|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
4-384 |
0e+00 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 683.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 4 TEEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQdEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFV 83
Cdd:PRK14037 1 MSVISKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSY-EETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 84 INAIRQLPRESDAVAMQMAAVAAMAASETKFKWnKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLN 163
Cdd:PRK14037 80 IDSIYLMPRDSDAIGLMEAAFAALASIDKNFKW-KENDKEKAISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 164 AAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMV 243
Cdd:PRK14037 159 ASFAREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 244 EKWFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYFSGI 323
Cdd:PRK14037 239 EMWFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGIYPNTDFYSGI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499203056 324 VYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:PRK14037 319 VFYALGFPV--YMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
5-385 |
0e+00 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 673.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 5 EEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVI 84
Cdd:NF041157 1 MEISKGLENVFIKYTSLTYIDGEKGILRYRGYDINDL-VNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 85 NAIRQLPRESDAVAMQMAAVAAMAaSETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNA 164
Cdd:NF041157 80 SIIRSLPRDSDALAMMETAFSALA-SIENYKWNKENDREKALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 165 AFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVE 244
Cdd:NF041157 159 TFGRKPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 245 KWFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYFSGIV 324
Cdd:NF041157 239 KWFNENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTN-EAKKYLEIAEKLEELGIKHFGSKGIYPNTDFYSGIV 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499203056 325 YMSIGFPLRnnIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVYVGPAERKYVPIAERK 385
Cdd:NF041157 318 FYSLGFPVY--MFTSLFALSRVLGWLAHIIEYVEEQHRLIRPRALYVGPEKRDFVPIDERK 376
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
9-384 |
0e+00 |
|
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: 550.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASgAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:TIGR01800 1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEH-ASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRESDAVAMQMAAVAAMAASET-KFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFG 167
Cdd:TIGR01800 80 ALPAESHPMDVLRTAVSYLGALDPeKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 168 RKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWF 247
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 248 NDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIKafgSKGIYPNTDYFSGIVYMS 327
Cdd:TIGR01800 240 RKALEN-KERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGS-SKWYEIAERLEDVMEE---EKGIYPNVDFFSASVYYM 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 328 IGFPLRnnIYTALFALSRVTGWQAHFIEYVeEQQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:TIGR01800 315 MGIPTD--LFTPIFAMSRVTGWTAHIIEQV-ENNRLIRPRADYVGPEERKYVPIEER 368
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
9-370 |
2.80e-175 |
|
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: 492.12 E-value: 2.80e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEEL-AEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRESDAVAMQMAAVAAMAASETKFK-WNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFG 167
Cdd:cd06118 80 LLPKNAHPMDVLRTAVSALGSFDPFARdKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 168 RKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWF 247
Cdd:cd06118 160 EEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 248 NDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYFSGIVYMS 327
Cdd:cd06118 240 WKKLAN-KRRIMGFGHRVYKTYDPRAKILKELAEELAEEK-GDDKLFEIAEELEEIALEVLGEKGIYPNVDFYSGVVYKA 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499203056 328 IGFPlrNNIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVY 370
Cdd:cd06118 318 LGFP--TELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
6-384 |
1.64e-149 |
|
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: 427.97 E-value: 1.64e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 6 EISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVIN 85
Cdd:COG0372 12 TVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDL-AEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 86 AIRQLPRES----------------DavamqmaavaamaasETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAE 149
Cdd:COG0372 91 FLDGFPRDAhpmdvlrtavsalgafD---------------PDADDIDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 150 LPKPSDSYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEA 229
Cdd:COG0372 156 YPDPDLSYAENFLYMLFGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 230 AIAQFDEIKDPAMVEKWFnDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIKA-- 307
Cdd:COG0372 236 VLEMLEEIGSPDNVEEYI-RKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGD-DPLLEIAEELEEVALEDey 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 308 FGSKGIYPNTDYFSGIVYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:COG0372 314 FIEKKLYPNVDFYSGIVYHALGIPT--DMFTPIFAISRVAGWIAHWLEQRAD-NRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
10-367 |
3.52e-132 |
|
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: 382.62 E-value: 3.52e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQ 89
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEEL-AERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 90 LPRESDAVAMQMAAVAAMAASETKFKWNKDTDRDVAAE--MIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFG 167
Cdd:pfam00285 80 LPRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRddLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 168 RKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWF 247
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 248 NDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIK--AFGSKGIYPNTDYFSGIVY 325
Cdd:pfam00285 240 RKVLNKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGD-DPLLELAEELEEVAPEdlYFVEKNLYPNVDFYSGVLY 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499203056 326 MSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPR 367
Cdd:pfam00285 319 HALGIPT--DMFTPLFAISRTAGWLAHWIEQLAD-NRIIRPR 357
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
9-370 |
7.86e-115 |
|
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: 335.05 E-value: 7.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASgAQDEEIQYLFLYGNLPteqelrkyketvqkgykipdfvinair 88
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAEN-SSFEEVAYLLLTGELP--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 qlpresdavamqmaavaamaasetkfkwnkdtdrdvaaemigrmsaitvnvyrhimnmpaelpkpsdSYAESFLNAAFGR 168
Cdd:cd06101 53 -------------------------------------------------------------------SYAENFLYMLGGE 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 169 KATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDP--AMVEKW 246
Cdd:cd06101 66 EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPknEPAEAY 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 247 FNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYFSGIVYM 326
Cdd:cd06101 146 IRKKLNS-KRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEK-GLDPMFELAAELEKIAPEVLYEKKLYPNVDFYSGVLYK 223
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499203056 327 SIGFPlrNNIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVY 370
Cdd:cd06101 224 AMGFP--TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
7-381 |
1.07e-100 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.
Pssm-ID: 99865 Cd Length: 373 Bit Score: 303.19 E-value: 1.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 7 ISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQdEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINA 86
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSF-EEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 87 IRQLPRES---DAVAMQMAAVAAMAASETKFKWNKDTDRDVAAEMIGRMSAItVNVYRHIMNM--PAElPKPSDSYAESF 161
Cdd:cd06112 80 MKCFPETGhpmDMLQATVAALGMFYPKPEVLKPNPDYIDAATVKLIAKMPTL-VAMWARIRNGddPIE-PRPDLDYAENF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 162 LNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPA 241
Cdd:cd06112 158 LYMLFGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 242 MVEKWFnDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYFS 321
Cdd:cd06112 238 NVKAYL-DKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEELLGHKGVYPNVDFYS 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 322 GIVYMSIGFPlrNNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERKYVPI 381
Cdd:cd06112 317 GIVYKELGIP--ADLFTPIFAVARVAGWLAHWKEQLGD-NRIFRPTQIYIGEIDRKYVPL 373
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
9-372 |
1.27e-100 |
|
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: 302.27 E-value: 1.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:cd06110 1 KGLEGVIAADSKISYIDGDAGILIYRGYDIHDL-AENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRESDAVAMQMAAVAAMAASETKFK-WNKDTDRDVAAEMIGRMSAItVNVYRHIMN--MPAElPKPSDSYAESFLNAA 165
Cdd:cd06110 80 LLPKDAHPMDVLRTAVSALALYDPEADdMSREANLRKAIRLIAKMPTI-VAAFHRIRNglEPVA-PDPDLSHAANFLYML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 166 FGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEK 245
Cdd:cd06110 158 TGEKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 246 WFnDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLsSKKPEVHKVYEIATKLEDFgikAFGSKGIYPNTDYFSGIVY 325
Cdd:cd06110 238 YV-KDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRL-GKETGEPKWYEMSEAIEQA---MRDEKGLNPNVDFYSASVY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499203056 326 MSIGFPLrnNIYTALFALSRVTGWQAHFIeyveEQQ---RLIRPRAVYVG 372
Cdd:cd06110 313 YMLGIPV--DLFTPIFAISRVSGWCAHIL----EQYfnnRLIRPRAEYVG 356
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
22-372 |
5.69e-88 |
|
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding.
Pssm-ID: 99867 Cd Length: 400 Bit Score: 271.38 E-value: 5.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 22 TTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESD--AVAM 99
Cdd:cd06114 42 TYIDGEKGILRYRGYPIEQL-AEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHpmAILS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 100 QMAAVAAMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGR-----KATKEE 174
Cdd:cd06114 121 AMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVpyepyEVDPVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 175 IDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFN---DNi 251
Cdd:cd06114 201 VKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAkakDK- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 252 iNGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGIKA--FGSKGIYPNTDYFSGIVYMSIG 329
Cdd:cd06114 280 -NDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPLLEIAMELEEIALKDdyFIERKLYPNVDFYSGIILRALG 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499203056 330 FPLrnNIYTALFALSRVTGWQAHFIEYVEE-QQRLIRPRAVYVG 372
Cdd:cd06114 359 IPT--EMFTVLFALGRTPGWIAQWREMHEDpELKIGRPRQLYTG 400
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
10-372 |
4.16e-85 |
|
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: 263.53 E-value: 4.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASgAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQ 89
Cdd:cd06107 8 GYLNTAVCESSITYIDGDKGILLYRGYPIEQLAES-STYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 90 LPRESD-------AVAMQMAAVAAMAASETKFKWNKDTD-RDVAA-EMIGRMSAITVNVYRHIMNMPAELPKPSDSYAES 160
Cdd:cd06107 87 FPRDAHpmgilcaGLSALSAFYPEAIPAHTGDLYQNNPEvRDKQIiRTLAKMPTIAAAAYCHRIGRPFVYPRANLSYIEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 161 FLNAAFGRKATKEEID-----AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFD 235
Cdd:cd06107 167 FLYMMGYVDQEPYEPNprlarALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 236 EIKDPAMVEKwFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGI--KAFGSKGI 313
Cdd:cd06107 247 EIGTPENVPA-FIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEV-EKDPLLKVAMELERIALedEYFVSRKL 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 314 YPNTDYFSGIVYMSIGFPlrNNIYTALFALSRVTGWQAHFIEYVEE-QQRLIRPRAVYVG 372
Cdd:cd06107 325 YPNVDFYSGFIYKALGFP--PEFFTVLFAVARTSGWMAHWREMMEDpLQRIWRPRQVYTG 382
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
10-381 |
4.30e-83 |
|
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: 257.62 E-value: 4.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIdGNKGI-LRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:cd06108 2 GLAGVVAGQTAISTV-GKGGKgLTYRGYDIEDL-AENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRESD--AVAMQMAAVAAMAASETKFkwnkDTDRDVAAEMIGRMSAITVNVYR-HIMNMPAELPKPSDSYAESFLNAA 165
Cdd:cd06108 80 LIPKDSHpmDVMRTGCSMLGCLEPENEF----SQQYEIAIRLLAIFPSILLYWYHySHSGKRIETETDEDSIAGHFLHLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 166 FGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEK 245
Cdd:cd06108 156 HGKKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 246 WFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIKafgSKGIYPNTDYFSGIVY 325
Cdd:cd06108 236 GLLEKLER-KELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGD-PLLYQISERIEEVMWE---EKKLFPNLDFYSASAY 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499203056 326 MSIGFPlrNNIYTALFALSRVTGWQAHFIEYvEEQQRLIRPRAVYVGPAERKYVPI 381
Cdd:cd06108 311 HFCGIP--TELFTPIFVMSRVTGWAAHIMEQ-RANNRLIRPSADYIGPEPRPFVPI 363
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
1-381 |
2.53e-82 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 256.03 E-value: 2.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 1 MPETEEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASgAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIP 80
Cdd:PRK14033 3 TDETPEIKKGLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAAR-CSFEEVAYLLWNGELPTDAELALFSQRERAYRRLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 81 DFVINAIRQLPRES---DAVAMQMAAVAAMAASEtkFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSY 157
Cdd:PRK14033 82 RSVLSLIDKLPTTChpmDVVRTAVSYLGAEDPEA--DDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 158 AESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEI 237
Cdd:PRK14033 160 AENFLHMCFGEVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 238 KDPAMVEKWFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSS--KKPEVHKVYEIatkLEDFGIKAfgsKGIYP 315
Cdd:PRK14033 240 GDPARAAEWLRDALAR-KEKVMGFGHRVYKHGDSRVPTMKAALRRVAAvrDGQRWLDIYEA---LEKAMAEA---TGIKP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499203056 316 NTDYFSGIVYMSIGFPLRnnIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERKYVPI 381
Cdd:PRK14033 313 NLDFPAGPAYYLMGFDID--FFTPIFVMSRITGWTAHIMEQRAS-NALIRPLSEYNGPEQREVPPI 375
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
7-384 |
5.73e-82 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 255.07 E-value: 5.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 7 ISKGLEDVNIKWTRLTTIDGNkgILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINA 86
Cdd:PRK14034 3 VTRGLEGVVATTSSVSSIIDD--TLTYVGYNIDDL-AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 87 IRQLPRES--DAVAMQMAAVAAMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNA 164
Cdd:PRK14034 80 LKQYDLKKvhPMSVLRTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 165 AFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVE 244
Cdd:PRK14034 160 LNGEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 245 KWFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFgikAFGSKGIYPNTDYFSGIV 324
Cdd:PRK14034 240 SYIHNKLQN-KEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGE-EKWYNMSIKIEEI---VTKEKGLPPNVDFYSASV 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 325 YMSIGfpLRNNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:PRK14034 315 YHCLG--IDHDLFTPIFAISRMSGWLAHILEQYEN-NRLIRPRADYVGPTHQVYVPIEER 371
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
6-384 |
2.11e-81 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 253.53 E-value: 2.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 6 EISKGLEDVNIKWTRLTTIDGNKgiLRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPD---- 81
Cdd:PRK14035 2 ELQRGLEGVIAAETKISSIIDSQ--LTYAGYDIDDL-AENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDrvyq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 82 -FVINAIRQLPRESDAVAMQMAAVAAMAASETKfkwNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAES 160
Cdd:PRK14035 79 hFEEYSTDHVHPMTALRTSVSYLAHFDPDAEEE---SDEARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 161 FLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDP 240
Cdd:PRK14035 156 FLYMLRGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 241 AMVEKWFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLsSKKPEVHKVYEIATKLEDFgIKAfgSKGIYPNTDYF 320
Cdd:PRK14035 236 GDVDAYLDEKFAN-KEKIMGFGHRVYKDGDPRAKYLREMSRKI-TKGTGREELFEMSVKIEKR-MKE--EKGLIPNVDFY 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 321 SGIVYMSIGFPlrNNIYTALFALSRVTGWQAHfieyVEEQQ---RLIRPRAVYVGPAERKYVPIAER 384
Cdd:PRK14035 311 SATVYHVMGIP--HDLFTPIFAVSRVAGWIAH----ILEQYkdnRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
10-384 |
4.65e-81 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 252.96 E-value: 4.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQ 89
Cdd:PRK14036 7 GLEGVPATQSSISYVDGQKGILEYRGYPIEEL-AEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 90 LP----------------------RESDavamqmaavaamaasetkfkwNKDTDRDVAAEMIGRMSAItVNVYRHIM--N 145
Cdd:PRK14036 86 FPetghpmdalqasaaalglfysrRALD---------------------DPEYIRDAVVRLIAKIPTM-VAAFQLIRkgN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 146 MPAElPKPSDSYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGG 225
Cdd:PRK14036 144 DPIQ-PRDDLDYAANFLYMLTEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 226 AAEAAIAQFDEIKDPAMVEKWFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGI 305
Cdd:PRK14036 223 ANEDVLAMLEEIGSVENVRPYLDERLAN-KQKIMGFGHREYKVKDPRATILQKLAEELFARFGH-DEYYEIALELERVAE 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499203056 306 KAFGSKGIYPNTDYFSGIVYMSIGFPlrNNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:PRK14036 301 ERLGPKGIYPNVDFYSGLVYRKLGIP--RDLFTPIFAIARVAGWLAHWREQLGA-NRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
156-370 |
2.89e-80 |
|
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: 245.32 E-value: 2.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 156 SYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFD 235
Cdd:cd06099 1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 236 EIKDPAM--VEKWFNDNiINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHkVYEIATKLEDFGIKAFGSKGI 313
Cdd:cd06099 81 EIGTPKNepAEAYIRKK-LESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDP-MFELAAELEKIAEEVLYEKKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 314 YPNTDYFSGIVYMSIGFPLRnnIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVY 370
Cdd:cd06099 159 YPNVDFYSGVLYKAMGFPTE--LFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
9-377 |
4.95e-80 |
|
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: 249.64 E-value: 4.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASgAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:cd06111 1 KGLAGVVADTTAISKVMPETNSLTYRGYPVQDLAEN-CSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRES---DAVAMQMAAVAAMAASEtkFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAA 165
Cdd:cd06111 80 SLPKNChpmDVLRTAVSVLGAEDSET--DDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 166 FGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEK 245
Cdd:cd06111 158 FGEVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 246 WFNDNIINgKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIKAfgsKGIYPNTDYFSGIVY 325
Cdd:cd06111 238 WMLDALAR-KEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDG-QKWLAMYDALEDAMVAA---KGIKPNLDFPAGPAY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499203056 326 MSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVGPAERK 377
Cdd:cd06111 313 YLMGFDI--DFFTPIFVMARITGWTAHIMEQRAD-NALIRPLSEYNGPEQRP 361
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
15-384 |
3.85e-75 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 239.93 E-value: 3.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 15 NIKWTRLTT--IDGNKGILRYGGYSVEDIIASGAQdEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPR 92
Cdd:PLN02456 70 NTAPVLSEIslIDGDEGILRFRGYPIEELAEKSPF-EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 93 E--------------SDAVAMQMAAVAAMAASETKFKWNKDTDRdvaaeMIGRMSAITVNVYRHIMNMPAELPKPSDSYA 158
Cdd:PLN02456 149 DahpmtqlvsgvmalSTFSPDANAYLRGQHKYKSWEVRDEDIVR-----LIGKLPTLAAAIYRRMYGRGPVIPDNSLDYA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 159 ESFLNAAFGRKATKEEID-----AMNTALILYTDHEVPAST-TAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIA 232
Cdd:PLN02456 224 ENFLYMLGSLGDRSYKPDprlarLLDLYFIIHADHEGGCSTaAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 233 QFDEI----KDPAMVEKwfndnIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGI--K 306
Cdd:PLN02456 304 MLKEIgtveNIPEYVEG-----VKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGD-DPLFKVASALEEVALldE 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499203056 307 AFGSKGIYPNTDYFSGIVYMSIGFPlrNNIYTALFALSRVTGWQAHFIEYV-EEQQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:PLN02456 378 YFKVRKLYPNVDFYSGVLLRALGFP--EEFFTVLFAVSRAAGYLSQWDEALgLPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
31-384 |
3.46e-74 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 235.20 E-value: 3.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 31 LRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAAVAAMAAS 110
Cdd:PRK12351 32 LHYRGYDILDL-AEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 111 ET-KFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMN-MPAELPKPSDSYAESFLNAAFGRKATKEEIDAMNTALILYTDH 188
Cdd:PRK12351 111 LPeKEDHNFSGARDIADRLLASLGSILLYWYHYSHNgRRIEVETDDDSIGGHFLHLLHGKKPSESWVKAMHTSLILYAEH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 189 EVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDP--------AMVEKwfndniingKKRLMG 260
Cdd:PRK12351 191 EFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPdeaeadirRRVEN---------KEVVIG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 261 FGHRVYKTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFgikAFGSKGIYPNTDYFSGIVYMSIGFPlrNNIYTAL 340
Cdd:PRK12351 262 FGHPVYTISDPRNKVIKEVAKKLSKEAGD-TKLYDIAERLETV---MWEEKKMFPNLDWFSAVSYHMMGVP--TAMFTPL 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499203056 341 FALSRVTGWQAHFIEYvEEQQRLIRPRAVYVGPAERKYVPIAER 384
Cdd:PRK12351 336 FVISRTTGWAAHVIEQ-RQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| gltA |
PRK05614 |
citrate synthase; |
22-372 |
5.76e-72 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 230.92 E-value: 5.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 22 TTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRES------- 94
Cdd:PRK05614 60 TYIDGDKGILLYRGYPIEQL-AEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAhpmavlc 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 95 -----------DAVAMqmaavaamaasetkfkwNKDTDRDVAA-EMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFL 162
Cdd:PRK05614 139 gvvgalsafyhDSLDI-----------------NDPEHREIAAiRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 163 NAAFGRKATKEEID-----AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEI 237
Cdd:PRK05614 202 RMMFATPCEEYEVNpvlvrALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 238 KDPAMVEKWF------NDNIingkkRLMGFGHRVYKTYDPRAKIFKGIA----EKLSSKKPevhkVYEIATKLEDFGIKA 307
Cdd:PRK05614 282 GSVDNIPEFIarakdkNDGF-----RLMGFGHRVYKNYDPRAKIMRETChevlKELGLNDP----LLEVAMELEEIALND 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499203056 308 --FGSKGIYPNTDYFSGIVYMSIGFPLRnnIYTALFALSRVTGWQAHFIEYVEE-QQRLIRPRAVYVG 372
Cdd:PRK05614 353 eyFIERKLYPNVDFYSGIILKALGIPTS--MFTVIFALARTVGWIAHWNEMHSDpEQKIGRPRQLYTG 418
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
19-380 |
3.98e-70 |
|
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.
Pssm-ID: 99868 Cd Length: 410 Bit Score: 225.78 E-value: 3.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 19 TRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVA 98
Cdd:cd06115 37 SKISYIDGDKGILRYRGYPIEEL-AEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 99 MQMAAVAAMAA----------SETKFKWNKDTDRDVAaEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGR 168
Cdd:cd06115 116 MLVSAISALSAfhpeanpalaGQDIYKNKQVRDKQIV-RILGKAPTIAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 169 KATKEEID-----AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMV 243
Cdd:cd06115 195 GERKYKPNprlarALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 244 EKwFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAE---KLSSKKPevhkVYEIATKLEDFGIKA--FGSKGIYPNTD 318
Cdd:cd06115 275 PA-FIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADevfEIVGKDP----LIEIAVALEKAALSDeyFVKRKLYPNVD 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499203056 319 YFSGIVYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEQQ-RLIRPRAVYVGPAERKYVP 380
Cdd:cd06115 350 FYSGLIYRAMGFPT--DFFPVLFAIPRMAGYLAHWRESLDDPDtKIMRPQQLYTGVWLRHYVP 410
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
21-381 |
4.41e-70 |
|
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.
Pssm-ID: 99869 Cd Length: 384 Bit Score: 224.71 E-value: 4.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 21 LTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKetvqkgYKIPD--FVINAIRQLPR--ESDA 96
Cdd:cd06116 19 ITYIDGEKGILRYRGYPIEQL-AEQSSYLEVAYLLLHGELPTKERLAQWV------YDITRhtMTHENLKKFMDgfRYDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 97 VAMQMAAVAAMAASeTKFKWNKDTDRDVAAEM-----IGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGRKAT 171
Cdd:cd06116 92 HPMGILISSVAALS-TFYPEAKNIGDEEQRNKqiirlIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNFLSMLFKMTEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 172 KEEID-----AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKw 246
Cdd:cd06116 171 KYEPNpvlakALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPD- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 247 FNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKL---SSKKPEVhkvyEIATKLEDFGIK--AFGSKGIYPNTDYFS 321
Cdd:cd06116 250 FIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVfeaTGRNPLL----DIAVELEKIALEdeYFISRKLYPNVDFYS 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499203056 322 GIVYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEE-QQRLIRPRAVYVGPAERKYVPI 381
Cdd:cd06116 326 GLIYQALGFPT--EAFTVLFAIPRTSGWLAQWIEMLRDpEQKIARPRQVYTGPRDRDYVPI 384
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
3-373 |
5.52e-70 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 224.21 E-value: 5.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 3 ETEEISKGLEDVNIKWTRLTTIDGNKGILRYGGYsveDIIASGAQDE--EIQYLFLYGNLPTEQELRKYKETVQKGYKIP 80
Cdd:PRK12349 1 AEEKFSPGLDGVIAAETKISFLDTVKGEIVIQGY---DLIELSKTKEylDIVHLLLEEHLPNEDEKATLEKKLKEEYAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 81 DFVINAIRQLPRESDAVAMQMAAVAAMAASETKFKwNKDT--DRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYA 158
Cdd:PRK12349 78 EGVFNILKALPKETHPMDGLRTGVSALAGYDNDIE-DRSLevNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 159 ESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIK 238
Cdd:PRK12349 157 ANFLYMLTGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 239 DPAMVEKWFNDNIINgKKRLMGFGHRVY-KTYDPRAKIFKGIAEKLSSKKPEvHKVYEIATKLEDFGIKafgSKGIYPNT 317
Cdd:PRK12349 237 TVEKFEELLQKKLYN-KEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGD-YTLYEMCEAGEKIMEK---EKGLYPNL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499203056 318 DYFSGIVYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYvEEQQRLIRPRAVYVGP 373
Cdd:PRK12349 312 DYYAAPVYWMLGIPI--QLYTPIFFSSRTVGLCAHVIEQ-HANNRLFRPRVNYIGE 364
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
19-378 |
1.68e-67 |
|
citrate synthase I (hexameric type); This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes. [Energy metabolism, TCA cycle]
Pssm-ID: 273811 Cd Length: 412 Bit Score: 218.88 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 19 TRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVA 98
Cdd:TIGR01798 44 SKITFIDGDKGILLYRGYPIDQL-AEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 99 MQMAAVAAMAA-SETKFKWNKDTDRDVAA-EMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGRKATKEEID 176
Cdd:TIGR01798 123 VMVGVVGALSAfYHDALDINDPRHREISAiRLIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 177 -----AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKD----PAMVEKWF 247
Cdd:TIGR01798 203 pvlarAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSvkniDEFIKKVK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 248 NDniiNGKKRLMGFGHRVYKTYDPRAKIFKGIA-EKLSSKKPEVHKVYEIATKLEDFGIKA--FGSKGIYPNTDYFSGIV 324
Cdd:TIGR01798 283 DK---NDPFRLMGFGHRVYKNYDPRAKVMRETChEVLKELGLHDDPLFKLAMELEKIALNDpyFIERKLYPNVDFYSGII 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499203056 325 YMSIGFPlrNNIYTALFALSRVTGWQAHFIEYVEE-QQRLIRPRAVYVGPAERKY 378
Cdd:TIGR01798 360 LKAMGIP--TSMFTVIFALARTVGWISHWSEMISDpGQKIGRPRQLYTGETQRDY 412
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
19-381 |
4.94e-66 |
|
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: 213.94 E-value: 4.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 19 TRLTTIDGNKGILRYGGYSVEDIiASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVA 98
Cdd:cd06117 11 TALCTVGRSGNDLHYRGYDILDL-AEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 99 MQMAAVAAM-AASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMN-MPAELPKPSDSYAESFLNAAFGRKATKEEID 176
Cdd:cd06117 90 VMRTGVSVLgCVLPEKEDHPVSGARDIADRLMASLGSILLYWYHYSHNgKRIEVETDDDSIGGHFLHLLHGEKPSESWEK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 177 AMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIINgKK 256
Cdd:cd06117 170 AMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVEN-KE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 257 RLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVhKVYEIATKLEDFgikAFGSKGIYPNTDYFSGIVYMSIGFPlrNNI 336
Cdd:cd06117 249 VVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDM-KMFDIAERLETV---MWEEKKMFPNLDWFSAVSYHMMGVP--TAM 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499203056 337 YTALFALSRVTGWQAHFIEYvEEQQRLIRPRAVYVGPAERKYVPI 381
Cdd:cd06117 323 FTPLFVIARTTGWSAHIIEQ-RQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
9-372 |
2.57e-64 |
|
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: 208.70 E-value: 2.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 9 KGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQdEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIR 88
Cdd:cd06109 1 PGLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASF-EDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 89 QLPRESDAVAMQMAAVAAmaasetkfkwNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGR 168
Cdd:cd06109 80 ALAGLDPMDALRALLALL----------PDSPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 169 KATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFN 248
Cdd:cd06109 150 PPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 249 DNIINGkKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEvhkvYEIATKLEDFGIKAFGSK----GIYPNTDYFSGIV 324
Cdd:cd06109 230 EALARG-ERLMGFGHRVYRVRDPRADVLKAAAERLGAPDER----LEFAEAVEQAALALLREYkpgrPLETNVEFYTALL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 499203056 325 YMSIGFPlrNNIYTALFALSRVTGWQAHFIEYVEEqQRLIRPRAVYVG 372
Cdd:cd06109 305 LEALGLP--REAFTPTFAAGRTAGWTAHVLEQART-GRLIRPQSRYVG 349
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
24-372 |
2.38e-54 |
|
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: 184.39 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 24 IDGNK----GILRYGGYSVEDIIaSGAQD------EEIQYLFLYGNLPTEQELRKYKETVQKGYKIPD-FVINAIRQLPr 92
Cdd:cd06113 27 IDGEKvpcpGKLYYRGYDVEDLV-NGAQKenrfgfEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDnFVEDVILKAP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 93 ESDAVAMQMAAVAAMAASETKfkwNKDTDRD----VAAEMIGRMSAITV---NVYRHIM---NMPAELPKPSDSYAESFL 162
Cdd:cd06113 105 SKDIMNKLQRSVLALYSYDDK---PDDISLEnvlrQSIQLIARLPTIAVyayQAKRHYYdgeSLYIHHPQPELSTAENIL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 163 NAAF-GRKATKEEIDAMNTALILYTDHEVPA-STTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDP 240
Cdd:cd06113 182 SMLRpDKKYTELEAKLLDLCLVLHAEHGGGNnSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKEN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 241 amVEKWFNDNII-------------NGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGIKA 307
Cdd:cd06113 262 --VKDWTDEDEVraylrkilnkeafDKSGLIYGMGHAVYTLSDPRAVVLKKYARSLAKEK-GREEEFALYERIERLAPEV 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 308 FG-----SKGIYPNTDYFSGIVYMSIGFPLrnNIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVYVG 372
Cdd:cd06113 339 IAeergiGKTVCANVDFYSGFVYKMLGIPQ--ELYTPLFAVARIVGWCAHRIEELLNSGRIIRPAYKYVG 406
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
6-384 |
3.30e-53 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 182.41 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 6 EISKGLEDVNIK--WTRLTTI---------DGNK----GILRYGGYSVEDIIASGAQD-----EEIQYLFLYGNLPTEQE 65
Cdd:PRK14032 28 DVKRGLRNEDGTgvLVGLTNIgdvhgyeidDGEKipdeGKLYYRGYDIKDLVNGFLKEkrfgfEEVAYLLLFGELPTKEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 66 LRKYKETVQKGYKIPD-FVINAIRQLPresdavamqmaavaamaaseTKFKWNK----------------DTDRD----V 124
Cdd:PRK14032 108 LAEFTELLGDYRELPDgFTRDMILKAP--------------------SKDIMNSlarsvlalysyddnpdDTSIDnvlrQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 125 AAEMIGRMSAITV---NVYRHIMN---MPAELPKPSDSYAESFLNAAFG-RKATKEEIDAMNTALILYTDHEV-PASTTA 196
Cdd:PRK14032 168 SISLIARFPTLAVyayQAYRHYHDgksLYIHPPKPELSTAENILYMLRPdNKYTELEARLLDLALVLHAEHGGgNNSTFT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 197 GLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDpaMVEKWFNDN--------IING----KKRLM-GFGH 263
Cdd:PRK14032 248 TRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKE--NVKDWEDEDeiadyltkILNKeafdKSGLIyGMGH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 264 RVYKTYDPRAKIFKGIAEKLSSKKpEVHKVYEIATKLEDFGIKAFG-----SKGIYPNTDYFSGIVYMSIGFPlrNNIYT 338
Cdd:PRK14032 326 AVYTISDPRAVILKKFAEKLAKEK-GREEEFNLYEKIEKLAPELIAeergiYKGVSANVDFYSGFVYDMLGIP--EELYT 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 499203056 339 ALFALSRVTGWQAHFIEYVEEQQRLIRPRAVYVGPaERKYVPIAER 384
Cdd:PRK14032 403 PLFAIARIVGWSAHRIEELVNGGKIIRPAYKSVLE-RREYVPLEER 447
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
151-377 |
1.10e-44 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 157.82 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 151 PKPSDSYAESFLNAAFGR---KATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAA 227
Cdd:PRK12350 128 PQREIDHAATILERFMGRwrgEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 228 EAAIAQFDEIKDPAMVEKWFnDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKpevhkvYEIATKLEDFGIKA 307
Cdd:PRK12350 208 ARVLPMLDAVERTGDARGWV-KGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGAPR------YEVAEAVEQAALAE 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 308 FGSKG----IYPNTDYFSGIVYMSIGFPlrNNIYTALFALSRVTGWQAHfieyVEEQQ---RLIRPRAVYVGPAERK 377
Cdd:PRK12350 281 LRERRpdrpLETNVEFWAAVLLDFAGVP--AHMFTAMFTCGRTAGWSAH----ILEQKrtgRLVRPSARYVGPAPRS 351
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
10-385 |
8.83e-34 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 130.26 E-value: 8.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIDGNKGIlRYGGYSVEDII-----ASGAQD---EEIQYLFLYGNLPTEQELRKYKETVQKGYKIPD 81
Cdd:PRK09569 41 GARDIRSLVTDISYLDPQEGI-RFRGKTIPETFealpkAPGSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 82 FVINAIRQLPRESD--------AVAMQMAAVAAMAASETKFkwNKDTDRDVAAE----MIGRMSAITVNVYRHIMNMPAE 149
Cdd:PRK09569 120 YVIDAIRALPRDSHpmvmlsvgILAMQRESKFAKFYNEGKF--NKMDAWEYMYEdasdLVARIPVIAAYIYNLKYKGDKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 150 LP-KPSDSYAESF---LNAAfgrkatKEEIDAMNTALILYTDHE---VPASTTAgLVAvSTLSDMYSGITAALAALKGPL 222
Cdd:PRK09569 198 IPsDPELDYGANFahmIGQP------KPYKDVARMYFILHSDHEsgnVSAHTTH-LVA-SALSDAYYSYSAGLNGLAGPL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 223 HGGAAEAA---IAQF-----DEIKDPAMVEKWFNDNIINGKKrLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKP---EVH 291
Cdd:PRK09569 270 HGLANQEVlgwIQQFqeklgGEEPTKEQVEQALWDTLNAGQV-IPGYGHAVLRKTDPRYTAQREFCLKHLPDDPlfkLVA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 292 KVYEIATK-LEDFGiKAfgsKGIYPNTDYFSGIVYMSIGFPlRNNIYTALFALSRVTGWQAHFIEYVEEQQRLIRPRAVY 370
Cdd:PRK09569 349 MIFEVAPGvLTEHG-KT---KNPWPNVDAQSGVIQWYYGVK-EWDFYTVLFGVGRALGVMANITWDRGLGYAIERPKSVT 423
|
410
....*....|....*
gi 499203056 371 VGPAErKYVPIAERK 385
Cdd:PRK09569 424 TEMLE-KWAAEGGRK 437
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
176-372 |
3.22e-33 |
|
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: 125.07 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 176 DAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIINGk 255
Cdd:cd06102 99 DLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRG- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 256 KRLMGFGHRVYKTYDPRAkifkgiAEKLSSKKPEVHKVYEIATKLEDFGIKAFGSKgiyPNTDYfsGIVYMSIGFPLRNN 335
Cdd:cd06102 178 EALPGFGHPLYPDGDPRA------AALLAALRPLGPAAPPAARALIEAARALTGAR---PNIDF--ALAALTRALGLPAG 246
|
170 180 190
....*....|....*....|....*....|....*..
gi 499203056 336 IYTALFALSRVTGWQAHFIEYVeEQQRLIRPRAVYVG 372
Cdd:cd06102 247 AAFALFALGRSAGWIAHALEQR-AQGKLIRPRARYVG 282
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
10-348 |
2.80e-29 |
|
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: 117.40 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 10 GLEDVNIKWTRLTTIDGNKGIlRYGGYSVEDIIA--SGAQD------EEIQYLFLYGNLPTEQELRKYKETVQKGYKIPD 81
Cdd:cd06103 39 GMRGMKGLVYETSVLDPDEGI-RFRGKTIPECQEllPKADGggeplpEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 82 FVINAIRQLPRESdAVAMQMAAVAAMAASETKF-------KWNKDTDRDVAAE----MIGRMSAITVNVYRHIMNmPAEL 150
Cdd:cd06103 118 HVVKMIDNLPRNL-HPMTQLSAAILALQSESKFakayaegKINKTTYWEYVYEdamdLIAKLPVVAAKIYRRKYR-KGGE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 151 PKPSDS---YAESFlnAAFGRKATKEEIDAMNTALILYTDHE---VPASTTAgLVAvSTLSDMYSGITAALAALKGPLHG 224
Cdd:cd06103 196 IGAIDSkldWSANF--AHMLGYEDEEFTDLMRLYLTLHSDHEggnVSAHTSH-LVG-SALSDPYLSFSAALNGLAGPLHG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 225 GAAEAA---IAQFDEIKDPAM----VEKwFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPE---VHKVY 294
Cdd:cd06103 272 LANQEVlkwLLKMQKELGKDVsdeeLEK-YIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALKHLPDDPLfklVAQCY 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499203056 295 EIATKLedfgIKAFGS-KGIYPNTDYFSGIVYMSIGfpLRN-NIYTALFALSRVTG 348
Cdd:cd06103 351 KIIPGV----LKEHGKvKNPYPNVDAHSGVLLQHYG--MTEpQYYTVLFGVSRALG 400
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
22-348 |
9.51e-23 |
|
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: 99.12 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 22 TTIDGNKGIlRYGGYSVED---IIASGAQDEEIQ-----YLFLYGNLPTEQELRKY-KETVQKGyKIPDFVINAIRQLPR 92
Cdd:cd06106 51 SVLDAEEGI-RFHGKTIPEcqkELPKAPIGGEMLpesmlWLLLTGKVPTFEQARGLsKELAERG-KLPHYIEKLLDSLPK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 93 eSDAVAMQMAAVAAMAASETKFKWN-----------KDTDRDvAAEMIGRMSAITVNVYRHIMNMPAELPK--PSDSYAE 159
Cdd:cd06106 129 -TLHPMTQLSIGVAALNHDSKFAAAyekgikkteywEPTLED-SLNLIARLPALAARIYRNVYGEGHGLGKidPEVDWSY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 160 SFLNAaFGRKATKEEIDAMNTALILYTDHE---VPASTTAgLVAvSTLSDMYSGITAALAALKGPLHGGAAE-------- 228
Cdd:cd06106 207 NFTSM-LGYGDNLDFVDLLRLYIALHGDHEggnVSAHTTH-LVG-SALSDPYLSYSAGLMGLAGPLHGLAAQevlrwile 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 229 -----AAIAQFDEIKDPAmvekWfndNIINGKKRLMGFGHRVYKTYDPRakiFKGIAEkLSSKKPE---------VHKVY 294
Cdd:cd06106 284 mqkniGSKATDQDIRDYL----W---KTLKSGRVVPGYGHAVLRKPDPR---FTALME-FAQTRPElendpvvqlVQKLS 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 499203056 295 EIATK-LEDFGikafGSKGIYPNTDYFSGIVYMSIGF--PLrnnIYTALFALSRVTG 348
Cdd:cd06106 353 EIAPGvLTEHG----KTKNPFPNVDAASGVLFYHYGIreFL---YYTVIFGVSRALG 402
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
166-362 |
5.23e-21 |
|
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: 90.70 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 166 FGRKATKEEIDAMNTALILYTDH--EVPASTTAGLVAVSTLSDMYSGITAALAALkGPLHGGAAEAAIAQFDEIKD---- 239
Cdd:cd06100 22 KGRLPTPYEARLLEALLVALADHgpATPSAHAARLTASAGPEDLQSAVAAGLLGI-GDRFGGAGEGAARLFKEAVDsgda 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 240 -PAMVEKWFNDnIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLsskkPEVHKVYEIATKLEDFGIKAFGSKgiYP-NT 317
Cdd:cd06100 101 lDAAAAEFVAE-YRAAKKRIPGFGHPVHKNPDPRVPRLLELAREL----GPAGPHLDYALAVEKALTAAKGKP--LPlNV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499203056 318 DYFSGIVYMSIGFPLRnnIYTALFALSRVTGWQAHfieYVEEQQR 362
Cdd:cd06100 174 DGAIAAILLDLGFPPG--ALRGLFVLGRSPGLIAH---ALEEKRL 213
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
156-377 |
6.55e-18 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 82.61 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 156 SYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALkGPLHGGAAEAAIAQFD 235
Cdd:PRK06224 36 SFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 236 EIKDPAMVEKWFNDNIING-------KKRLMGFGHRVYKTYDPRAKIFKGIAEKLSskkpeVHKVY-EIATKLEDFGIKA 307
Cdd:PRK06224 115 EIAAAADAGADLDAAARAIvaeyraaGKRVPGFGHPLHKPVDPRAPRLLALAREAG-----VAGRHcRLAEALEAALAAA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499203056 308 FGsKGIYPNTDYFSGIVYMSIGFPLRnnIYTALFALSRVTGWQAHfieYVEEQQRLIRPRAV--------YVGPAERK 377
Cdd:PRK06224 190 KG-KPLPLNVDGAIAAILADLGFPPA--LARGLFVISRAAGLVAH---VWEELQQPIGFRIWdpaeeaveYTGPPPRE 261
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
24-354 |
1.90e-15 |
|
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: 77.41 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 24 IDGNKGIlRYGGYSVEDI-----IASGAQD---EEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPrESD 95
Cdd:cd06105 53 LDPEEGI-RFRGLSIPECqkllpKAPGGEEplpEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFP-TNL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 96 AVAMQMAAVAAMAASETKFK--WNKDTDRDV--------AAEMIGRMSAITVNVYRHIMNMPAELPK-PSDSYAESFLNA 164
Cdd:cd06105 131 HPMSQLSAAITALNSESKFAkaYAEGIHKSKyweyvyedSMDLIAKLPCVAAKIYRNLYRGGKIIAIdSNLDWSANFANM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 165 -AFGRKATKEeidAMNTALILYTDHE---VPASTTAgLVAvSTLSDMYSGITAALAALKGPLHGGAAEAAIAQF----DE 236
Cdd:cd06105 211 lGYTDPQFTE---LMRLYLTIHSDHEggnVSAHTTH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtklqKE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499203056 237 IKDPAMVEK-----WfndNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPE---VHKVYEIATK-LEDFGiKA 307
Cdd:cd06105 286 VGKDVSDEQlreyvW---KTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLfklVSQLYKIVPPvLTEQG-KA 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499203056 308 fgsKGIYPNTDYFSGIVYMSIGFPlRNNIYTALFALSRVTGWQAHFI 354
Cdd:cd06105 362 ---KNPWPNVDAHSGVLLQYYGLT-EMNYYTVLFGVSRALGVLSQLI 404
|
|
| |
