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Conserved domains on  [gi|2556165550|ref|WP_303943050|]
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citrate synthase [Enorma burkinafasonensis]

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 ...
44-471 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 PRK14032:

Pssm-ID: 469765 [Multi-domain]  Cd Length: 447  Bit Score: 688.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  44 NEALFREHNVKRGLRNANGSGVVAGLTRISDVHGYRKVDGAVVPDEGKLTIWGYDIQELVDHAQQEQRFGYEEIVFLLLT 123
Cdd:PRK14032   20 DPELYDKYDVKRGLRNEDGTGVLVGLTNIGDVHGYEIDDGEKIPDEGKLYYRGYDIKDLVNGFLKEKRFGFEEVAYLLLF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 124 GQLPRADELEALRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIA 203
Cdd:PRK14032  100 GELPTKEELAEFTELLGDYRELPDGFTRDMILKAPSKDIMNSLARSVLALYSYDDNPDDTSIDNVLRQSISLIARFPTLA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 204 AIAHTTRQAELEGRRAHIPRPVETYSMAETILQILREGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAY 283
Cdd:PRK14032  180 VYAYQAYRHYHDGKSLYIHPPKPELSTAENILYMLRPDNKYTELEARLLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTY 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 284 SAYAAAIGSLKGPRHGGANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNREAFDGAGLIYGMGHAVYTLSDPRAQLCR 363
Cdd:PRK14032  260 SAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNKEAFDKSGLIYGMGHAVYTISDPRAVILK 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 364 RYARSLAEQKGLGDEFALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRME 443
Cdd:PRK14032  340 KFAEKLAKEKGREEEFNLYEKIEKLAPELIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIE 419
                         410       420
                  ....*....|....*....|....*...
gi 2556165550 444 ELYGANRIIRPAYNSVMEDVTYVPLAER 471
Cdd:PRK14032  420 ELVNGGKIIRPAYKSVLERREYVPLEER 447
 
Name Accession Description Interval E-value
PRK14032 PRK14032
citrate synthase; Provisional
44-471 0e+00

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 688.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  44 NEALFREHNVKRGLRNANGSGVVAGLTRISDVHGYRKVDGAVVPDEGKLTIWGYDIQELVDHAQQEQRFGYEEIVFLLLT 123
Cdd:PRK14032   20 DPELYDKYDVKRGLRNEDGTGVLVGLTNIGDVHGYEIDDGEKIPDEGKLYYRGYDIKDLVNGFLKEKRFGFEEVAYLLLF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 124 GQLPRADELEALRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIA 203
Cdd:PRK14032  100 GELPTKEELAEFTELLGDYRELPDGFTRDMILKAPSKDIMNSLARSVLALYSYDDNPDDTSIDNVLRQSISLIARFPTLA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 204 AIAHTTRQAELEGRRAHIPRPVETYSMAETILQILREGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAY 283
Cdd:PRK14032  180 VYAYQAYRHYHDGKSLYIHPPKPELSTAENILYMLRPDNKYTELEARLLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTY 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 284 SAYAAAIGSLKGPRHGGANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNREAFDGAGLIYGMGHAVYTLSDPRAQLCR 363
Cdd:PRK14032  260 SAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNKEAFDKSGLIYGMGHAVYTISDPRAVILK 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 364 RYARSLAEQKGLGDEFALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRME 443
Cdd:PRK14032  340 KFAEKLAKEKGREEEFNLYEKIEKLAPELIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIE 419
                         410       420
                  ....*....|....*....|....*...
gi 2556165550 444 ELYGANRIIRPAYNSVMEDVTYVPLAER 471
Cdd:PRK14032  420 ELVNGGKIIRPAYKSVLERREYVPLEER 447
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
55-460 0e+00

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: 643.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  55 RGLRNANGSGVVAGLTRISDVHGYRKVDGAVVPDEGKLTIWGYDIQELVDHAQQEQRFGYEEIVFLLLTGQLPRADELEA 134
Cdd:cd06113     1 RGLRNEDGTGVLAGLTNISDVVGYKIIDGEKVPCPGKLYYRGYDVEDLVNGAQKENRFGFEETAYLLLFGYLPNKEELEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 135 LRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQAEL 214
Cdd:cd06113    81 FCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQRSVLALYSYDDKPDDISLENVLRQSIQLIARLPTIAVYAYQAKRHYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 215 EGRRAHIPRPVETYSMAETILQILREGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:cd06113   161 DGESLYIHHPQPELSTAENILSMLRPDKKYTELEAKLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:cd06113   241 GPRHGGANIKVMEMLEDIKENVKDWTDEDEVRAYLRKILNKEAFDKSGLIYGMGHAVYTLSDPRAVVLKKYARSLAKEKG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGANRIIRP 454
Cdd:cd06113   321 REEEFALYERIERLAPEVIAEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRP 400

                  ....*.
gi 2556165550 455 AYNSVM 460
Cdd:cd06113   401 AYKYVG 406
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
52-471 8.62e-147

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: 424.51  E-value: 8.62e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  52 NVKRGLRnangsGVVAGLTRISDVhgyrkvDGavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQLPRADE 131
Cdd:COG0372    12 TVDPGLE-----GVVAGETAISYI------DG----EKGILRYRGYPIEDLAEKS------SFEEVAYLLLYGELPTKEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 132 LEALRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQ 211
Cdd:COG0372    71 LAEFKAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDIDPEARLEKAIRLIAKLPTIAAYAYRYRR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 212 aeleGRRAHIPRPveTYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHgGGNNSTFACRVLSSSATDAYSAYAAAIG 291
Cdd:COG0372   151 ----GLPPVYPDP--DLSYAENFLYMLF-GEEPDPEEARALDLLLILHADH-EQNASTFTARVVASTLADLYSAIAAAIG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 292 SLKGPRHGGANSKVMAMHEDIRahvrrwdDDGEVAGYLMKILNReafdgAGLIYGMGHAVYTLSDPRAQLCRRYARSLAE 371
Cdd:COG0372   223 ALKGPLHGGANEAVLEMLEEIG-------SPDNVEEYIRKALDK-----KERIMGFGHRVYKNYDPRAKILKEAAEELLE 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 372 QKGLGDEFALIERIERLAPqvmREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRI 451
Cdd:COG0372   291 ELGDDPLLEIAEELEEVAL---EDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQ-RADNRI 366
                         410       420
                  ....*....|....*....|.
gi 2556165550 452 IRPAYNSVME-DVTYVPLAER 471
Cdd:COG0372   367 IRPRQIYVGPeDRDYVPIEER 387
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
56-455 5.12e-128

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: 375.31  E-value: 5.12e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  56 GLRnangsGVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHaqqeqrFGYEEIVFLLLTGQLPRADELEAL 135
Cdd:pfam00285   1 GLR-----GVAAGETEISYIDG----------EKGILRYRGYDIEELAER------SSFEEVAYLLLTGELPTKEELEEF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 136 RARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVA-LSLLARLPRIAAIAHTTRQael 214
Cdd:pfam00285  60 SAELAAHRELPEDVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALrDDLIAKLPTIAAYIYRHRR--- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 215 eGRRAHIPRPVETYsmAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:pfam00285 137 -GLPPIYPDPDLSY--AENFLYMLF-GYEPDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALK 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLMKILNReafdGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:pfam00285 212 GPLHGGANEAVLEMLEEI-------GSPDEVEEYIRKVLNK----GKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIERLAPQVMREERgttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:pfam00285 281 DDPLLELAEELEEVAPEDLYFVE---KNLYPNVDFYSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQ-LADNRIIRP 356

                  .
gi 2556165550 455 A 455
Cdd:pfam00285 357 R 357
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
63-471 2.82e-90

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


Pssm-ID: 130859  Cd Length: 368  Bit Score: 279.25  E-value: 2.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRISdvhgyrKVDGavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGL 142
Cdd:TIGR01800   4 EGVIAGETALS------TIDG----SGGILTYRGYDIEDLAEHAS------FEEVAYLLLHGKLPTRSELRKFKTELAKL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 143 RLLPTDYI---HEFPMTTASksiMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRqaelEGRRA 219
Cdd:TIGR01800  68 RGLPDEVIeliEALPAESHP---MDVLRTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIR----HGGEI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 220 HIPRpvETYSMAETILQILrEGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHG 299
Cdd:TIGR01800 141 IAPK--DDDSIAGNFLYML-HGEEPTKEWEKAMDIALILYAEHEF-NASTFAARVIASTLSDMYSAITAAIGALKGPLHG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 300 GANSKVMAMhedirahVRRWDDDGEVAGYLMKIL-NREAfdgaglIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDE 378
Cdd:TIGR01800 217 GANEAVMAM-------LDEIGDPDKAEAWIRKALeNKER------IMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKW 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 379 FALIERIERlapqVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP--AY 456
Cdd:TIGR01800 284 YEIAERLED----VMEEEKG----IYPNVDFFSASVYYMMGIPTDLFTPIFAMSRVTGWTAHIIEQ-VENNRLIRPraDY 354
                         410
                  ....*....|....*
gi 2556165550 457 NSVmEDVTYVPLAER 471
Cdd:TIGR01800 355 VGP-EERKYVPIEER 368
 
Name Accession Description Interval E-value
PRK14032 PRK14032
citrate synthase; Provisional
44-471 0e+00

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 688.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  44 NEALFREHNVKRGLRNANGSGVVAGLTRISDVHGYRKVDGAVVPDEGKLTIWGYDIQELVDHAQQEQRFGYEEIVFLLLT 123
Cdd:PRK14032   20 DPELYDKYDVKRGLRNEDGTGVLVGLTNIGDVHGYEIDDGEKIPDEGKLYYRGYDIKDLVNGFLKEKRFGFEEVAYLLLF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 124 GQLPRADELEALRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIA 203
Cdd:PRK14032  100 GELPTKEELAEFTELLGDYRELPDGFTRDMILKAPSKDIMNSLARSVLALYSYDDNPDDTSIDNVLRQSISLIARFPTLA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 204 AIAHTTRQAELEGRRAHIPRPVETYSMAETILQILREGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAY 283
Cdd:PRK14032  180 VYAYQAYRHYHDGKSLYIHPPKPELSTAENILYMLRPDNKYTELEARLLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTY 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 284 SAYAAAIGSLKGPRHGGANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNREAFDGAGLIYGMGHAVYTLSDPRAQLCR 363
Cdd:PRK14032  260 SAIAAAIGSLKGPKHGGANIKVMEMFEDIKENVKDWEDEDEIADYLTKILNKEAFDKSGLIYGMGHAVYTISDPRAVILK 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 364 RYARSLAEQKGLGDEFALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRME 443
Cdd:PRK14032  340 KFAEKLAKEKGREEEFNLYEKIEKLAPELIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIE 419
                         410       420
                  ....*....|....*....|....*...
gi 2556165550 444 ELYGANRIIRPAYNSVMEDVTYVPLAER 471
Cdd:PRK14032  420 ELVNGGKIIRPAYKSVLERREYVPLEER 447
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
55-460 0e+00

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: 643.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  55 RGLRNANGSGVVAGLTRISDVHGYRKVDGAVVPDEGKLTIWGYDIQELVDHAQQEQRFGYEEIVFLLLTGQLPRADELEA 134
Cdd:cd06113     1 RGLRNEDGTGVLAGLTNISDVVGYKIIDGEKVPCPGKLYYRGYDVEDLVNGAQKENRFGFEETAYLLLFGYLPNKEELEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 135 LRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQAEL 214
Cdd:cd06113    81 FCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQRSVLALYSYDDKPDDISLENVLRQSIQLIARLPTIAVYAYQAKRHYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 215 EGRRAHIPRPVETYSMAETILQILREGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:cd06113   161 DGESLYIHHPQPELSTAENILSMLRPDKKYTELEAKLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:cd06113   241 GPRHGGANIKVMEMLEDIKENVKDWTDEDEVRAYLRKILNKEAFDKSGLIYGMGHAVYTLSDPRAVVLKKYARSLAKEKG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGANRIIRP 454
Cdd:cd06113   321 REEEFALYERIERLAPEVIAEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRP 400

                  ....*.
gi 2556165550 455 AYNSVM 460
Cdd:cd06113   401 AYKYVG 406
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
52-471 8.62e-147

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: 424.51  E-value: 8.62e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  52 NVKRGLRnangsGVVAGLTRISDVhgyrkvDGavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQLPRADE 131
Cdd:COG0372    12 TVDPGLE-----GVVAGETAISYI------DG----EKGILRYRGYPIEDLAEKS------SFEEVAYLLLYGELPTKEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 132 LEALRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQ 211
Cdd:COG0372    71 LAEFKAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDIDPEARLEKAIRLIAKLPTIAAYAYRYRR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 212 aeleGRRAHIPRPveTYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHgGGNNSTFACRVLSSSATDAYSAYAAAIG 291
Cdd:COG0372   151 ----GLPPVYPDP--DLSYAENFLYMLF-GEEPDPEEARALDLLLILHADH-EQNASTFTARVVASTLADLYSAIAAAIG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 292 SLKGPRHGGANSKVMAMHEDIRahvrrwdDDGEVAGYLMKILNReafdgAGLIYGMGHAVYTLSDPRAQLCRRYARSLAE 371
Cdd:COG0372   223 ALKGPLHGGANEAVLEMLEEIG-------SPDNVEEYIRKALDK-----KERIMGFGHRVYKNYDPRAKILKEAAEELLE 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 372 QKGLGDEFALIERIERLAPqvmREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRI 451
Cdd:COG0372   291 ELGDDPLLEIAEELEEVAL---EDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQ-RADNRI 366
                         410       420
                  ....*....|....*....|.
gi 2556165550 452 IRPAYNSVME-DVTYVPLAER 471
Cdd:COG0372   367 IRPRQIYVGPeDRDYVPIEER 387
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
56-455 5.12e-128

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: 375.31  E-value: 5.12e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  56 GLRnangsGVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHaqqeqrFGYEEIVFLLLTGQLPRADELEAL 135
Cdd:pfam00285   1 GLR-----GVAAGETEISYIDG----------EKGILRYRGYDIEELAER------SSFEEVAYLLLTGELPTKEELEEF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 136 RARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVA-LSLLARLPRIAAIAHTTRQael 214
Cdd:pfam00285  60 SAELAAHRELPEDVLELLRALPRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALrDDLIAKLPTIAAYIYRHRR--- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 215 eGRRAHIPRPVETYsmAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:pfam00285 137 -GLPPIYPDPDLSY--AENFLYMLF-GYEPDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALK 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLMKILNReafdGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:pfam00285 212 GPLHGGANEAVLEMLEEI-------GSPDEVEEYIRKVLNK----GKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIERLAPQVMREERgttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:pfam00285 281 DDPLLELAEELEEVAPEDLYFVE---KNLYPNVDFYSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQ-LADNRIIRP 356

                  .
gi 2556165550 455 A 455
Cdd:pfam00285 357 R 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
64-458 6.44e-101

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: 306.07  E-value: 6.44e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQLPRADELEALRARIGGLR 143
Cdd:cd06118     5 GVKAKETSISYIDG----------DEGILRYRGYDIEELAEKS------SFEEVAYLLLYGKLPTKEELAEFKKKLASHR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 144 LLP---TDYIHEFPMTTASksiMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAA-IAHTTRqaeleGRRA 219
Cdd:cd06118    69 ALPehvVEILDLLPKNAHP---MDVLRTAVSALGSFDPFARDKSPEARYEKAIRLIAKLPTIAAnIYRNRE-----GLEI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 220 HIPRPVETYsmAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHG 299
Cdd:cd06118   141 IAPDPDLSY--AENFLYMLF-GEEPDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 300 GANSKVMAMHEDI--RAHVRRWDDDgevagylmKILNREafdgagLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGD 377
Cdd:cd06118   217 GANEAVLKMLLEIgtPENVEAYIWK--------KLANKR------RIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDK 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 378 EFALIERIERLAPQVMREergttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGANRIIRPAYN 457
Cdd:cd06118   283 LFEIAEELEEIALEVLGE-----KGIYPNVDFYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAE 357

                  .
gi 2556165550 458 S 458
Cdd:cd06118   358 Y 358
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
55-454 1.95e-91

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: 281.86  E-value: 1.95e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  55 RGLRnangsGVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEA 134
Cdd:cd06110     1 KGLE-----GVIAADSKISYIDG----------DAGILIYRGYDIHDLAENST------FEEVAYLLWNGELPTAEELDA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 135 LRARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQael 214
Cdd:cd06110    60 FKAQLAAERELPAEIIDLLKLLPKDAHPMDVLRTAVSALALYDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRN--- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 215 eGRRAHIPRPveTYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:cd06110   137 -GLEPVAPDP--DLSHAANFLYMLT-GEKPSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALK 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLmkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:cd06110   212 GPLHGGANERVMKMLLEI-------GSVDNVAAYV-----KDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETG 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIErlapQVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:cd06110   280 EPKWYEMSEAIE----QAMRDEKG----LNPNVDFYSASVYYMLGIPVDLFTPIFAISRVSGWCAHILEQ-YFNNRLIRP 350
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
63-471 2.82e-90

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


Pssm-ID: 130859  Cd Length: 368  Bit Score: 279.25  E-value: 2.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRISdvhgyrKVDGavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGL 142
Cdd:TIGR01800   4 EGVIAGETALS------TIDG----SGGILTYRGYDIEDLAEHAS------FEEVAYLLLHGKLPTRSELRKFKTELAKL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 143 RLLPTDYI---HEFPMTTASksiMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRqaelEGRRA 219
Cdd:TIGR01800  68 RGLPDEVIeliEALPAESHP---MDVLRTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIR----HGGEI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 220 HIPRpvETYSMAETILQILrEGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHG 299
Cdd:TIGR01800 141 IAPK--DDDSIAGNFLYML-HGEEPTKEWEKAMDIALILYAEHEF-NASTFAARVIASTLSDMYSAITAAIGALKGPLHG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 300 GANSKVMAMhedirahVRRWDDDGEVAGYLMKIL-NREAfdgaglIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDE 378
Cdd:TIGR01800 217 GANEAVMAM-------LDEIGDPDKAEAWIRKALeNKER------IMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKW 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 379 FALIERIERlapqVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP--AY 456
Cdd:TIGR01800 284 YEIAERLED----VMEEEKG----IYPNVDFFSASVYYMMGIPTDLFTPIFAMSRVTGWTAHIIEQ-VENNRLIRPraDY 354
                         410
                  ....*....|....*
gi 2556165550 457 NSVmEDVTYVPLAER 471
Cdd:TIGR01800 355 VGP-EERKYVPIEER 368
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
64-468 1.67e-73

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: 236.17  E-value: 1.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISDVHGYRkvdgavvpdeGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGLR 143
Cdd:cd06112     7 GVPAAESSISYIDGKN----------GILEYRGYDIEELAEYSS------FEEVALLLLDGDLPTAAELEEFDKELRQHR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 144 LLP---TDYIHEFPMTTaskSIMNVLARAVLLLYAF--DETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRqaelEGRR 218
Cdd:cd06112    71 RVKyniRDMMKCFPETG---HPMDMLQATVAALGMFypKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIR----NGDD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 219 AHIPRPVETYsmAETILQIL--REGDDFTrdeAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGP 296
Cdd:cd06112   144 PIEPRPDLDY--AENFLYMLfgEEPDPAT---AKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGP 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 297 RHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLMKILNREAfdgagLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLG 376
Cdd:cd06112   218 LHGGANEDVLEMLEEI-------GSPENVKAYLDKKLANKQ-----KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGEL 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 377 DE-FALIERIERLApqvmrEERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELyGANRIIRPA 455
Cdd:cd06112   286 SKlYEIALEVERLC-----EELLGHKGVYPNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQL-GDNRIFRPT 359
                         410
                  ....*....|....
gi 2556165550 456 YNSVME-DVTYVPL 468
Cdd:cd06112   360 QIYIGEiDRKYVPL 373
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
63-468 7.53e-72

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: 231.43  E-value: 7.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRISdvhgyrkvdgaVVPDEGK-LTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGG 141
Cdd:cd06108     4 AGVVAGQTAIS-----------TVGKGGKgLTYRGYDIEDLAENAT------FEEVAYLLLYGKLPTRKQLDAYKTKLVA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 142 LRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDEtpdDTSPNHEVDVALSLLARLPRIAAIAHttrqaelegRRAHI 221
Cdd:cd06108    67 LRRLPAALKTVLELIPKDSHPMDVMRTGCSMLGCLEP---ENEFSQQYEIAIRLLAIFPSILLYWY---------HYSHS 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 222 PRPVETYSMAETI----LQIL---REGDDFTRdeAMllDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLK 294
Cdd:cd06108   135 GKRIETETDEDSIaghfLHLLhgkKPGELEIK--AM--DVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLR 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 295 GPRHGGANSKVMAMHEDIRAhvrrwDDDGEvAGYLMKILNREafdgagLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKG 374
Cdd:cd06108   210 GPLHGGANEAAMELIERFKS-----PEEAE-QGLLEKLERKE------LIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 375 LGDEFALIERIErlapQVMREErgttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:cd06108   278 DPLLYQISERIE----EVMWEE----KKLFPNLDFYSASAYHFCGIPTELFTPIFVMSRVTGWAAHIMEQ-RANNRLIRP 348
                         410
                  ....*....|....*
gi 2556165550 455 AYNSV-MEDVTYVPL 468
Cdd:cd06108   349 SADYIgPEPRPFVPI 363
PRK14036 PRK14036
citrate synthase; Provisional
64-471 7.23e-71

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 229.46  E-value: 7.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGLR 143
Cdd:PRK14036   10 GVPATQSSISYVDG----------QKGILEYRGYPIEELAEKSS------FLETAYLLIWGELPTAEELEEFEQEVRMHR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 144 LLP---TDYIHEFPmttASKSIMNVL---ARAVLLLYAFDETPDdtsPNHEVDVALSLLARLPRIAAIAHTTRQaeleGR 217
Cdd:PRK14036   74 RVKyriRDMMKCFP---ETGHPMDALqasAAALGLFYSRRALDD---PEYIRDAVVRLIAKIPTMVAAFQLIRK----GN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 218 RAHIPRPVETYsmAETILQIL--REGDDFtrdEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKG 295
Cdd:PRK14036  144 DPIQPRDDLDY--AANFLYMLteREPDPL---AARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 296 PRHGGANSKVMAMHEDIRA--HVRRWDDDgevagylmKILNREAfdgaglIYGMGHAVYTLSDPRAQLCRRYARSLAEQK 373
Cdd:PRK14036  218 PLHGGANEDVLAMLEEIGSveNVRPYLDE--------RLANKQK------IMGFGHREYKVKDPRATILQKLAEELFARF 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 374 GLGDEFALIERIERLApqvmrEERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELyGANRIIR 453
Cdd:PRK14036  284 GHDEYYEIALELERVA-----EERLGPKGIYPNVDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQL-GANRIFR 357
                         410       420
                  ....*....|....*....|
gi 2556165550 454 PA--YNSVmEDVTYVPLAER 471
Cdd:PRK14036  358 PTqiYTGS-HNRRYIPLEER 376
PRK14035 PRK14035
citrate synthase; Provisional
54-471 1.37e-68

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 223.48  E-value: 1.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  54 KRGLRnangsGVVAGLTRISdvhgyrkvdgAVVPDegKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELE 133
Cdd:PRK14035    4 QRGLE-----GVIAAETKIS----------SIIDS--QLTYAGYDIDDLAENAS------FEEVIFLLWNYRLPTEEELA 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 134 ALRARI-GGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQa 212
Cdd:PRK14035   61 HLKGKLrKYMTLNDRVYQHFEEYSTDHVHPMTALRTSVSYLAHFDPDAEEESDEARYERAIRIQAKVASLVTAFARVRQ- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 213 eleGRRAHIPRPVETYsmAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGS 292
Cdd:PRK14035  140 ---GKEPLKPRPDLSY--AANFLYMLR-GELPTDIEVEAFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGS 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 293 LKGPRHGGANSKVMAMHEDIRahvrrwdDDGEVAGYLmkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQ 372
Cdd:PRK14035  213 LKGPLHGGANERVMDMLSEIR-------SIGDVDAYL-----DEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 373 KGLGDEFALIERIERLapqvMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRII 452
Cdd:PRK14035  281 TGREELFEMSVKIEKR----MKEEKG----LIPNVDFYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQ-YKDNRIM 351
                         410       420
                  ....*....|....*....|
gi 2556165550 453 RPAYNSV-MEDVTYVPLAER 471
Cdd:PRK14035  352 RPRAKYIgETNRKYIPIEER 371
PRK12351 PRK12351
methylcitrate synthase; Provisional
63-471 4.54e-68

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 222.11  E-value: 4.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRISDVhgyrkvdgavvpdeGK----LTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRAR 138
Cdd:PRK12351   13 SGVVAGNTALCTV--------------GKsgndLHYRGYDILDLAEHCE------FEEVAHLLVHGKLPTQAELAAYKTK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 139 IGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHttrqaelegRR 218
Cdd:PRK12351   73 LKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEDHNFSGARDIADRLLASLGSILLYWY---------HY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 219 AHIPRPVETYSMAETI----LQIL---REGDDFTRdeAMllDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIG 291
Cdd:PRK12351  144 SHNGRRIEVETDDDSIgghfLHLLhgkKPSESWVK--AM--HTSLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 292 SLKGPRHGGANSKVMAMHEdirahvrRWD--DDGEvAGYLMKILNREafdgagLIYGMGHAVYTLSDPRAQLCRRYARSL 369
Cdd:PRK12351  219 ALRGPKHGGANEVAFEIQQ-------RYDtpDEAE-ADIRRRVENKE------VVIGFGHPVYTISDPRNKVIKEVAKKL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 370 AEQKGLGDEFALIERIErlapQVMREErgttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGaN 449
Cdd:PRK12351  285 SKEAGDTKLYDIAERLE----TVMWEE----KKMFPNLDWFSAVSYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQD-N 355
                         410       420
                  ....*....|....*....|...
gi 2556165550 450 RIIRPAYNSV-MEDVTYVPLAER 471
Cdd:PRK12351  356 KIIRPSANYTgPEDRKFVPIEKR 378
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
50-461 5.98e-67

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 219.05  E-value: 5.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  50 EHNVKRGLrnangSGVVAGLTRISDVhgyrkvdgavVPDEGKLTIWGYDIQELVDHaqqeQRFgyEEIVFLLLTGQLPRA 129
Cdd:PRK14033    6 TPEIKKGL-----AGVVVDTTAISKV----------VPETNSLTYRGYPVQDLAAR----CSF--EEVAYLLWNGELPTD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 130 DELEALRARIGGLRLLPT---DYIHEFPMTTASksiMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIA 206
Cdd:PRK14033   65 AELALFSQRERAYRRLDRsvlSLIDKLPTTCHP---MDVVRTAVSYLGAEDPEADDSSPEANLAKALRLFAVLPTIVAAD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 207 HTTRQaeleGRRAHIPRPVETYsmAETILQI-LREGDDFTRDEAMllDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSA 285
Cdd:PRK14033  142 QRRRR----GLDPIAPRSDLGY--AENFLHMcFGEVPEPEVVRAF--EVSLILYAEHSF-NASTFTARVITSTLSDIYSA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 286 YAAAIGSLKGPRHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLmkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRY 365
Cdd:PRK14033  213 VTGAIGALKGPLHGGANEAVMHTMLEI-------GDPARAAEWL-----RDALARKEKVMGFGHRVYKHGDSRVPTMKAA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 366 ARSLAEQKGLGDEFALIERIERlapqVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEEl 445
Cdd:PRK14033  281 LRRVAAVRDGQRWLDIYEALEK----AMAEATG----IKPNLDFPAGPAYYLMGFDIDFFTPIFVMSRITGWTAHIMEQ- 351
                         410
                  ....*....|....*...
gi 2556165550 446 YGANRIIRP--AYNSVME 461
Cdd:PRK14033  352 RASNALIRPlsEYNGPEQ 369
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
63-458 2.79e-66

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: 213.71  E-value: 2.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPradelealrariggl 142
Cdd:cd06101     4 RGVAALESEISVIDG----------DEGGLRYRGYPIEELAENSS------FEEVAYLLLTGELP--------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 143 rllptDYIHEFpmttasksimnvlaravlLLYAFDETPDDtspnhevdvalsllarlpriaaiahttrqaelegrrahip 222
Cdd:cd06101    53 -----SYAENF------------------LYMLGGEEPDP---------------------------------------- 69
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 223 rpvetysmaetilqilregddftrDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGAN 302
Cdd:cd06101    70 ------------------------EFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGAN 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 303 SKVMAMHEDIRAHVrrwdddgevAGYLMKILNREAFDGaGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDEFALI 382
Cdd:cd06101   125 EAVLKMLEEIGTPK---------NEPAEAYIRKKLNSK-RVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELA 194
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2556165550 383 ERIERLAPQVMREergttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGANRIIRPAYNS 458
Cdd:cd06101   195 AELEKIAPEVLYE-----KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
64-459 4.28e-66

Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-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). 2-methylcitrate synthase (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: 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. DsCS, compared with CS from the hyperthermophile Pyrococcus furiosus (not included in this group), has an increase in the size of surface loops, a higher proline content in the loop regions, a more accessible active site, and a higher number of intramolecular ion pairs. 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. For example, included in this group are Corynebacterium glutamicum (Cg) PrpC1 and -2, which are only synthesized during growth on propionate-containing medium, can use PrCoA, AcCoA and butyryl-CoA as substrates, and have comparable catalytic activity with AcCoA as the major CgCS (GltA, not included in this group).


Pssm-ID: 99864 [Multi-domain]  Cd Length: 362  Bit Score: 216.51  E-value: 4.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISdvhgyrkvdgAVVPDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGLR 143
Cdd:cd06111     5 GVVADTTAIS----------KVMPETNSLTYRGYPVQDLAENCS------FEEVAYLLWNGELPNAAQLAEFSQRERSYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 144 LLPT---DYIHEFPMTTASksiMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQAElegrrAH 220
Cdd:cd06111    69 RLDRnllSLIASLPKNCHP---MDVLRTAVSVLGAEDSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGL-----DP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 221 IPrPVETYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGG 300
Cdd:cd06111   141 IP-PDSDLGIAENFLHMCF-GEVPSPEVVRAFDVSLILYAEHSF-NASTFTARVITSTLSDIYSAITGAIGALKGPLHGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 301 ANSKVMAMHEDIrahvrrwdDDGEVAGYLMkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDEFA 380
Cdd:cd06111   218 ANEAVMHMMLEI--------DDPEKAAQWM----LDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLA 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 381 LIERIErlapQVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP--AYNS 458
Cdd:cd06111   286 MYDALE----DAMVAAKG----IKPNLDFPAGPAYYLMGFDIDFFTPIFVMARITGWTAHIMEQ-RADNALIRPlsEYNG 356

                  .
gi 2556165550 459 V 459
Cdd:cd06111   357 P 357
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
229-458 8.24e-66

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


Pssm-ID: 99853 [Multi-domain]  Cd Length: 213  Bit Score: 210.66  E-value: 8.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 229 SMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKVMAM 308
Cdd:cd06099     1 SYAENFLYMLG-GEEPDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 309 HEDIRAHVRRwdddgevagYLMKILNREAFDGaGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDEFALIERIERL 388
Cdd:cd06099    79 LEEIGTPKNE---------PAEAYIRKKLESK-RVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKI 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 389 APQVMREergttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGANRIIRPAYNS 458
Cdd:cd06099   149 AEEVLYE-----KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
PRK12349 PRK12349
citrate synthase;
64-454 6.52e-60

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 200.72  E-value: 6.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRIS--DVhgyrkvdgavvpDEGKLTIWGYDIQELvdhaqqEQRFGYEEIVFLLLTGQLPRADELEALRARIGG 141
Cdd:PRK12349   11 GVIAAETKISflDT------------VKGEIVIQGYDLIEL------SKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 142 LRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTrqaeLEGRRAhI 221
Cdd:PRK12349   73 EYAVPEGVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSRAYKLLSKVPNIVANSYHI----LNNEEP-I 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 222 PrPVETYSMAETILQILrEGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGA 301
Cdd:PRK12349  148 E-PLKELSYSANFLYML-TGKKPTELEEKIFDRSLVLYSEHEM-PNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 302 NSKVMAMHEDIrahvrrwdddGEVAGYLM----KILNREAfdgaglIYGMGHAVYTLS-DPRAQLCRRYARSLAEQKGlg 376
Cdd:PRK12349  225 NEAVMYMLLEA----------GTVEKFEEllqkKLYNKEK------IMGFGHRVYMKKmDPRALMMKEALKQLCDVKG-- 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2556165550 377 dEFALIERIERlAPQVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:PRK12349  287 -DYTLYEMCEA-GEKIMEKEKG----LYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQ-HANNRLFRP 357
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
64-455 1.49e-59

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: 199.07  E-value: 1.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQLPRADELEALRARIGGLR 143
Cdd:cd06109     5 GVVAAETVLSDVDG----------EAGRLIIRGYSVEDLAGSA------SFEDVAALLWNGFFPDLPELEEFRAALAAAR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 144 LLPtDYIHEFPMTTASKSIMNVLARAVLLLyafdetpddtSPNHEVDVALSLLARLPRIAAIAHttRQAEleGRRAHIPR 223
Cdd:cd06109    69 ALP-DVVAALLPALAGLDPMDALRALLALL----------PDSPDLATALRLLAAAPVITAALL--RLSR--GKQPIAPD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 224 PveTYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANS 303
Cdd:cd06109   134 P--SLSHAADYLRMLT-GEPPSEAHVRALDAYLVTVADHGM-NASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 304 KVMAMHEDIRAHvrrwdddGEVAGYLmkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAeqkGLGDEFALIE 383
Cdd:cd06109   210 PVLDMLDAIGTP-------ENAEAWL-----REALARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAE 274
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2556165550 384 RIERLAPQVMREERgTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELyGANRIIRPA 455
Cdd:cd06109   275 AVEQAALALLREYK-PGRPLETNVEFYTALLLEALGLPREAFTPTFAAGRTAGWTAHVLEQA-RTGRLIRPQ 344
PRK14034 PRK14034
citrate synthase; Provisional
53-471 5.94e-58

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 195.37  E-value: 5.94e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  53 VKRGLRnangsGVVAGLTRISdvhgyrkvdgAVVPDEgkLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADEL 132
Cdd:PRK14034    3 VTRGLE-----GVVATTSSVS----------SIIDDT--LTYVGYNIDDLAENAS------FEEVVYLLWHRKLPNKQEL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 133 EALRARIGGLRLLPTDYIHEFPMTTASK-SIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRq 211
Cdd:PRK14034   60 AEFKEQLSENAKVPGEIIEHLKQYDLKKvHPMSVLRTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIR- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 212 aelEGRRAHIPRpvETYSMAETILQIL--REGDDfTRDEAMllDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAA 289
Cdd:PRK14034  139 ---KGLDPVEPR--KDLSLAANFLYMLngEEPDE-VEVEAF--NKALVLHADHEL-NASTFTARVCVATLSDVYSGITAA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 290 IGSLKGPRHGGANSKVMAMHEDIrahvrrwDDDGEVAGYLmkilnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSL 369
Cdd:PRK14034  210 IGALKGPLHGGANENVMKMLTEI-------GEEENVESYI-----HNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRL 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 370 AEQKGLGDEFALIERIErlapQVMREERGttkpICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGAN 449
Cdd:PRK14034  278 TVLLGEEKWYNMSIKIE----EIVTKEKG----LPPNVDFYSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQ-YENN 348
                         410       420
                  ....*....|....*....|...
gi 2556165550 450 RIIRPAYNSVMEDV-TYVPLAER 471
Cdd:PRK14034  349 RLIRPRADYVGPTHqVYVPIEER 371
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
63-468 9.12e-56

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: 189.67  E-value: 9.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  63 SGVVAGLTRI-------SDVHgYRkvdgavvpdegkltiwGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEAL 135
Cdd:cd06117     4 SGVAAGNTALctvgrsgNDLH-YR----------------GYDILDLAEKCE------FEEVAHLLVHGKLPTKSELAAY 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 136 RARIGGLRLLPTDYIHEFPMTTASKSIMNVLARAVLLLYAFDETPDDTSPNHEVDVALSLLARLPRIAA----IAHTTRQ 211
Cdd:cd06117    61 KTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGARDIADRLMASLGSILLywyhYSHNGKR 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 212 AELEgrrahiprpVETYSMAETILQILrEGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIG 291
Cdd:cd06117   141 IEVE---------TDDDSIGGHFLHLL-HGEKPSESWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 292 SLKGPRHGGANSKVMAMHEdirahvrRWDDDGEV-AGYLMKILNREafdgagLIYGMGHAVYTLSDPRAQLCRRYARSLA 370
Cdd:cd06117   210 ALRGPKHGGANEVAFEIQQ-------RYESADEAeADIRRRVENKE------VVIGFGHPVYTIADPRNQVIKEVAKQLS 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 371 EQKGLGDEFALIERIErlapQVMREErgttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELYGaNR 450
Cdd:cd06117   277 KEGGDMKMFDIAERLE----TVMWEE----KKMFPNLDWFSAVSYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQD-GK 347
                         410
                  ....*....|....*....
gi 2556165550 451 IIRPAYNSV-MEDVTYVPL 468
Cdd:cd06117   348 IIRPSANYTgPEDLKFVPI 366
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
88-454 7.23e-51

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: 177.24  E-value: 7.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  88 DEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGLRLLP---TDYIHEFPMTTASKSIMN 164
Cdd:cd06107    25 DKGILLYRGYPIEQLAESST------YEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPesvHRLIQTFPRDAHPMGILC 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 165 VLARAVLLLY-----AFDETPDDTSPNHEVDVALSLLARLPRIAAIAHTTRQaeleGRRAHIPRPVETYsmAETILQILR 239
Cdd:cd06107    99 AGLSALSAFYpeaipAHTGDLYQNNPEVRDKQIIRTLAKMPTIAAAAYCHRI----GRPFVYPRANLSY--IENFLYMMG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 240 EGDDFTRD----EAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKVMAMHEDIrah 315
Cdd:cd06107   173 YVDQEPYEpnprLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREI--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 316 vrrwdddGEVAGYLMKIlnREAFDGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDEFALIERIERLApqvMRE 395
Cdd:cd06107   249 -------GTPENVPAFI--ERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIA---LED 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 396 ERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEEL-YGANRIIRP 454
Cdd:cd06107   317 EYFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMeDPLQRIWRP 376
PLN02456 PLN02456
citrate synthase
69-471 1.80e-50

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 177.91  E-value: 1.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  69 LTRISDVHGYRKVDG-----AVV--------PDEGKLTIWGYDIQELvdhaqqEQRFGYEEIVFLLLTGQLPRADELEAL 135
Cdd:PLN02456   52 IKAGKDDLGLKTVDPgyrntAPVlseislidGDEGILRFRGYPIEEL------AEKSPFEEVAYLLLYGNLPTKEQLADW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 136 RARIGGLRLLPT---DYIHEFPMTTASksiMNVLARAVLLLYAFDETP------DDTSPNHEV--DVALSLLARLPRIAA 204
Cdd:PLN02456  126 EAELRQHSAVPEhvlDVIDALPHDAHP---MTQLVSGVMALSTFSPDAnaylrgQHKYKSWEVrdEDIVRLIGKLPTLAA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 205 IAHTTrqaeLEGRRAHIPRPVETYsmAETILQIL-REGDDFTRDE---AMLLDVMLMLHAEHgGGNNSTFACRVLSSSA- 279
Cdd:PLN02456  203 AIYRR----MYGRGPVIPDNSLDY--AENFLYMLgSLGDRSYKPDprlARLLDLYFIIHADH-EGGCSTAAARHLVGSSg 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 280 TDAYSAYAAAIGSLKGPRHGGANSKVMAMHEDIrahvrrwdddGEVAG---YLMKILNREAfdgagLIYGMGHAVYTLSD 356
Cdd:PLN02456  276 VDPYTSVAAGVNALAGPLHGGANEAVLKMLKEI----------GTVENipeYVEGVKNSKK-----VLPGFGHRVYKNYD 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 357 PRAQLCRRYArsLAEQKGLGDEfALIERIERLAPQVMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAG 436
Cdd:PLN02456  341 PRAKCIREFA--LEVFKHVGDD-PLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAG 417
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2556165550 437 WAAHRMEEL-YGANRIIRP--AYNSVMEDvTYVPLAER 471
Cdd:PLN02456  418 YLSQWDEALgLPDERIMRPkqVYTGEWLR-HYCPKAER 454
gltA PRK05614
citrate synthase;
81-454 3.79e-46

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 165.43  E-value: 3.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  81 VDGavvpDEGKLTIWGYDIQELVDHAQqeqrfgYEEIVFLLLTGQLPRADELEALRARIGGLRLLPTD---YIHEFPmtt 157
Cdd:PRK05614   62 IDG----DKGILLYRGYPIEQLAEKSD------FLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQlkrFFRGFR--- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 158 ASKSIMNVLARAVLLLYAFdeTPDDTSPNHEVDVALS---LLARLPRIAAIAHttrqaelegrRAHIPRPVeTY-----S 229
Cdd:PRK05614  129 RDAHPMAVLCGVVGALSAF--YHDSLDINDPEHREIAairLIAKMPTLAAMAY----------KYSIGQPF-VYprndlS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 230 MAETILQILR----EGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKV 305
Cdd:PRK05614  196 YAENFLRMMFatpcEEYEVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAV 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 306 MAMHEDIrahvrrwDDDGEVAGYLMKILNREafDGAGLIyGMGHAVYTLSDPRAQLCRRYARSLAEQKGLGDE-FALIER 384
Cdd:PRK05614  275 LKMLEEI-------GSVDNIPEFIARAKDKN--DGFRLM-GFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPlLEVAME 344
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2556165550 385 IERLApqvMREERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELY-GANRIIRP 454
Cdd:PRK05614  345 LEEIA---LNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSdPEQKIGRP 412
PRK14037 PRK14037
citrate synthase; Provisional
52-471 1.47e-45

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 162.99  E-value: 1.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  52 NVKRGLRNANGSgvVAGLTRIsdvhgyrkvDGavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQLPRADE 131
Cdd:PRK14037    3 VISKGLENVIIK--VTNLTFI---------DG----EKGILRYRGYNIEDLVNYG------SYEETIYLMLYGELPTKKE 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 132 LEALRARIGGLRLLP---TDYIHEFPMTTASKSIMNVlarAVLLLYAFDETPDDTSPNHevDVALSLLARLPRIAAIAHT 208
Cdd:PRK14037   62 LNDLKEKLNEEYEVPqevIDSIYLMPRDSDAIGLMEA---AFAALASIDKNFKWKENDK--EKAISIIAKMATIVANVYR 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 209 TRqaelEGRRAHIPRPVETYsmAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAA 288
Cdd:PRK14037  137 RK----EGNKPRIPEPSDSF--AESFLLASF-AREPTAEEIKAMDAALILYTDHEV-PASTTAALVAASTLSDMYSCITA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 289 AIGSLKGPRHGGANSKVMAMHEDIR--AHVRRWDDDgevagylmKILNreafdGAGLIYGMGHAVYTLSDPRAQLCRRYA 366
Cdd:PRK14037  209 ALAALKGPLHGGAAEEAFKQFVEIGdpNNVEMWFND--------KIIN-----GKKRLMGFGHRVYKTYDPRAKIFKELA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 367 RSLAEQKGLGDE-FALIERIERLAPQVMreergTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEEL 445
Cdd:PRK14037  276 ETLIERNSEAKKyFEIAQKLEELGIKQF-----GSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYV 350
                         410       420
                  ....*....|....*....|....*..
gi 2556165550 446 YGANRIIRP-AYNSVMEDVTYVPLAER 471
Cdd:PRK14037  351 EEQHRLIRPrALYVGPEHREYVPIDKR 377
PRK12350 PRK12350
citrate synthase 2; Provisional
64-455 4.53e-40

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 147.42  E-value: 4.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  64 GVVAGLTRISDVHGyrkvdgavvpDEGKLTIWGYDIQELVDHAqqeqrfGYEEIVFLLLTGQ----LPRADELEaLRARI 139
Cdd:PRK12350    7 GVVAFETEIAEPDG----------DGGALRYRGVDIEDLVGRV------TFEDVWALLVDGRfgpgLPPAEPFP-LPVHL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 140 GGLRLlptdyihefpmttasksimNVLARAVLL--LYAFDETPDDTSPNHEVDvalslLARLPRIA--AIAHTTRQAEle 215
Cdd:PRK12350   70 GDARV-------------------DVQAALAMLapVWGFRPLLDIDDLTARLD-----LARASVMAlsAVAQSARGIG-- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 216 grRAHIPRPveTYSMAETILQIL--REGDDFTRDEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSL 293
Cdd:PRK12350  124 --QPAVPQR--EIDHAATILERFmgRWRGEPDPAHVAALDAYWVSAAEHGM-NASTFTARVIASTGADVAAALSGAIGAL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 294 KGPRHGGANSKVMAMHEDIRAHvrrwdddGEVAGYLMKILNReafdGAGLIyGMGHAVYTLSDPRAQLCRRYARSLAeqk 373
Cdd:PRK12350  199 SGPLHGGAPARVLPMLDAVERT-------GDARGWVKGALDR----GERLM-GFGHRVYRAEDPRARVLRATAKRLG--- 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 374 glGDEFALIERIERLAPQVMReERGTTKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELyGANRIIR 453
Cdd:PRK12350  264 --APRYEVAEAVEQAALAELR-ERRPDRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQK-RTGRLVR 339

                  ..
gi 2556165550 454 PA 455
Cdd:PRK12350  340 PS 341
PRK09569 PRK09569
citrate (Si)-synthase;
115-456 2.30e-32

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 127.94  E-value: 2.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 115 EEIVFLLLTGQLPRADELEA----LRAR-------IGGLRLLPTDyIHefPMTTASKSIMnVLARAVLLLYAFDETP--- 180
Cdd:PRK09569   87 ESFWYFLLTGEVPTQEQVQEvvaeWKKRqnvpqyvIDAIRALPRD-SH--PMVMLSVGIL-AMQRESKFAKFYNEGKfnk 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 181 -DDTSPNHEvDvALSLLARLPRIAA--IAHTTRQAElegrraHIPrPVETYSMAETILQILREGDDFTrdeamllDVMLM 257
Cdd:PRK09569  163 mDAWEYMYE-D-ASDLVARIPVIAAyiYNLKYKGDK------QIP-SDPELDYGANFAHMIGQPKPYK-------DVARM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 258 ---LHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKVMAMHEDIRAHVRrwddDGEVAGYLMKILN 334
Cdd:PRK09569  227 yfiLHSDHESGNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLG----GEEPTKEQVEQAL 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 335 REAFDGAGLIYGMGHAVYTLSDPRAQLCRRYArslaeQKGLGDE--FALIERIERLAPQVMrEERGTTKPICANIDLYTG 412
Cdd:PRK09569  303 WDTLNAGQVIPGYGHAVLRKTDPRYTAQREFC-----LKHLPDDplFKLVAMIFEVAPGVL-TEHGKTKNPWPNVDAQSG 376
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2556165550 413 FIYSMLGVPE-DLFTPIFAVARTAGWAAHRMEELYGANRIIRPAY 456
Cdd:PRK09569  377 VIQWYYGVKEwDFYTVLFGVGRALGVMANITWDRGLGYAIERPKS 421
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
82-436 1.83e-27

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: 113.75  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  82 DGAVV-PDEG----KLTIwgYDIQELVDHAQQEQRFGYEEIVFLLLTGQLPRADELEALRARIGGLRLLP---TDYIHEF 153
Cdd:cd06106    49 EGSVLdAEEGirfhGKTI--PECQKELPKAPIGGEMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPhyiEKLLDSL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 154 PMTTASksiMNVLARAVLLL---YAFDETPDDTSPNHE-----VDVALSLLARLPRIAAIAHTTRQAELEGRRAHIPrpv 225
Cdd:cd06106   127 PKTLHP---MTQLSIGVAALnhdSKFAAAYEKGIKKTEyweptLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDP--- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 226 eTYSMAETILQILREGD--DFTRdeamLLDVMLMLHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANS 303
Cdd:cd06106   201 -EVDWSYNFTSMLGYGDnlDFVD----LLRLYIALHGDHEGGNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQ 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 304 KV----MAMHEDIRAHVRrwddDGEVAGYLMKILNreafdGAGLIYGMGHAVYTLSDPRAQLCRRYARSLAEQKGlGDEF 379
Cdd:cd06106   276 EVlrwiLEMQKNIGSKAT----DQDIRDYLWKTLK-----SGRVVPGYGHAVLRKPDPRFTALMEFAQTRPELEN-DPVV 345
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2556165550 380 ALIERIERLAPQVMREErGTTKPICANIDLYTGFIYSMLGVPEDLF-TPIFAVARTAG 436
Cdd:cd06106   346 QLVQKLSEIAPGVLTEH-GKTKNPFPNVDAASGVLFYHYGIREFLYyTVIFGVSRALG 402
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
45-436 1.53e-25

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: 108.16  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  45 EALFREHNVKR----GLRNANGSGVVAGLTRISDVHGYRKVDGAVV------PDEGkLTIWGYDIQELVDHAQQEQRFGY 114
Cdd:cd06103     3 DKLAELIPKKQarikELRKKYGNTKLGQITVDQVIGGMRGMKGLVYetsvldPDEG-IRFRGKTIPECQELLPKADGGGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 115 ---EEIVFLLLTGQLPRADELEAL------RARIGG-----LRLLPTDyIHefPMTTASKSIM-----NVLARAvlllYA 175
Cdd:cd06103    82 plpEGLFWLLLTGEVPTEEQVDELskewakRAEVPShvvkmIDNLPRN-LH--PMTQLSAAILalqseSKFAKA----YA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 176 FDETPDDTSPNHEVDVALSLLARLPRIAAIAHttrqaelegRRahiprpveTYSMAETILQILREGD---DFTR----DE 248
Cdd:cd06103   155 EGKINKTTYWEYVYEDAMDLIAKLPVVAAKIY---------RR--------KYRKGGEIGAIDSKLDwsaNFAHmlgyED 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 249 AMLLDVM---LMLHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKVMAMHEDIRAHVRRWDDDGEV 325
Cdd:cd06103   218 EEFTDLMrlyLTLHSDHEGGNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEEL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 326 AGYLMKILNreafdGAGLIYGMGHAVYTLSDPRAQLCRRYArslaeQKGLGDE--FALIERIERLAPQVMREErGTTKPI 403
Cdd:cd06103   298 EKYIWDTLN-----SGRVVPGYGHAVLRKTDPRFTCQREFA-----LKHLPDDplFKLVAQCYKIIPGVLKEH-GKVKNP 366
                         410       420       430
                  ....*....|....*....|....*....|....
gi 2556165550 404 CANIDLYTGFIYSMLGVPE-DLFTPIFAVARTAG 436
Cdd:cd06103   367 YPNVDAHSGVLLQHYGMTEpQYYTVLFGVSRALG 400
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
87-436 1.81e-21

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: 96.28  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550  87 PDEGkLTIWGYDI---QELVDHAQQEQRFGYEEIVFLLLTGQLPRADELEAL------RARIGG-----LRLLPTDyIHe 152
Cdd:cd06105    55 PEEG-IRFRGLSIpecQKLLPKAPGGEEPLPEGLFWLLLTGEVPTKEQVSALskewaaRAALPShvvtmLDNFPTN-LH- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 153 fPMTTASKSIMNV-----LARAvlllYAfDETPDDTSPNHEVDVALSLLARLPRIAAIahttrqaelegrrahIPRPVET 227
Cdd:cd06105   132 -PMSQLSAAITALnseskFAKA----YA-EGIHKSKYWEYVYEDSMDLIAKLPCVAAK---------------IYRNLYR 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 228 YSMAETILQILREGDDFTR----DEAMLLDVM---LMLHAEHGGGNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGG 300
Cdd:cd06105   191 GGKIIAIDSNLDWSANFANmlgyTDPQFTELMrlyLTIHSDHEGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 301 ANSKVMAMHEDIRAHVRRWDDDGEVAGYLMKILNreafdgAG-LIYGMGHAVYTLSDPRAQLCRRYArslaeQKGLGDE- 378
Cdd:cd06105   271 ANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLN------SGrVVPGYGHAVLRKTDPRYTCQREFA-----LKHLPNDp 339
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 379 -FALIERIERLAPQVMREErGTTKPICANIDLYTGFIYSMLGVPE-DLFTPIFAVARTAG 436
Cdd:cd06105   340 lFKLVSQLYKIVPPVLTEQ-GKAKNPWPNVDAHSGVLLQYYGLTEmNYYTVLFGVSRALG 398
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
247-454 4.41e-21

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


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 93.09  E-value: 4.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 247 DEAMLLDVMLMLHAEHGGgNNSTFACRVLSSSATDAYSAYAAAIGSLKGPRHGGANSKVMAM------HEDIRAHVRRWD 320
Cdd:cd06102    96 AAADLLRRALVLLADHEL-NASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALldealrAGDAEAAVRERL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 321 DDGEVagylmkilnreafdgaglIYGMGHAVYTLSDPRAQlcrryarslaeqkglgdefALIERIERLAPQVMR------ 394
Cdd:cd06102   175 RRGEA------------------LPGFGHPLYPDGDPRAA-------------------ALLAALRPLGPAAPPaarali 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2556165550 395 ---EERGTTKPicaNIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEElYGANRIIRP 454
Cdd:cd06102   218 eaaRALTGARP---NIDFALAALTRALGLPAGAAFALFALGRSAGWIAHALEQ-RAQGKLIRP 276
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
225-465 1.48e-15

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: 75.68  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 225 VETYSMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGGNNSTFACRV-LSSSATDAYSAYAAAIGSLkGPRHGGANS 303
Cdd:cd06100     8 IGKISFGDVLYLLLK-GRLPTPYEARLLEALLVALADHGPATPSAHAARLtASAGPEDLQSAVAAGLLGI-GDRFGGAGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 304 KVMAMHEDIRahvrrwDDDGEVAGYLMKILNREAFDGAgLIYGMGHAVYTLSDPRAQLCRRYARSLAEQkglGDEFALIE 383
Cdd:cd06100    86 GAARLFKEAV------DSGDALDAAAAEFVAEYRAAKK-RIPGFGHPVHKNPDPRVPRLLELARELGPA---GPHLDYAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 384 RIERlapqVMREERGttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELyganRIIRPAYNSVMEDV 463
Cdd:cd06100   156 AVEK----ALTAAKG--KPLPLNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEK----RLGQPLYRHPWDDI 225

                  ..
gi 2556165550 464 TY 465
Cdd:cd06100   226 EY 227
PRK06224 PRK06224
citryl-CoA lyase;
229-471 1.90e-14

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 72.98  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 229 SMAETILQILReGDDFTRDEAMLLDVMLMLHAEHGGGNnSTFACRVLSSSATDAYSAYAAAIGSLkGPRHGGANSKVMAM 308
Cdd:PRK06224   36 SFTDMIFLLLR-GRLPTPNEARLLDAVLVALVDHGLTP-SAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 309 HEDIRAHVRRWDDDGEVAGYLMkilnREAFDGAGLIYGMGHAVYTLSDPRAQlcRRYArsLAEQKGL-GDEFALIERIER 387
Cdd:PRK06224  113 LQEIAAAADAGADLDAAARAIV----AEYRAAGKRVPGFGHPLHKPVDPRAP--RLLA--LAREAGVaGRHCRLAEALEA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556165550 388 LAPqvmrEERGttKPICANIDLYTGFIYSMLGVPEDLFTPIFAVARTAGWAAHRMEELY--GANRIIRPAynsvMEDVTY 465
Cdd:PRK06224  185 ALA----AAKG--KPLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQqpIGFRIWDPA----EEAVEY 254

                  ....*.
gi 2556165550 466 VPLAER 471
Cdd:PRK06224  255 TGPPPR 260
 
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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