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Conserved domains on  [gi|1039016053|gb|ANM65553|]
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citrate synthase 5 [Arabidopsis thaliana]

Protein Classification

citrate synthase family protein( domain architecture ID 475)

citrate synthase family protein similar to citrate synthase that catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle

CATH:  1.10.580.10
EC:  2.3.-.-
Gene Ontology:  GO:0016746
PubMed:  3013232
SCOP:  3001050

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CS_ACL-C_CCL super family cl00416
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
37-422 0e+00

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.


The actual alignment was detected with superfamily member cd06105:

Pssm-ID: 469765  Cd Length: 427  Bit Score: 757.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:cd06105     1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdISK 196
Cdd:cd06105    81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEG-IHK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNVSA 276
Cdd:cd06105   160 SKYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 277 HAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVLRK 356
Cdd:cd06105   240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039016053 357 TDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTEAS 422
Cdd:cd06105   320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMN 385
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
37-422 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: 757.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:cd06105     1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdISK 196
Cdd:cd06105    81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEG-IHK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNVSA 276
Cdd:cd06105   160 SKYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 277 HAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVLRK 356
Cdd:cd06105   240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039016053 357 TDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTEAS 422
Cdd:cd06105   320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMN 385
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
35-422 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: 691.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  35 LDLKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAES 114
Cdd:TIGR01793   2 LDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 115 GEEPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdI 194
Cdd:TIGR01793  82 GEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKG-I 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 195 SKSKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNV 274
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 275 SAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVL 354
Cdd:TIGR01793 241 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVL 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039016053 355 RKTDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTEAS 422
Cdd:TIGR01793 321 RKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEAR 388
PLN02456 PLN02456
citrate synthase
5-420 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 555.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053   5 RSVSAISRLRSRAVQQSSLSNSVRWLHSSELDLKSQMQEIIPEQQDRLKKLKSeqGKVPVGNITVDmvlGGMRGMTGLLW 84
Cdd:PLN02456    2 AAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVLS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  85 ETSLLDADEGI-RFRGMSIPECQKILPSAESgeeplpeslLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALP 163
Cdd:PLN02456   77 EISLIDGDEGIlRFRGYPIEELAEKSPFEEV---------AYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 164 STAHPMTQFASGVMALQVQSEFQKAYEQGdISKSKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPlDDSLDYGAN 243
Cdd:PLN02456  148 HDAHPMTQLVSGVMALSTFSPDANAYLRG-QHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP-DNSLDYAEN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 244 FSHMLGF-------DSPQMKELMRLYVTIHSDHEGGNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 316
Cdd:PLN02456  226 FLYMLGSlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 317 KlvveECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFAL---KHLPDDPLFQLVSKLYEVVppILT 393
Cdd:PLN02456  306 K----EIG---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLD 376
                         410       420
                  ....*....|....*....|....*..
gi 1039016053 394 ELGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:PLN02456  377 EYFKVRKLYPNVDFYSGVLLRALGFPE 403
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
75-420 1.26e-110

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: 329.08  E-value: 1.26e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  75 GMRGMTGLLWETSLLDADEG-IRFRGMSIPE-CQKilpsaESGEEP---LpesllwllLTGKVPTKEQANALSTELAHRA 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAER-----SSFEEVaylL--------LTGELPTKEELEEFSAELAAHR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 150 AVPDYIYKAIDALPSTAHPMTQFASGVMALQvqsefqKAYEQGDISKSKYWEPTFEDalNLIARVPVVASYVYRRMYKDG 229
Cdd:pfam00285  68 ELPEDVLELLRALPRDAHPMAVLRAAVSALA------AFDPEAISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 230 SIIPlDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGL 307
Cdd:pfam00285 140 PIYP-DPDLSYAENFLYMLFGYepDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 308 ANQEVLLWIKlvveecgESISKEQLKDYVWKTLNSGK-VVPGYGHGVLRKTDPRYICQREFALKHLP---DDPLFQLVSK 383
Cdd:pfam00285 218 ANEAVLEMLE-------EIGSPDEVEEYIRKVLNKGKeRIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEE 290
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1039016053 384 LYEVVPPILTELGkvKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:pfam00285 291 LEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT 325
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
75-418 2.25e-87

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: 270.81  E-value: 2.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  75 GMRGMTGLLWETSLLDADEGI-RFRGMSIPECqkilpsAE--SGEEplpesllwlllT------GKVPTKEQANALSTEL 145
Cdd:COG0372    16 GLEGVVAGETAISYIDGEKGIlRYRGYPIEDL------AEksSFEE-----------VaylllyGELPTKEELAEFKAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 146 AHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQvqsefqkAYEQGDISKSKywEPTFEDALNLIARVPVVASYVYRrm 225
Cdd:COG0372    79 ARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALG-------AFDPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 226 YKDG-SIIPLDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAG 302
Cdd:COG0372   148 YRRGlPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 303 PLHGLANQEVLLWIKlvveecgESISKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFA---LKHLPDDPLFQ 379
Cdd:COG0372   227 PLHGGANEAVLEMLE-------EIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLE 299
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039016053 380 LVSKLYEVVPPilTELGKVKNPWPNVDAHSGVLLNYYGL 418
Cdd:COG0372   300 IAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGI 336
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
37-422 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: 757.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:cd06105     1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdISK 196
Cdd:cd06105    81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEG-IHK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNVSA 276
Cdd:cd06105   160 SKYWEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 277 HAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVLRK 356
Cdd:cd06105   240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039016053 357 TDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTEAS 422
Cdd:cd06105   320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMN 385
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
35-422 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: 691.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  35 LDLKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAES 114
Cdd:TIGR01793   2 LDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 115 GEEPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdI 194
Cdd:TIGR01793  82 GEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKG-I 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 195 SKSKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNV 274
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSISIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGNV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 275 SAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVL 354
Cdd:TIGR01793 241 SAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAVL 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039016053 355 RKTDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTEAS 422
Cdd:TIGR01793 321 RKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEAR 388
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
37-420 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: 631.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:cd06103     1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGDISK 196
Cdd:cd06103    81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGKINK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMY-KDGSIIPLDDSLDYGANFSHMLGFDSPQMKELMRLYVTIHSDHEGGNVS 275
Cdd:cd06103   161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYrKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 276 AHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVLR 355
Cdd:cd06103   241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039016053 356 KTDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:cd06103   321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTE 385
PLN02456 PLN02456
citrate synthase
5-420 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 555.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053   5 RSVSAISRLRSRAVQQSSLSNSVRWLHSSELDLKSQMQEIIPEQQDRLKKLKSeqGKVPVGNITVDmvlGGMRGMTGLLW 84
Cdd:PLN02456    2 AAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKA--GKDDLGLKTVD---PGYRNTAPVLS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  85 ETSLLDADEGI-RFRGMSIPECQKILPSAESgeeplpeslLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALP 163
Cdd:PLN02456   77 EISLIDGDEGIlRFRGYPIEELAEKSPFEEV---------AYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 164 STAHPMTQFASGVMALQVQSEFQKAYEQGdISKSKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPlDDSLDYGAN 243
Cdd:PLN02456  148 HDAHPMTQLVSGVMALSTFSPDANAYLRG-QHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP-DNSLDYAEN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 244 FSHMLGF-------DSPQMKELMRLYVTIHSDHEGGNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 316
Cdd:PLN02456  226 FLYMLGSlgdrsykPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 317 KlvveECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFAL---KHLPDDPLFQLVSKLYEVVppILT 393
Cdd:PLN02456  306 K----EIG---TVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLD 376
                         410       420
                  ....*....|....*....|....*..
gi 1039016053 394 ELGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:PLN02456  377 EYFKVRKLYPNVDFYSGVLLRALGFPE 403
PRK09569 PRK09569
citrate (Si)-synthase;
37-420 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 541.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:PRK09569    3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGDISK 196
Cdd:PRK09569   83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGKFNK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFdSPQMKELMRLYVTIHSDHEGGNVSA 276
Cdd:PRK09569  163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQIPSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVSA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 277 HAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEE-CGESISKEQLKDYVWKTLNSGKVVPGYGHGVLR 355
Cdd:PRK09569  242 HTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKlGGEEPTKEQVEQALWDTLNAGQVIPGYGHAVLR 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039016053 356 KTDPRYICQREFALKHLPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:PRK09569  322 KTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKE 386
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
37-420 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: 527.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  37 LKSQMQEIIPEQQDRLKKLKSEQGKVPVGNITVDMVLGGMRGMTGLLWETSLLDADEGIRFRGMSIPECQKILPSAESGE 116
Cdd:cd06106     1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 117 EPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVQSEFQKAYEQGdISK 196
Cdd:cd06106    81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKG-IKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 197 SKYWEPTFEDALNLIARVPVVASYVYRRMYKDGSIIP-LDDSLDYGANFSHMLGF-DSPQMKELMRLYVTIHSDHEGGNV 274
Cdd:cd06106   160 TEYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGkIDPEVDWSYNFTSMLGYgDNLDFVDLLRLYIALHGDHEGGNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 275 SAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLNSGKVVPGYGHGVL 354
Cdd:cd06106   240 SAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVL 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039016053 355 RKTDPRYICQREFALKH--LPDDPLFQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:cd06106   320 RKPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIRE 387
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
75-420 1.26e-110

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: 329.08  E-value: 1.26e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  75 GMRGMTGLLWETSLLDADEG-IRFRGMSIPE-CQKilpsaESGEEP---LpesllwllLTGKVPTKEQANALSTELAHRA 149
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAER-----SSFEEVaylL--------LTGELPTKEELEEFSAELAAHR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 150 AVPDYIYKAIDALPSTAHPMTQFASGVMALQvqsefqKAYEQGDISKSKYWEPTFEDalNLIARVPVVASYVYRRMYKDG 229
Cdd:pfam00285  68 ELPEDVLELLRALPRDAHPMAVLRAAVSALA------AFDPEAISDKADYWENALRD--DLIAKLPTIAAYIYRHRRGLP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 230 SIIPlDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGL 307
Cdd:pfam00285 140 PIYP-DPDLSYAENFLYMLFGYepDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 308 ANQEVLLWIKlvveecgESISKEQLKDYVWKTLNSGK-VVPGYGHGVLRKTDPRYICQREFALKHLP---DDPLFQLVSK 383
Cdd:pfam00285 218 ANEAVLEMLE-------EIGSPDEVEEYIRKVLNKGKeRIMGFGHRVYKNYDPRAKILKEFAEELAEeggDDPLLELAEE 290
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1039016053 384 LYEVVPPILTELGkvKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:pfam00285 291 LEEVAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT 325
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
74-417 5.64e-100

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: 302.21  E-value: 5.64e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  74 GGMRGMTGLLWETSLLDADEGI-RFRGMSIPECQkilpsaesgEEPLPESLLWLLLTGKVPTKEQANALSTELAHRAAVP 152
Cdd:cd06118     1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELA---------EKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 153 DYIYKAIDALPSTAHPMTQFASGVMALQVQSEFqkayeqgdiSKSKYWEPTFEDALNLIARVPVVASYVYRrmYKDG-SI 231
Cdd:cd06118    72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPF---------ARDKSPEARYEKAIRLIAKLPTIAANIYR--NREGlEI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 232 IPLDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLAN 309
Cdd:cd06118   141 IAPDPDLSYAENFLYMLFGEepDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGAN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 310 QEVLLWIklvvEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLP---DDPLFQLVSKLYE 386
Cdd:cd06118   220 EAVLKML----LEIG---TPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEekgDDKLFEIAEELEE 292
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1039016053 387 VVPPILTElgkvKNPWPNVDAHSGVLLNYYG 417
Cdd:cd06118   293 IALEVLGE----KGIYPNVDFYSGVVYKALG 319
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
75-418 2.25e-87

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: 270.81  E-value: 2.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  75 GMRGMTGLLWETSLLDADEGI-RFRGMSIPECqkilpsAE--SGEEplpesllwlllT------GKVPTKEQANALSTEL 145
Cdd:COG0372    16 GLEGVVAGETAISYIDGEKGIlRYRGYPIEDL------AEksSFEE-----------VaylllyGELPTKEELAEFKAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 146 AHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQvqsefqkAYEQGDISKSKywEPTFEDALNLIARVPVVASYVYRrm 225
Cdd:COG0372    79 ARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALG-------AFDPDADDIDP--EARLEKAIRLIAKLPTIAAYAYR-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 226 YKDG-SIIPLDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAG 302
Cdd:COG0372   148 YRRGlPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGALKG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 303 PLHGLANQEVLLWIKlvveecgESISKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFA---LKHLPDDPLFQ 379
Cdd:COG0372   227 PLHGGANEAVLEMLE-------EIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDPLLE 299
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039016053 380 LVSKLYEVVPPilTELGKVKNPWPNVDAHSGVLLNYYGL 418
Cdd:COG0372   300 IAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGI 336
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
239-419 8.62e-62

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: 200.62  E-value: 8.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 239 DYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 316
Cdd:cd06101    53 SYAENFLYMLGGEepDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKML 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 317 klvvEECGESIsKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLP---DDPLFQLVSKLYEVVPPILT 393
Cdd:cd06101   132 ----EEIGTPK-NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKekgLDPMFELAAELEKIAPEVLY 206
                         170       180
                  ....*....|....*....|....*.
gi 1039016053 394 ElgkvKNPWPNVDAHSGVLLNYYGLT 419
Cdd:cd06101   207 E----KKLYPNVDFYSGVLYKAMGFP 228
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
239-419 4.47e-61

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: 197.17  E-value: 4.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 239 DYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWI 316
Cdd:cd06099     1 SYAENFLYMLGGEepDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 317 klvvEECGESIsKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLP---DDPLFQLVSKLYEVVPpilt 393
Cdd:cd06099    80 ----EEIGTPK-NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKedgDDPMFELAAELEKIAE---- 150
                         170       180
                  ....*....|....*....|....*.
gi 1039016053 394 ELGKVKNPWPNVDAHSGVLLNYYGLT 419
Cdd:cd06099   151 EVLYEKKLYPNVDFYSGVLYKAMGFP 176
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
75-418 2.37e-40

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: 147.04  E-value: 2.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  75 GMRGMTGLLWETSLLDADEGI-RFRGMSIPEcqkiLPSAESGEEplpesLLWLLLTGKVPTKEQANALSTELAHRAAVPD 153
Cdd:cd06110     2 GLEGVIAADSKISYIDGDAGIlIYRGYDIHD----LAENSTFEE-----VAYLLWNGELPTAEELDAFKAQLAAERELPA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 154 YIYKAIDALPSTAHPMTQFASGVMALQVQSEfqkayEQGDISKskywEPTFEDALNLIARVPVVASYvYRRMYKDGSIIP 233
Cdd:cd06110    73 EIIDLLKLLPKDAHPMDVLRTAVSALALYDP-----EADDMSR----EANLRKAIRLIAKMPTIVAA-FHRIRNGLEPVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 234 LDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQE 311
Cdd:cd06110   143 PDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANER 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 312 VLLWIklvvEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFA--LKHLPDDPlfqlvsKLYEVVP 389
Cdd:cd06110   222 VMKML----LEIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSrrLGKETGEP------KWYEMSE 288
                         330       340
                  ....*....|....*....|....*....
gi 1039016053 390 PILTELGKVKNPWPNVDAHSGVLlnYYGL 418
Cdd:cd06110   289 AIEQAMRDEKGLNPNVDFYSASV--YYML 315
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
87-417 2.08e-36

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: 136.78  E-value: 2.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  87 SLLDADEGI-RFRGMSIPEcqkiLPSAESGEEplpesLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPST 165
Cdd:cd06112    16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 166 AHPMTQFASGVMALQVQSEFQKaYEQGDiskSKYwepTFEDALNLIARVP-VVASYvyRRMYKDGSIIPLDDSLDYGANF 244
Cdd:cd06112    87 GHPMDMLQATVAALGMFYPKPE-VLKPN---PDY---IDAATVKLIAKMPtLVAMW--ARIRNGDDPIEPRPDLDYAENF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 245 SHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLlwikLVVEE 322
Cdd:cd06112   158 LYMLFGEepDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVL----EMLEE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 323 CGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLPDDPLFqlvSKLYEV---VPPILTELGKVK 399
Cdd:cd06112   233 IG---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGEL---SKLYEIaleVERLCEELLGHK 306
                         330
                  ....*....|....*...
gi 1039016053 400 NPWPNVDAHSGVLLNYYG 417
Cdd:cd06112   307 GVYPNVDFYSGIVYKELG 324
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
87-413 2.52e-32

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: 126.01  E-value: 2.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  87 SLLDADEGI-RFRGMSIPEcqkiLPSAESGEEPLpesllWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPST 165
Cdd:cd06107    20 TYIDGDKGIlLYRGYPIEQ----LAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 166 AHPMTQFASGVMALQV-QSEFQKAYEQGDISKSKywEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPlDDSLDYGANF 244
Cdd:cd06107    91 AHPMGILCAGLSALSAfYPEAIPAHTGDLYQNNP--EVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYP-RANLSYIENF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 245 SHMLGF-------DSPQMKELMRLYVTIHSDHEgGNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIk 317
Cdd:cd06107   168 LYMMGYvdqepyePNPRLARALDRLWILHADHE-MNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKML- 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 318 lvvEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFA---LKHLPDDPLFQLVSKLYEVVppILTE 394
Cdd:cd06107   246 ---REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIA--LEDE 317
                         330
                  ....*....|....*....
gi 1039016053 395 LGKVKNPWPNVDAHSGVLL 413
Cdd:cd06107   318 YFVSRKLYPNVDFYSGFIY 336
PRK14036 PRK14036
citrate synthase; Provisional
130-412 9.55e-31

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 121.60  E-value: 9.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQVqseFqkaYEQGDISKSKYwepTFEDALN 209
Cdd:PRK14036   54 GELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPETGHPMDALQASAAALGL---F---YSRRALDDPEY---IRDAVVR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVP-VVASYvyRRMYKDGSIIPLDDSLDYGANFSHMLGFD--SPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSAL 286
Cdd:PRK14036  125 LIAKIPtMVAAF--QLIRKGNDPIQPRDDLDYAANFLYMLTERepDPLAARIFDRCLILHAEHTI-NASTFSARVTASTL 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 287 SDPYLSFAAALNGLAGPLHGLANQEVLlwikLVVEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQRE 366
Cdd:PRK14036  202 TDPYAVIASAVGTLAGPLHGGANEDVL----AMLEEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQK 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039016053 367 FA---LKHLPDDPLFQLVSKLYEVVPPILTElgkvKNPWPNVDAHSGVL 412
Cdd:PRK14036  275 LAeelFARFGHDEYYEIALELERVAEERLGP----KGIYPNVDFYSGLV 319
gltA PRK05614
citrate synthase;
130-413 1.92e-30

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 121.52  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALqvqSEFQkaYEQGDISKSKYWEPTfedALN 209
Cdd:PRK05614   95 GELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGAL---SAFY--HDSLDINDPEHREIA---AIR 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVPVVASYVYRrmYKDGS--IIPlDDSLDYGANFSHMLgFD--------SPQMKELMRLYVTIHSDHEgGNVSAHAG 279
Cdd:PRK05614  167 LIAKMPTLAAMAYK--YSIGQpfVYP-RNDLSYAENFLRMM-FAtpceeyevNPVLVRALDRIFILHADHE-QNASTSTV 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 280 HLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLV--VEECGESIskEQLKDyvwKtlNSGKVVPGYGHGVLRKT 357
Cdd:PRK05614  242 RLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIgsVDNIPEFI--ARAKD---K--NDGFRLMGFGHRVYKNY 314
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039016053 358 DPRYICQREFA---LKHL-PDDPLFQLVSKLYEVVppiLT-ELGKVKNPWPNVDAHSGVLL 413
Cdd:PRK05614  315 DPRAKIMRETChevLKELgLNDPLLEVAMELEEIA---LNdEYFIERKLYPNVDFYSGIIL 372
PRK14032 PRK14032
citrate synthase; Provisional
130-410 3.33e-28

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 115.39  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPD-YIYKAIDALPStAHPMTQFASGVMALQvqsefqkAY--EQGDISKSKywepTFED 206
Cdd:PRK14032  100 GELPTKEELAEFTELLGDYRELPDgFTRDMILKAPS-KDIMNSLARSVLALY-------SYddNPDDTSIDN----VLRQ 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 207 ALNLIARVPVVASY---VYRRMYKDGSII--PLDDSLDYGANFSHMLGFD---SPQMKELMRLYVTIHSDHEGGNVSAHA 278
Cdd:PRK14032  168 SISLIARFPTLAVYayqAYRHYHDGKSLYihPPKPELSTAENILYMLRPDnkyTELEARLLDLALVLHAEHGGGNNSTFT 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 279 GHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLN------SGkVVPGYGHG 352
Cdd:PRK14032  248 TRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNkeafdkSG-LIYGMGHA 326
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039016053 353 VLRKTDPRYICQREFAL-----KHLPDDplFQLVSKLYEVVPPILTELGKV-KNPWPNVDAHSG 410
Cdd:PRK14032  327 VYTISDPRAVILKKFAEklakeKGREEE--FNLYEKIEKLAPELIAEERGIyKGVSANVDFYSG 388
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
87-412 5.74e-27

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: 111.38  E-value: 5.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  87 SLLDADEGI-RFRGMSIpecqkilpsaesgeEPLPESLLWLLLT-----GKVPTKEQANALSTELAHRAAVPDYIYKAID 160
Cdd:cd06115    40 SYIDGDKGIlRYRGYPI--------------EELAEKSTFLEVAylliyGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 161 ALPSTAHPMTQFASGVMALQV-QSEFQKAYEQGDISKSKywEPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDsLD 239
Cdd:cd06115   106 SFPHDAHPMGMLVSAISALSAfHPEANPALAGQDIYKNK--QVRDKQIVRILGKAPTIAAAAYRRRAGRPPNLPSQD-LS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 240 YGANFSHMLgfDS---------PQMKELMRLYVTIHSDHEGGNVSAHAGHLvGSALSDPYLSFAAALNGLAGPLHGLANQ 310
Cdd:cd06115   183 YTENFLYML--DSlgerkykpnPRLARALDILFILHAEHEMNCSTAAVRHL-ASSGVDVYTAVAGAVGALYGPLHGGANE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 311 EVLlwikLVVEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFAlkhlpdDPLFQLVSK--LYEVV 388
Cdd:cd06115   260 AVL----RMLAEIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLA------DEVFEIVGKdpLIEIA 326
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1039016053 389 ppilTELGKV---------KNPWPNVDAHSGVL 412
Cdd:cd06115   327 ----VALEKAalsdeyfvkRKLYPNVDFYSGLI 355
PRK12349 PRK12349
citrate synthase;
130-406 2.43e-24

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 103.26  E-value: 2.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALqvqSEFQKAYEQGDISKSKyweptfEDALN 209
Cdd:PRK12349   55 EHLPNEDEKATLEKKLKEEYAVPEGVFNILKALPKETHPMDGLRTGVSAL---AGYDNDIEDRSLEVNK------SRAYK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVPVVASYVYRRMYKDGSIIPlDDSLDYGANFSHMLG--FDSPQMKELMRLYVTIHSDHEGGNvSAHAGHLVGSALS 287
Cdd:PRK12349  126 LLSKVPNIVANSYHILNNEEPIEP-LKELSYSANFLYMLTgkKPTELEEKIFDRSLVLYSEHEMPN-STFTARVIASTQS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 288 DPYLSFAAALNGLAGPLHGLANQEVLLWIKlvveecgESISKEQLKDYVWKTLNSGKVVPGYGHGV-LRKTDPRYICQRE 366
Cdd:PRK12349  204 DLYGALTGAVASLKGSLHGGANEAVMYMLL-------EAGTVEKFEELLQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039016053 367 fALKHL----PDDplfqlvsKLYEVVPPILTELGKVKNPWPNVD 406
Cdd:PRK12349  277 -ALKQLcdvkGDY-------TLYEMCEAGEKIMEKEKGLYPNLD 312
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
129-420 2.72e-24

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: 103.89  E-value: 2.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 129 TGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALQvqsefqkAY--EQGDISKskywEPTFED 206
Cdd:cd06113    69 FGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQRSVLALY-------SYddKPDDISL----ENVLRQ 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 207 ALNLIARVPVVASY---VYRRMYKDGS--IIPLDDSLDYGANFSHMLGFD---SPQMKELMRLYVTIHSDHEGGNVSAHA 278
Cdd:cd06113   138 SIQLIARLPTIAVYayqAKRHYYDGESlyIHHPQPELSTAENILSMLRPDkkyTELEAKLLDLCLVLHAEHGGGNNSTFT 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 279 GHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKLVVEECGESISKEQLKDYVWKTLN------SGkVVPGYGHG 352
Cdd:cd06113   218 TRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENVKDWTDEDEVRAYLRKILNkeafdkSG-LIYGMGHA 296
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039016053 353 VLRKTDPRYICQREFAL-----KHLPDDplFQLVSKLYEVVPPILTE-LGKVKNPWPNVDAHSGVLLNYYGLTE 420
Cdd:cd06113   297 VYTLSDPRAVVLKKYARslakeKGREEE--FALYERIERLAPEVIAEeRGIGKTVCANVDFYSGFVYKMLGIPQ 368
PRK14035 PRK14035
citrate synthase; Provisional
131-409 8.89e-24

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 101.76  E-value: 8.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 131 KVPTKEQANALSTELAHRAAVPDYIYKAI-DALPSTAHPMTQFASGVMALQVQSEfqKAYEQGDiskskywEPTFEDALN 209
Cdd:PRK14035   52 RLPTEEELAHLKGKLRKYMTLNDRVYQHFeEYSTDHVHPMTALRTSVSYLAHFDP--DAEEESD-------EARYERAIR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVP-VVASYVYRRMYKDgSIIPLDDsLDYGANFSHMLGFDSP---QMKELMRLYVtIHSDHEGgNVSAHAGHLVGSA 285
Cdd:PRK14035  123 IQAKVAsLVTAFARVRQGKE-PLKPRPD-LSYAANFLYMLRGELPtdiEVEAFNKALV-LHADHEL-NASTFTARCAVSS 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 286 LSDPYLSFAAALNGLAGPLHGLANQEVLLWIKlvveECGESiskEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQR 365
Cdd:PRK14035  199 LSDMYSGVVAAVGSLKGPLHGGANERVMDMLS----EIRSI---GDVDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLR 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039016053 366 EFAlKHLPDDplfQLVSKLYEVVPPILTELGKVKNPWPNVDAHS 409
Cdd:PRK14035  272 EMS-RKITKG---TGREELFEMSVKIEKRMKEEKGLIPNVDFYS 311
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
129-410 7.72e-23

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 99.25  E-value: 7.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 129 TGKVPTKEQANALST-ELAHRAAVPDYIyKAIDALPSTAHPM--TQFASGVMALQVQSEFqkayeqgDISKskywEPTFE 205
Cdd:PRK14033   58 NGELPTDAELALFSQrERAYRRLDRSVL-SLIDKLPTTCHPMdvVRTAVSYLGAEDPEAD-------DSSP----EANLA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 206 DALNLIARVPVVASYVYRRMyKDGSIIPLDDSLDYGANFSHMLgFD---SPQMKELMRLYVTIHSDHeGGNVSAHAGHLV 282
Cdd:PRK14033  126 KALRLFAVLPTIVAADQRRR-RGLDPIAPRSDLGYAENFLHMC-FGevpEPEVVRAFEVSLILYAEH-SFNASTFTARVI 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 283 GSALSDPYLSFAAALNGLAGPLHGLANQEVLlwikLVVEECGesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYI 362
Cdd:PRK14033  203 TSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHGDSRVP 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039016053 363 CQREfALKHLPDDPLFQLVSKLYEVVPPILTELGKVKnpwPNVDAHSG 410
Cdd:PRK14033  276 TMKA-ALRRVAAVRDGQRWLDIYEALEKAMAEATGIK---PNLDFPAG 319
PRK14034 PRK14034
citrate synthase; Provisional
130-409 4.83e-22

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 96.76  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALP-STAHPMTQFASGVMALQVQSEFQKAYEQgdiskskywEPTFEDAL 208
Cdd:PRK14034   51 RKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDlKKVHPMSVLRTAISMLGLYDEEAEIMDE---------EANYRKAV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 209 NLIARVPVVASyVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQ--MKELMRLYVTIHSDHEGgNVSAHAGHLVGSAL 286
Cdd:PRK14034  122 RLQAKVPTIVA-AFSRIRKGLDPVEPRKDLSLAANFLYMLNGEEPDevEVEAFNKALVLHADHEL-NASTFTARVCVATL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 287 SDPYLSFAAALNGLAGPLHGLANQEVLlwikLVVEECGESiskEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQRE 366
Cdd:PRK14034  200 SDVYSGITAAIGALKGPLHGGANENVM----KMLTEIGEE---ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLRE 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039016053 367 FALKhlpddpLFQLV--SKLYEVVPPILTELGKVKNPWPNVDAHS 409
Cdd:PRK14034  273 MSKR------LTVLLgeEKWYNMSIKIEEIVTKEKGLPPNVDFYS 311
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
89-419 1.14e-21

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: 96.05  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  89 LDADEGI-RFRGMSIPEcqkiLPSAESGEEplpesLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAH 167
Cdd:cd06116    22 IDGEKGIlRYRGYPIEQ----LAEQSSYLE-----VAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 168 PMTQFASGVMALQvqSEFQKAYEQGDISKSKyweptfEDALNLIARVPVVASYVYRRMYKDGSIIPlDDSLDYGANFSHM 247
Cdd:cd06116    93 PMGILISSVAALS--TFYPEAKNIGDEEQRN------KQIIRLIGKMPTIAAFAYRHRLGLPYVLP-DNDLSYTGNFLSM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 248 LGF-------DSPQMKELMRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWIKlvv 320
Cdd:cd06116   164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQ--- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 321 eECGesiSKEQLKDYVwKTLNSGKV-VPGYGHGVLRKTDPRYICQREFA---LKHLPDDPLFQLVSKLYEVVppILTELG 396
Cdd:cd06116   240 -QIG---SPKNIPDFI-ETVKQGKErLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIA--LEDEYF 312
                         330       340
                  ....*....|....*....|...
gi 1039016053 397 KVKNPWPNVDAHSGVLLNYYGLT 419
Cdd:cd06116   313 ISRKLYPNVDFYSGLIYQALGFP 335
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
130-418 3.56e-18

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


Pssm-ID: 99861 [Multi-domain]  Cd Length: 363  Bit Score: 85.43  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMALqvqsefqkayeqGDISKSKYWEPTFEDALN 209
Cdd:cd06108    49 GKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCSML------------GCLEPENEFSQQYEIAIR 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSP--QMKELMRLYVTIHSDHEgGNVSAHAGHLVGSALS 287
Cdd:cd06108   117 LLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKKPgeLEIKAMDVSLILYAEHE-FNASTFAARVTASTLS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 288 DPYLSFAAALNGLAGPLHGLANQEVLLWIklvveecgESI-SKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQRE 366
Cdd:cd06108   196 DFYSAITGAIGTLRGPLHGGANEAAMELI--------ERFkSPEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKK 267
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039016053 367 FALKHLPD--DPlfqlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGL 418
Cdd:cd06108   268 WSKKLSEEggDP------LLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGI 315
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
130-418 4.61e-18

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: 84.90  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMAL---QVQSEFQKAYEQGDIskskyweptfed 206
Cdd:cd06117    49 GKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLgcvLPEKEDHPVSGARDI------------ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 207 ALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHMLGFDSPQ--MKELMRLYVTIHSDHEGgNVSAHAGHLVGS 284
Cdd:cd06117   117 ADRLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLHGEKPSesWEKAMHISLILYAEHEF-NASTFTARVIAG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 285 ALSDPYLSFAAALNGLAGPLHGLANqEVLLWIKLVVEECGESISKeqlkdyVWKTLNSGKVVPGYGHGVLRKTDPRYICQ 364
Cdd:cd06117   196 TGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQRYESADEAEAD------IRRRVENKEVVIGFGHPVYTIADPRNQVI 268
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039016053 365 REFAlKHLPDDPLFQlvsKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYGL 418
Cdd:cd06117   269 KEVA-KQLSKEGGDM---KMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGV 318
PRK14037 PRK14037
citrate synthase; Provisional
86-418 7.03e-18

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 84.80  E-value: 7.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053  86 TSL--LDADEGI-RFRGMSIPECqkilpsAESGEEplpESLLWLLLTGKVPTKEQANALSTELAHRAAVPDYIYKAIDAL 162
Cdd:PRK14037   16 TNLtfIDGEKGIlRYRGYNIEDL------VNYGSY---EETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 163 P--STAHPMTQFASGVMAlqvqsefqkayeqgDISKSKYWEPTFED-ALNLIARVPVVASYVYRRMYKDGSIIPlDDSLD 239
Cdd:PRK14037   87 PrdSDAIGLMEAAFAALA--------------SIDKNFKWKENDKEkAISIIAKMATIVANVYRRKEGNKPRIP-EPSDS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 240 YGANFSHMLGFDSPQMKEL--MRLYVTIHSDHEGgNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVllwIK 317
Cdd:PRK14037  152 FAESFLLASFAREPTAEEIkaMDAALILYTDHEV-PASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEA---FK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 318 LVVEECGESISKEQLKDyvwKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLPDDPlfqLVSKLYEVVPPiLTELG- 396
Cdd:PRK14037  228 QFVEIGDPNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNS---EAKKYFEIAQK-LEELGi 300
                         330       340
                  ....*....|....*....|....*
gi 1039016053 397 ---KVKNPWPNVDAHSGVLlnYYGL 418
Cdd:PRK14037  301 kqfGSKGIYPNTDFYSGIV--FYAL 323
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
130-360 2.85e-16

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: 79.66  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAhPMTQFASGVMALqvqsefqkayeqGDiskskywEPTFEDALN 209
Cdd:cd06109    49 GFFPDLPELEEFRAALAAARALPDVVAALLPALAGLD-PMDALRALLALL------------PD-------SPDLATALR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 210 LIARVPVVASYVYRRMYKDGSIIPlDDSLDYGANFSHMLGFDSPQMKELMRL--YVTIHSDHeGGNVSAHAGHLVGSALS 287
Cdd:cd06109   109 LLAAAPVITAALLRLSRGKQPIAP-DPSLSHAADYLRMLTGEPPSEAHVRALdaYLVTVADH-GMNASTFTARVIASTEA 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039016053 288 DPYLSFAAALNGLAGPLHGLANQEVLLwiklVVEECGEsisKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPR 360
Cdd:cd06109   187 DLTSAVLGAIGALKGPLHGGAPGPVLD----MLDAIGT---PENAEAWLREALARGERLMGFGHRVYRVRDPR 252
PRK12351 PRK12351
methylcitrate synthase; Provisional
130-417 6.44e-14

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 72.65  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 130 GKVPTKEQANALSTELAHRAAVPDYIYKAIDALPSTAHPMTQFASGVMAL---QVQSEFQKAYEQGDIskskyweptfed 206
Cdd:PRK12351   58 GKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgclLPEKEDHNFSGARDI------------ 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 207 ALNLIARVPVVASYVYRRMYkDGSIIPL---DDSLdyGANFSHMLGFDSPQ--MKELMRLYVTIHSDHEgGNVSAHAGHL 281
Cdd:PRK12351  126 ADRLLASLGSILLYWYHYSH-NGRRIEVetdDDSI--GGHFLHLLHGKKPSesWVKAMHTSLILYAEHE-FNASTFTARV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 282 VGSALSDPYLSFAAALNGLAGPLHGLANqEVLLWIKLVVEecgesiSKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRY 361
Cdd:PRK12351  202 IAGTGSDMYSAITGAIGALRGPKHGGAN-EVAFEIQQRYD------TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRN 274
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039016053 362 ICQREFAlKHLPDDplfQLVSKLYEVVPPILTELGKVKNPWPNVDAHSGVLLNYYG 417
Cdd:PRK12351  275 KVIKEVA-KKLSKE---AGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMG 326
PRK12350 PRK12350
citrate synthase 2; Provisional
201-360 1.64e-09

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 59.21  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 201 EPTFEDALNLIARVPVVASYVYRRMYKDGSIIPLDDSLDYGANFSHML-----GFDSPQMKELMRLYVTIHSDHeGGNVS 275
Cdd:PRK12350   95 IDDLTARLDLARASVMALSAVAQSARGIGQPAVPQREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNAS 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 276 AHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLwiklVVEECGESiskEQLKDYVWKTLNSGKVVPGYGHGVLR 355
Cdd:PRK12350  174 TFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLP----MLDAVERT---GDARGWVKGALDRGERLMGFGHRVYR 246

                  ....*
gi 1039016053 356 KTDPR 360
Cdd:PRK12350  247 AEDPR 251
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
242-413 9.80e-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: 37.55  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 242 ANFSHMLGF-------DSPQMKELMRLYVTIhSDHEGGNVSAHAGHLVGSALSDPYLSFAAALNGLAGPLHGLANQ---E 311
Cdd:cd06100    11 ISFGDVLYLllkgrlpTPYEARLLEALLVAL-ADHGPATPSAHAARLTASAGPEDLQSAVAAGLLGIGDRFGGAGEgaaR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039016053 312 VLLWIklvveECGESISKEQLKDYVWKTLNSGKVVPGYGHGVLRKTDPRYICQREFALKHLPDDPLFqlvsKLYEVVPPI 391
Cdd:cd06100    90 LFKEA-----VDSGDALDAAAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPAGPHL----DYALAVEKA 160
                         170       180
                  ....*....|....*....|..
gi 1039016053 392 LTELGKVKNPWpNVDAHSGVLL 413
Cdd:cd06100   161 LTAAKGKPLPL-NVDGAIAAIL 181
 
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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