL--- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 319 kSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREFAlkhlpdDPLFQLVSK--LYEVVppilTE 396
Cdd:cd06115  263 -RMLAEIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGKdpLIEIA----VA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 397 LGKV---------KNPWPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIGICSQliWDRAL---GLPLERPKSVTM-EWL 463
Cdd:cd06115  329 LEKAalsdeyfvkRKLYPNVDFYSGLIYRAMGFP-TDFFPVLFAIPRMAGYLAH--WRESLddpDTKIMRPQQLYTgVWL 405

                 ...
gi 508704881 464 ENY 466
Cdd:cd06115  406 RHY 408
PRK12349 PRK12349
citrate synthase;
133-443 5.97e-29

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 117.13  E-value: 5.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALqvqSEFQKAYEKGIPkskywEPTYEDALSL 212
Cdd:PRK12349  55 EHLPNEDEKATLEKKLKEEYAVPEGVFNILKALPKETHPMDGLRTGVSAL---AGYDNDIEDRSL-----EVNKSRAYKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVPLVASYVYRRIYKDgNFIAMDDSLDYGGNFSHMLGFKSPQMQElMRLY---VTIHSDHEGGNvSAHTGHLVGSALS 289
Cdd:PRK12349 127 LSKVPNIVANSYHILNNE-EPIEPLKELSYSANFLYMLTGKKPTELE-EKIFdrsLVLYSEHEMPN-STFTARVIASTQS 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 290 DPYLSFAAALNGLAGPLHGLANQEVLLWIKsvvdecgENITKEQLKDYVWKTLNSGKVVPGFGHGV-LRKTDPRYTCQRE 368
Cdd:PRK12349 204 DLYGALTGAVASLKGSLHGGANEAVMYMLL-------EAGTVEKFEELLQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508704881 369 fALKHL----PDDplfqlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIGICSQLI 443
Cdd:PRK12349 277 -ALKQLcdvkGDY-------TLYEMCEAGEKIMEKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
PRK14034 PRK14034
citrate synthase; Provisional
133-437 3.84e-28

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 114.86  E-value: 3.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPV-SAHPMTQFATGVMALQVQSEFQKAYEKgipkskywEPTYEDALS 211
Cdd:PRK14034  51 RKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDLkKVHPMSVLRTAISMLGLYDEEAEIMDE--------EANYRKAVR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 LIARVP-LVASYvyRRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQ--MQELMRLYVTIHSDHEGgNVSAHTGHLVGSAL 288
Cdd:PRK14034 123 LQAKVPtIVAAF--SRIRKGLDPVEPRKDLSLAANFLYMLNGEEPDevEVEAFNKALVLHADHEL-NASTFTARVCVATL 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 289 SDPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGEnitKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQRE 368
Cdd:PRK14034 200 SDVYSGITAAIGALKGPLHGGANENVM----KMLTEIGE---EENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLRE 272
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508704881 369 FALKhlpddpLFQLV--SKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIG 437
Cdd:PRK14034 273 MSKR------LTVLLgeEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSG 336
PRK14032 PRK14032
citrate synthase; Provisional
209-439 2.49e-27

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 113.85  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 209 ALSLIARVPLVASYVYR--RIYKDGNFIAM---DDSLDYGGNFSHML----GFkSPQMQELMRLYVTIHSDHEGGNVSAH 279
Cdd:PRK14032 168 SISLIARFPTLAVYAYQayRHYHDGKSLYIhppKPELSTAENILYMLrpdnKY-TELEARLLDLALVLHAEHGGGNNSTF 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 280 TGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGENITKEQLKDYVWKTLN------SGkVVPGFGH 353
Cdd:PRK14032 247 TTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNkeafdkSG-LIYGMGH 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 354 GVLRKTDPRYTCQREFAL-----KHLPDDplFQLVSKLYEVVPPILTELGKV-KNPWPNVDAHSGVLLNYFGLTEaRYYT 427
Cdd:PRK14032 326 AVYTISDPRAVILKKFAEklakeKGREEE--FNLYEKIEKLAPELIAEERGIyKGVSANVDFYSGFVYDMLGIPE-ELYT 402
                        250
                 ....*....|..
gi 508704881 428 VLFGVSRSIGIC 439
Cdd:PRK14032 403 PLFAIARIVGWS 414
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
132-439 3.35e-27

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: 112.75  E-value: 3.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 132 TGKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQvqsefqkAYEKGiPKSKYWEPTYEDALS 211
Cdd:cd06113   69 FGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQRSVLALY-------SYDDK-PDDISLENVLRQSIQ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 LIARVPLVASYVYR--RIYKDGN--FI-AMDDSLDYGGNFSHMLgfkSPQMQ------ELMRLYVTIHSDHEGGNVSAHT 280
Cdd:cd06113  141 LIARLPTIAVYAYQakRHYYDGEslYIhHPQPELSTAENILSML---RPDKKyteleaKLLDLCLVLHAEHGGGNNSTFT 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 281 GHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDEcGENIT-KEQLKDYVWKTLN------SGkVVPGFGH 353
Cdd:cd06113  218 TRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKEN-VKDWTdEDEVRAYLRKILNkeafdkSG-LIYGMGH 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 354 GVLRKTDPRYTCQREFAL-----KHLPDDplFQLVSKLYEVVPPILTE-LGKVKNPWPNVDAHSGVLLNYFGLTEaRYYT 427
Cdd:cd06113  296 AVYTLSDPRAVVLKKYARslakeKGREEE--FALYERIERLAPEVIAEeRGIGKTVCANVDFYSGFVYKMLGIPQ-ELYT 372
                        330
                 ....*....|..
gi 508704881 428 VLFGVSRSIGIC 439
Cdd:cd06113  373 PLFAVARIVGWC 384
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
133-447 1.36e-26

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: 110.47  E-value: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMAL---QVQSEFQKAYEKGIpkskyweptyeda 209
Cdd:cd06108   49 GKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCSMLgclEPENEFSQQYEIAI------------- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 210 lSLIARVPLVASYVY------RRIYKDGNfiamDDSLdyGGNFSHMLGFKSPQMQEL--MRLYVTIHSDHEgGNVSAHTG 281
Cdd:cd06108  116 -RLLAIFPSILLYWYhyshsgKRIETETD----EDSI--AGHFLHLLHGKKPGELEIkaMDVSLILYAEHE-FNASTFAA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 282 HLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDEcgenitkEQLKDYVWKTLNSGKVVPGFGHGVLRKTDP 361
Cdd:cd06108  188 RVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSP-------EEAEQGLLEKLERKELIMGFGHRVYKEGDP 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 362 RYTCQREFALKHLPD--DPlfqlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGL-TEarYYTVLFGVSRSIGI 438
Cdd:cd06108  261 RSDIIKKWSKKLSEEggDP------LLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIpTE--LFTPIFVMSRVTGW 332

                 ....*....
gi 508704881 439 CSQLIWDRA 447
Cdd:cd06108  333 AAHIMEQRA 341
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
133-458 1.63e-26

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: 110.30  E-value: 1.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMALQvqSEFQKAYEKGIPKSKYWEptyedALSL 212
Cdd:cd06116   55 GELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALS--TFYPEAKNIGDEEQRNKQ-----IIRL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVPLVASYVYRriYKDG-NFIAMDDSLDYGGNFSHMLGFKS-------PQMQELMRLYVTIHSDHEGgNVSAHTGHLV 284
Cdd:cd06116  128 IGKMPTIAAFAYR--HRLGlPYVLPDNDLSYTGNFLSMLFKMTepkyepnPVLAKALDVLFILHADHEQ-NCSTSAMRSV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 285 GSALSDPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVwKTLNSGKV-VPGFGHGVLRKTDPRY 363
Cdd:cd06116  205 GSSRADPYTAVAAAVAALYGPLHGGANEAVL----RMLQQIG---SPKNIPDFI-ETVKQGKErLMGFGHRVYKNYDPRA 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 364 TCQREFA---LKHLPDDPLFQLVSKLYEVVppILTELGKVKNPWPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIGICS 440
Cdd:cd06116  277 RIIKKIAdevFEATGRNPLLDIAVELEKIA--LEDEYFISRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLA 353
                        330       340
                 ....*....|....*....|.
gi 508704881 441 QliWDRALGLP---LERPKSV 458
Cdd:cd06116  354 Q--WIEMLRDPeqkIARPRQV 372
PRK14035 PRK14035
citrate synthase; Provisional
134-437 1.68e-26

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 110.23  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 134 KVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVS-AHPMTQFATGVMALQVQSEfqKAYEKGIpkskywEPTYEDALSL 212
Cdd:PRK14035  52 RLPTEEELAHLKGKLRKYMTLNDRVYQHFEEYSTDhVHPMTALRTSVSYLAHFDP--DAEEESD------EARYERAIRI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVP-LVASYVyrRIYKDGNFIAMDDSLDYGGNFSHMLGFKSPQMQEL--MRLYVTIHSDHEGgNVSAHTGHLVGSALS 289
Cdd:PRK14035 124 QAKVAsLVTAFA--RVRQGKEPLKPRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTFTARCAVSSLS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 290 DPYLSFAAALNGLAGPLHGLANQEV---LLWIKSVvdecgenitkEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQ 366
Cdd:PRK14035 201 DMYSGVVAAVGSLKGPLHGGANERVmdmLSEIRSI----------GDVDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYL 270
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508704881 367 REFAlKHLPDDplfQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIG 437
Cdd:PRK14035 271 REMS-RKITKG---TGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGI-PHDLFTPIFAVSRVAG 336
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
132-437 2.22e-26

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 110.04  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 132 TGKVPSKAQVDALSQELRS-RAVVPDyVFKAIDALPVSAHPM--TQFATGVMALQVQSEFQKAYEKgipkskywepTYED 208
Cdd:PRK14033  58 NGELPTDAELALFSQRERAyRRLDRS-VLSLIDKLPTTCHPMdvVRTAVSYLGAEDPEADDSSPEA----------NLAK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 209 ALSLIARVPLVASYVYRRiYKDGNFIAMDDSLDYGGNFSHMLgF---KSPQMQELMRLYVTIHSDHeGGNVSAHTGHLVG 285
Cdd:PRK14033 127 ALRLFAVLPTIVAADQRR-RRGLDPIAPRSDLGYAENFLHMC-FgevPEPEVVRAFEVSLILYAEH-SFNASTFTARVIT 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 286 SALSDPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTC 365
Cdd:PRK14033 204 STLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHGDSRVPT 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508704881 366 QREfALKHLPDDPLFQLVSKLYEVVPPILTELGKVKnpwPNVDAHSGVLLNYFGLtEARYYTVLFGVSRSIG 437
Cdd:PRK14033 277 MKA-ALRRVAAVRDGQRWLDIYEALEKAMAEATGIK---PNLDFPAGPAYYLMGF-DIDFFTPIFVMSRITG 343
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
133-446 1.21e-23

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: 101.85  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMAL-QVQSEfqkayekgipKSKYWEPTYED-AL 210
Cdd:cd06117   49 GKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLgCVLPE----------KEDHPVSGARDiAD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 211 SLIARVPLVASYVY------RRIYKDGNfiamDDSLdyGGNFSHML-GFKSPQMQE-LMRLYVTIHSDHEGgNVSAHTGH 282
Cdd:cd06117  119 RLMASLGSILLYWYhyshngKRIEVETD----DDSI--GGHFLHLLhGEKPSESWEkAMHISLILYAEHEF-NASTFTAR 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 283 LVGSALSDPYLSFAAALNGLAGPLHGLANqEVLLWIKS---VVDECGENITKEqlkdyvwktLNSGKVVPGFGHGVLRKT 359
Cdd:cd06117  192 VIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQryeSADEAEADIRRR---------VENKEVVIGFGHPVYTIA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 360 DPRYTCQREFAlKHLPDDPLFQlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEArYYTVLFGVSRSIGIC 439
Cdd:cd06117  262 DPRNQVIKEVA-KQLSKEGGDM---KMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTA-MFTPLFVIARTTGWS 336

                 ....*..
gi 508704881 440 SQLIWDR 446
Cdd:cd06117  337 AHIIEQR 343
PRK14037 PRK14037
citrate synthase; Provisional
133-443 5.86e-22

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 97.13  E-value: 5.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALP--VSAHPMTQFATGVMAlqvqsefqkayekGIPKSKYWEPTYED-A 209
Cdd:PRK14037  54 GELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPrdSDAIGLMEAAFAALA-------------SIDKNFKWKENDKEkA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 210 LSLIARVPLVASYVYRriYKDGNFIAM-DDSLDYGGNFSHMLGFKSPQMQEL--MRLYVTIHSDHEggnVSAHT--GHLV 284
Cdd:PRK14037 121 ISIIAKMATIVANVYR--RKEGNKPRIpEPSDSFAESFLLASFAREPTAEEIkaMDAALILYTDHE---VPASTtaALVA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 285 GSALSDPYLSFAAALNGLAGPLHGLANQEVllwIKSVVDECGENITKEQLKDyvwKTLNSGKVVPGFGHGVLRKTDPRYT 364
Cdd:PRK14037 196 ASTLSDMYSCITAALAALKGPLHGGAAEEA---FKQFVEIGDPNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAK 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 365 CQREFALKHLPDDPlfqLVSKLYEVVPPiLTELG----KVKNPWPNVDAHSGVLlnYFGLTEARY-YTVLFGVSRSIGIC 439
Cdd:PRK14037 270 IFKELAETLIERNS---EAKKYFEIAQK-LEELGikqfGSKGIYPNTDFYSGIV--FYALGFPVYmFTALFALSRTLGWL 343

                 ....
gi 508704881 440 SQLI 443
Cdd:PRK14037 344 AHII 347
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
133-458 9.25e-22

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: 96.22  E-value: 9.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALpVSAHPMTQFATGVMALQVqsefqkayekgipkskywEPTYEDALSL 212
Cdd:cd06109   49 GFFPDLPELEEFRAALAAARALPDVVAALLPAL-AGLDPMDALRALLALLPD------------------SPDLATALRL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 213 IARVP-LVASYVYRRIYKDgnFIAMDDSLDYGGNFSHMLGFKSPQMQELMRL--YVTIHSDHeGGNVSAHTGHLVGSALS 289
Cdd:cd06109  110 LAAAPvITAALLRLSRGKQ--PIAPDPSLSHAADYLRMLTGEPPSEAHVRALdaYLVTVADH-GMNASTFTARVIASTEA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 290 DPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPRYTCQREf 369
Cdd:cd06109  187 DLTSAVLGAIGALKGPLHGGAPGPVL----DMLDAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA- 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 370 ALKHLP-DDPLFQLVSklyEVVPPILTELGKVKNPWP---NVDAHSGVLLNYFGLtEARYYTVLFGVSRSIGICSQLIWD 445
Cdd:cd06109  259 AAERLGaPDERLEFAE---AVEQAALALLREYKPGRPletNVEFYTALLLEALGL-PREAFTPTFAAGRTAGWTAHVLEQ 334
                        330
                 ....*....|...
gi 508704881 446 RALGLpLERPKSV 458
Cdd:cd06109  335 ARTGR-LIRPQSR 346
PRK12351 PRK12351
methylcitrate synthase; Provisional
133-447 1.35e-20

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 93.06  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 133 GKVPSKAQVDALSQELRSRAVVPDYVFKAIDALPVSAHPMTQFATGVMAL-QVQSEfqkAYEKGIPKSKyweptyEDALS 211
Cdd:PRK12351  58 GKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgCLLPE---KEDHNFSGAR------DIADR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 212 LIARVPLVASYVYRRIYkDGNFIAM---DDSLdyGGNFSHMLGFKSPQ------MQELMRLYvtihSDHEGgNVSAHTGH 282
Cdd:PRK12351 129 LLASLGSILLYWYHYSH-NGRRIEVetdDDSI--GGHFLHLLHGKKPSeswvkaMHTSLILY----AEHEF-NASTFTAR 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 283 LVGSALSDPYLSFAAALNGLAGPLHGLANqEVLLWIKSVVDecgeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDPR 362
Cdd:PRK12351 201 VIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQRYD------TPDEAEADIRRRVENKEVVIGFGHPVYTISDPR 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 363 YTCQREFAlKHLPDDplfQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYFGLTEArYYTVLFGVSRSIGICSQL 442
Cdd:PRK12351 274 NKVIKEVA-KKLSKE---AGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTA-MFTPLFVISRTTGWAAHV 348

                 ....*
gi 508704881 443 IWDRA 447
Cdd:PRK12351 349 IEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
207-459 8.34e-14

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 72.30  E-value: 8.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 207 EDALSLIARVPLVASYVYRRIYKDGNFIAMDDSLDYGGNFSHML-----GFKSPQMQELMRLYVTIHSDHeGGNVSAHTG 281
Cdd:PRK12350  99 TARLDLARASVMALSAVAQSARGIGQPAVPQREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 282 HLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLlwikSVVDECGeniTKEQLKDYVWKTLNSGKVVPGFGHGVLRKTDP 361
Cdd:PRK12350 178 RVIASTGADVAAALSGAIGALSGPLHGGAPARVL----PMLDAVE---RTGDARGWVKGALDRGERLMGFGHRVYRAEDP 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 362 RYTCQREfALKHLpDDPLFQLVSKLYEVVPPILTElgkvKNP----WPNVDAHSGVLLNYFGLTeARYYTVLFGVSRSIG 437
Cdd:PRK12350 251 RARVLRA-TAKRL-GAPRYEVAEAVEQAALAELRE----RRPdrplETNVEFWAAVLLDFAGVP-AHMFTAMFTCGRTAG 323
                        250       260
                 ....*....|....*....|..
gi 508704881 438 ICSQLIWDRALGLpLERPKSVT 459
Cdd:PRK12350 324 WSAHILEQKRTGR-LVRPSARY 344
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
254-362 2.16e-08

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


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 55.34  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 254 SPQMQELMRLYVTIHSDHEGgNVSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKSVVDECGenitkeq 333
Cdd:cd06102   94 DPAAADLLRRALVLLADHEL-NASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGD------- 165
                         90       100
                 ....*....|....*....|....*....
gi 508704881 334 LKDYVWKTLNSGKVVPGFGHGVLRKTDPR 362
Cdd:cd06102  166 AEAAVRERLRRGEALPGFGHPLYPDGDPR 194
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
277-438 1.67e-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: 39.86  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 277 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQ---EVLLWI---KSVVDECGENITKEQLKdyvwktlnSGKVVPG 350
Cdd:cd06100   50 SAHAARLTASAGPEDLQSAVAAGLLGIGDRFGGAGEgaaRLFKEAvdsGDALDAAAAEFVAEYRA--------AKKRIPG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508704881 351 FGHGVLRKTDPRYTCQREFALKHLPDDPLFqlvsKLYEVVPPILTELGKVKNPWpNVDAHSGVLLNYFGLTeARYYTVLF 430
Cdd:cd06100  122 FGHPVHKNPDPRVPRLLELARELGPAGPHL----DYALAVEKALTAAKGKPLPL-NVDGAIAAILLDLGFP-PGALRGLF 195

                 ....*...
gi 508704881 431 GVSRSIGI 438
Cdd:cd06100  196 VLGRSPGL 203
 
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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