|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-417 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 906.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 1 MADLKAKLELP-GNDSIELPVKQGSAGFDVIDISKL-GSKGYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLA 78
Cdd:PRK05614 1 MADKKATLTLNgGEASVELPILKGTLGPDVIDIRKLyGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 79 VDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDVNDPRHR 158
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 159 EIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTST 238
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 239 VRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKV 318
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 319 MRETCHEVLKELKVQDPLLDVAMELERIALEDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKE 398
Cdd:PRK05614 321 MRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNE 400
|
410
....*....|....*....
gi 499384458 399 MLDQPGHKISRPRQLYTGE 417
Cdd:PRK05614 401 MHSDPEQKIGRPRQLYTGY 419
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
13-422 |
0e+00 |
|
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: 782.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 13 NDSIELPVKQGSAGFDVIDISKLGS-KGYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLL 91
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKqTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 92 YGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDVNDPRHREIAAYRLVSKMPT 171
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 172 IAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 251
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 252 CIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKEL- 330
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 331 KVQDPLLDVAMELERIALEDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGHKISRP 410
Cdd:TIGR01798 321 LHDDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGRP 400
|
410
....*....|..
gi 499384458 411 RQLYTGETARDF 422
Cdd:TIGR01798 401 RQLYTGETQRDY 412
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
18-416 |
0e+00 |
|
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: 778.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 18 LPVKQGSAGFDVIDISKLGSK-GYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELP 96
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKtGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 97 TKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDVNDPRHREIAAYRLVSKMPTIAAMC 176
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 177 YKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAG 256
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 257 IASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDPL 336
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 337 LDVAMELERIALEDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGHKISRPRQLYTG 416
Cdd:cd06114 321 LEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYTG 400
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
33-428 |
0e+00 |
|
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: 639.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 33 SKLGSKGYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHT 112
Cdd:COG0372 3 SEIDIRAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 113 MVHEQIAFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDvNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDL 192
Cdd:COG0372 83 ELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD-IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 193 SYAGNFLSMMFAVpceeyKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEAC 272
Cdd:COG0372 162 SYAENFLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 273 LQMLEEIGSVDRIPEFIARAKDKndPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKvQDPLLDVAMELERIALEDEY 352
Cdd:COG0372 237 LEMLEEIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEY 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499384458 353 FISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDqpGHKISRPRQLYTGETARDFVDLDKR 428
Cdd:COG0372 314 FIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRA--DNRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
39-416 |
0e+00 |
|
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: 614.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 39 GYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQI 118
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 119 AFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDV-------NDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRND 191
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAhtgdlyqNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 192 LSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEA 271
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 272 CLQMLEEIGSVDRIPEFIARAKDKNdpFRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKvQDPLLDVAMELERIALEDE 351
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEVE-KDPLLKVAMELERIALEDE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499384458 352 YFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGHKISRPRQLYTG 416
Cdd:cd06107 318 YFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
46-411 |
0e+00 |
|
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: 527.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 46 GFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGF 125
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 126 RRDAHPMAMLCGVTGALSAFYQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAv 205
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 206 pceeYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRI 285
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 286 PEFIARAKDKNDpFRLMGFGHRVYKNFDPRAKVMRETCHEVLKElKVQDPLLDVAMELERIALEDEYFISKKLYPNVDFY 365
Cdd:pfam00285 236 EEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELAEE-GGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499384458 366 SGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLdqPGHKISRPR 411
Cdd:pfam00285 314 SGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQL--ADNRIIRPR 357
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
39-423 |
0e+00 |
|
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: 522.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 39 GYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQI 118
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 119 AFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNF 198
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 199 LSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEE 278
Cdd:cd06116 161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 279 IGSVDRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLkELKVQDPLLDVAMELERIALEDEYFISKKL 358
Cdd:cd06116 241 IGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVF-EATGRNPLLDIAVELEKIALEDEYFISRKL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499384458 359 YPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGHKISRPRQLYTGETARDFV 423
Cdd:cd06116 318 YPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYV 382
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
17-428 |
0e+00 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 521.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 17 ELPVKQG--SAGFDVIDISKLG-SKGYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYG 93
Cdd:PLN02456 35 ESPLSELgpVQAERLKKIKAGKdDLGLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 94 ELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLCGVTGALSAFYQDSLDV-------NDPRHREIAAYRLV 166
Cdd:PLN02456 115 NLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYlrgqhkyKSWEVRDEDIVRLI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 167 SKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVR-LAGSS 245
Cdd:PLN02456 195 GKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 246 GANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHE 325
Cdd:PLN02456 275 GVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIREFALE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 326 VLKeLKVQDPLLDVAMELERIALEDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGH 405
Cdd:PLN02456 353 VFK-HVGDDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLPDE 431
|
410 420
....*....|....*....|...
gi 499384458 406 KISRPRQLYTGETARDFVDLDKR 428
Cdd:PLN02456 432 RIMRPKQVYTGEWLRHYCPKAER 454
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-414 |
4.82e-174 |
|
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: 490.58 E-value: 4.82e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 45 PGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRG 124
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 125 FRRDAHPMAMLCGVTGALSAFYQDSLDVNdPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFA 204
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARDKS-PEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 205 VpceeyKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDR 284
Cdd:cd06118 160 E-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 285 ipEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKElKVQDPLLDVAMELERIALEDEYFisKKLYPNVDF 364
Cdd:cd06118 235 --VEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEE-KGDDKLFEIAEELEEIALEVLGE--KGIYPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499384458 365 YSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPgHKISRPRQLY 414
Cdd:cd06118 310 YSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENN-QRLIRPRAEY 358
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
36-424 |
5.45e-164 |
|
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: 467.30 E-value: 5.45e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 36 GSKGYFTFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVH 115
Cdd:cd06115 18 DDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 116 EQIAFFFRGFRRDAHPMAMLCGVTGALSAFY---------QDSLDVNDPRHREIaaYRLVSKMPTIAAMCYKYSSGQPFV 186
Cdd:cd06115 98 TGVLDMIKSFPHDAHPMGMLVSAISALSAFHpeanpalagQDIYKNKQVRDKQI--VRILGKAPTIAAAAYRRRAGRPPN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 187 YPRNDLSYAGNFLSMMFAVPCEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHG 266
Cdd:cd06115 176 LPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 267 GANEACLQMLEEIGSVDRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLkELKVQDPLLDVAMELERI 346
Cdd:cd06115 256 GANEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVF-EIVGKDPLIEIAVALEKA 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499384458 347 ALEDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGHKISRPRQLYTGETARDFVD 424
Cdd:cd06115 333 ALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLYTGVWLRHYVP 410
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
43-425 |
2.28e-122 |
|
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: 360.20 E-value: 2.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 43 FDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFF 122
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 123 RGFRRDAHPMAMLCGVTGALSAFY-QDSLDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSM 201
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYpKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 202 MFavpceEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGS 281
Cdd:cd06112 161 LF-----GEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 282 VDRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDPLLDVAMELERIALedEYFISKKLYPN 361
Cdd:cd06112 236 PENVKAYLDKKLANKQ--KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCE--ELLGHKGVYPN 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499384458 362 VDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDqpGHKISRPRQLYTGETARDFVDL 425
Cdd:cd06112 312 VDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLG--DNRIFRPTQIYIGEIDRKYVPL 373
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-414 |
1.20e-119 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and 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: 348.92 E-value: 1.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 45 PGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYldlcylllygelptkeqyaefvhtvkthtmvhEQIAFFFrg 124
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSF--------------------------------EEVAYLL-- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 125 frrdahpmamlcgvtgalsafyqdsldvndprhreiaayrLVSKMPtiaamcykyssgqpfvyprndlSYAGNFLSMMFA 204
Cdd:cd06101 47 ----------------------------------------LTGELP----------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 205 VpceeyKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDR 284
Cdd:cd06101 65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 285 IPEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVqDPLLDVAMELERIALEDEYFisKKLYPNVDF 364
Cdd:cd06101 140 EPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGL-DPMFELAAELEKIAPEVLYE--KKLYPNVDF 216
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499384458 365 YSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpGHKISRPRQLY 414
Cdd:cd06101 217 YSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQRED-GQRIIRPRAEY 265
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
43-428 |
2.60e-117 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 347.33 E-value: 2.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 43 FDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFF 122
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 123 RGFRRDAHPMAMLCGVTGALSAFYQDSlDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMM 202
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRR-ALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 203 FavpceEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSV 282
Cdd:PRK14036 163 T-----EREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 283 DRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKvQDPLLDVAMELERIAleDEYFISKKLYPNV 362
Cdd:PRK14036 238 ENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFG-HDEYYEIALELERVA--EERLGPKGIYPNV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499384458 363 DFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGETARDFVDLDKR 428
Cdd:PRK14036 313 DFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGA--NRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
193-414 |
3.99e-111 |
|
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: 325.45 E-value: 3.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 193 SYAGNFLSMMFAVpceeyKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEAC 272
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 273 LQMLEEIGSVDRIPEFIARAKDKNDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKElKVQDPLLDVAMELERIALEDEY 352
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKE-DGDDPMFELAAELEKIAEEVLY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499384458 353 FisKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpGHKISRPRQLY 414
Cdd:cd06099 155 E--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLED-NFKIIRPRSEY 213
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
52-428 |
1.01e-110 |
|
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: 330.10 E-value: 1.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 52 SCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHP 131
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 132 MAMLCGVTGALSAFyQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAvpceeYK 211
Cdd:TIGR01800 88 MDVLRTAVSYLGAL-DPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHG-----EE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 212 VNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIAR 291
Cdd:TIGR01800 162 PTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 292 AKDKNDpfRLMGFGHRVYKNFDPRAKVMRETChEVLKELKVQDPLLDVAMELERIALEdeyfiSKKLYPNVDFYSGIIMK 371
Cdd:TIGR01800 242 ALENKE--RIMGFGHRVYKTYDPRAKILKEYA-KKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYY 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 499384458 372 AIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGETARDFVDLDKR 428
Cdd:TIGR01800 314 MMGIPTDLFTPIFAMSRVTGWTAHIIEQVEN--NRLIRPRADYVGPEERKYVPIEER 368
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
54-428 |
4.32e-103 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 310.79 E-value: 4.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMA 133
Cdd:NF041157 14 YTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 134 MLCGVTGALSAFYqdSLDVNDPRHREIAAyRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVn 213
Cdd:NF041157 94 MMETAFSALASIE--NYKWNKENDREKAL-KIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATFGRKPSEEEI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 214 piveRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARaK 293
Cdd:NF041157 170 ----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNE-N 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 294 DKNDPFRLMGFGHRVYKNFDPRAKVMRETChEVLKELKVQDPLLDVAMELERIALedEYFISKKLYPNVDFYSGIIMKAI 373
Cdd:NF041157 245 IINGKKRLMGFGHRVYKTYDPRAKIFKEYA-EKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPNTDFYSGIVFYSL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499384458 374 GIPTSMFTVLFALSRTVGWIAHWKEMLDQPgHKISRPRQLYTGETARDFVDLDKR 428
Cdd:NF041157 322 GFPVYMFTSLFALSRVLGWLAHIIEYVEEQ-HRLIRPRALYVGPEKRDFVPIDER 375
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
53-416 |
1.43e-102 |
|
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: 308.82 E-value: 1.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 53 CESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPM 132
Cdd:cd06110 9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 133 AMLCGVTGALSAFYQDSLDVN-DPRHREiaAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMF-AVPceey 210
Cdd:cd06110 89 DVLRTAVSALALYDPEADDMSrEANLRK--AIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTgEKP---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 211 kvNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIA 290
Cdd:cd06110 163 --SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 291 RAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEvLKELKVQDPLLDVAmelerIALEDEYFISKKLYPNVDFYSGIIM 370
Cdd:cd06110 241 DKLANKE--KIMGFGHRVYKTGDPRAKHLREMSRR-LGKETGEPKWYEMS-----EAIEQAMRDEKGLNPNVDFYSASVY 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499384458 371 KAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPghKISRPRQLYTG 416
Cdd:cd06110 313 YMLGIPVDLFTPIFAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
57-428 |
2.06e-86 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 268.15 E-value: 2.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 57 ITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLC 136
Cdd:PRK14037 18 LTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGLME 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 137 GVTGALSAFYQDSLdvNDPRHREIAAyRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYKVNpiv 216
Cdd:PRK14037 98 AAFAALASIDKNFK--WKENDKEKAI-SIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTAEEIK--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 217 erAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIaraKDK- 295
Cdd:PRK14037 172 --AMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWF---NDKi 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 296 -NDPFRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDPLLDVAMELERIALEDeyFISKKLYPNVDFYSGIIMKAIG 374
Cdd:PRK14037 247 iNGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALG 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499384458 375 IPTSMFTVLFALSRTVGWIAHWKEMLDQPgHKISRPRQLYTGETARDFVDLDKR 428
Cdd:PRK14037 325 FPVYMFTALFALSRTLGWLAHIIEYVEEQ-HRLIRPRALYVGPEHREYVPIDKR 377
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
54-428 |
5.25e-84 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 261.88 E-value: 5.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGF-RRDAHPM 132
Cdd:NF041301 16 ESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFSDAMAAEREVDDGVLETVRALaAADEEPM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 133 AMLCGVTGALSAfYQDSLDVNDPRHREIA---AYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAvpcEE 209
Cdd:NF041301 96 AALRTAVSMLSA-YDPDADDADPTDREANlrkGRRITAKIPTILAAFARLRDGEDPVEPREDLSHAANFLYMLNG---EE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 210 ykVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIP-EF 288
Cdd:NF041301 172 --PDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDPvEW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 289 IARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEvLKELKVQDPLLDVAMELErialedEYFISKK-LYPNVDFYSG 367
Cdd:NF041301 250 VKDALEEGR--RVPGFGHRVYNVKDPRAKILGEKSEE-LGEAAGDTKWYEYSVAIE------EYMTEEKgLAPNVDFYSA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499384458 368 IIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDqpGHKISRPRQLYTGETARDFVDLDKR 428
Cdd:NF041301 321 STYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQYE--DNRLIRPRARYVGPKDREFVPLDER 379
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
46-428 |
3.78e-81 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 254.30 E-value: 3.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 46 GFLATASCESAITYIDGDQgiLLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGF 125
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 126 RRD-AHPMAMLCGVTGALSAFYQDSLDVNDPRHREiAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMF- 203
Cdd:PRK14035 84 STDhVHPMTALRTSVSYLAHFDPDAEEESDEARYE-RAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 204 AVPCEeykvnpIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVD 283
Cdd:PRK14035 163 ELPTD------IEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 284 RIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKvQDPLLDVAMELERIALEDeyfisKKLYPNVD 363
Cdd:PRK14035 237 DVDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRKITKGTG-REELFEMSVKIEKRMKEE-----KGLIPNVD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499384458 364 FYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTGETARDFVDLDKR 428
Cdd:PRK14035 309 FYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILE--QYKDNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
46-428 |
8.38e-79 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 248.53 E-value: 8.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 46 GFLATASCESAItyIDGdqgILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGF 125
Cdd:PRK14034 9 GVVATTSSVSSI--IDD---TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 126 RRD-AHPMAMLCGVTGALsAFYQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFA 204
Cdd:PRK14034 84 DLKkVHPMSVLRTAISML-GLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 205 vpcEEykVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDR 284
Cdd:PRK14034 163 ---EE--PDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 285 IPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEvLKELKVQDPLLDVAMELERIALEDeyfisKKLYPNVDF 364
Cdd:PRK14034 238 VESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKR-LTVLLGEEKWYNMSIKIEEIVTKE-----KGLPPNVDF 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499384458 365 YSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGETARDFVDLDKR 428
Cdd:PRK14034 310 YSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYEN--NRLIRPRADYVGPTHQVYVPIEER 371
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
54-416 |
2.89e-77 |
|
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: 243.75 E-value: 2.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFvhtvktHTMVHEQIAFFFR--GFRRDAHP 131
Cdd:cd06109 10 ETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEF------RAALAAARALPDVvaALLPALAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 132 MAMLCGVTGALSAfYQDSLDVNDprhreiaAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFAVPCEEYK 211
Cdd:cd06109 84 LDPMDALRALLAL-LPDSPDLAT-------ALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGEPPSEAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 212 VnpiveRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIAR 291
Cdd:cd06109 156 V-----RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 292 AKDKNDpfRLMGFGHRVYKNFDPRAKVMRetchEVLKELKVQDPLLDVAMELERIALE--DEYFISKKLYPNVDFYSGII 369
Cdd:cd06109 231 ALARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLGAPDERLEFAEAVEQAALAllREYKPGRPLETNVEFYTALL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499384458 370 MKAIGIPTSMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTG 416
Cdd:cd06109 305 LEALGLPREAFTPTFAAGRTAGWTAHVLE--QARTGRLIRPQSRYVG 349
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
54-421 |
4.22e-75 |
|
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: 238.46 E-value: 4.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMA 133
Cdd:cd06111 10 TTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 134 ML---CGVTGALSAFYQDSldvnDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMFA-VPcee 209
Cdd:cd06111 90 VLrtaVSVLGAEDSETDDS----SPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGeVP--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 210 ykvNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFI 289
Cdd:cd06111 163 ---SPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 290 ARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDplldvAMELERIaLEDEYFISKKLYPNVDFYSGII 369
Cdd:cd06111 240 LDALARKE--KVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQK-----WLAMYDA-LEDAMVAAKGIKPNLDFPAGPA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499384458 370 MKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGETARD 421
Cdd:cd06111 312 YYLMGFDIDFFTPIFVMARITGWTAHIMEQRAD--NALIRPLSEYNGPEQRP 361
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
42-417 |
1.01e-72 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 232.69 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 42 TFDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFF 121
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 122 FRGFRRDAHPMAMLCGVTGALSAFYQD----SLDVNdpRHReiaAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGN 197
Cdd:PRK12349 84 LKALPKETHPMDGLRTGVSALAGYDNDiedrSLEVN--KSR---AYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 198 FLSMMfavpcEEYKVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLE 277
Cdd:PRK12349 159 FLYML-----TGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 278 EIGSVDRIPEFIAR---AKDKndpfrLMGFGHRVY-KNFDPRAKVMRETCHEvLKELKVQDPLLDVAMELERIALEDeyf 353
Cdd:PRK12349 234 EAGTVEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMKEALKQ-LCDVKGDYTLYEMCEAGEKIMEKE--- 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499384458 354 isKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGE 417
Cdd:PRK12349 305 --KGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHAN--NRLFRPRVNYIGE 364
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
54-425 |
1.73e-68 |
|
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: 221.41 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIdGDQGILLH-RGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPM 132
Cdd:cd06108 10 QTAISTV-GKGGKGLTyRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 133 AMLCGVTGALSAFYQDsldvNDPRHREIAAYRLVSKMPTIAAMCYKYS-SGQPFVYPRNDLSYAGNFLSMMFAvpceeYK 211
Cdd:cd06108 89 DVMRTGCSMLGCLEPE----NEFSQQYEIAIRLLAIFPSILLYWYHYShSGKRIETETDEDSIAGHFLHLLHG-----KK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 212 VNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIAR 291
Cdd:cd06108 160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 292 AKDKNDpfRLMGFGHRVYKNFDPRAKVMRETChEVLKELKVQDPLLDVAMELERIALEdeyfiSKKLYPNVDFYSGIIMK 371
Cdd:cd06108 240 KLERKE--LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSASAYH 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499384458 372 AIGIPTSMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTGETARDFVDL 425
Cdd:cd06108 312 FCGIPTELFTPIFVMSRVTGWAAHIME--QRANNRLIRPSADYIGPEPRPFVPI 363
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
54-423 |
5.10e-68 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 220.59 E-value: 5.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 54 ESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMA 133
Cdd:PRK14033 20 TTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 134 ML---CGVTGALSAFYQDSldvnDPRHREIAAYRLVSKMPTIAAMCYKYSSGQPFVYPRNDLSYAGNFLSMMF-AVPCEE 209
Cdd:PRK14033 100 VVrtaVSYLGAEDPEADDS----SPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFgEVPEPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 210 ykvnpiVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFI 289
Cdd:PRK14033 176 ------VVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 290 ARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDplldvAMELERiALEDEYFISKKLYPNVDFYSGII 369
Cdd:PRK14033 250 RDALARKE--KVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQR-----WLDIYE-ALEKAMAEATGIKPNLDFPAGPA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499384458 370 MKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQpgHKISRPRQLYTGETARDFV 423
Cdd:PRK14033 322 YYLMGFDIDFFTPIFVMSRITGWTAHIMEQRAS--NALIRPLSEYNGPEQREVP 373
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
67-428 |
1.87e-58 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 195.91 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 67 LLHRGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFV----------HTVKThtmVHEQIAfffrgfrRDAHPM-AML 135
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKtklkalrglpAAVKT---VLEAIP-------AAAHPMdVMR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 136 CGVTgALSAFYQDSLDVNDPRHREIAAyRLVSKMPTIAAMCYKYS-SGQPFVYPRNDLSYAGNFLSMMFAV-PCEEYkvn 213
Cdd:PRK12351 102 TGVS-VLGCLLPEKEDHNFSGARDIAD-RLLASLGSILLYWYHYShNGRRIEVETDDDSIGGHFLHLLHGKkPSESW--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 214 pivERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIAR-- 291
Cdd:PRK12351 177 ---VKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRrv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 292 -AKDKndpfrLMGFGHRVYKNFDPRAKVMRETCHEVLKElkVQDPLL-DVAMELERIALEdeyfiSKKLYPNVDFYSGII 369
Cdd:PRK12351 254 eNKEV-----VIGFGHPVYTISDPRNKVIKEVAKKLSKE--AGDTKLyDIAERLETVMWE-----EKKMFPNLDWFSAVS 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499384458 370 MKAIGIPTSMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTGETARDFVDLDKR 428
Cdd:PRK12351 322 YHMMGVPTAMFTPLFVISRTTGWAAHVIE--QRQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
63-428 |
1.94e-54 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 187.03 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 63 DQGILLHRGYPIEQLAVDSDYLD------LCYLLLYGELPTKEQYAEFVHTVKTHTMVHEqiaFFFRGFRRDAHP---MA 133
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNGFLKEKrfgfeeVAYLLLFGELPTKEELAEFTELLGDYRELPD---GFTRDMILKAPSkdiMN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 134 MLCGVTGALSAfYQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYK----YSSGQPFV--YPRNDLSYAGNFLSMMFAvpc 207
Cdd:PRK14032 141 SLARSVLALYS-YDDNPDDTSIDNVLRQSISLIARFPTLAVYAYQayrhYHDGKSLYihPPKPELSTAENILYMLRP--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 208 eEYKVNPIVERAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEI------- 279
Cdd:PRK14032 217 -DNKYTELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIkenvkdw 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 280 GSVDRIPEFIARAKDKnDPF----RLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDPLLDVAMeLERIALE---DEY 352
Cdd:PRK14032 296 EDEDEIADYLTKILNK-EAFdksgLIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEK-IEKLAPEliaEER 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499384458 353 FISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGhKISRPRQLYTGETaRDFVDLDKR 428
Cdd:PRK14032 374 GIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGG-KIIRPAYKSVLER-REYVPLEER 447
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
43-420 |
6.68e-54 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 183.24 E-value: 6.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 43 FDPGFLATASCESAITYIDGDQGILLHRGYPIEQLAVDSDYLDLCYLLLYGE----LPTKEQYAEFVHTVKThtmvheqi 118
Cdd:PRK12350 1 FVPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRfgpgLPPAEPFPLPVHLGDA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 119 afffrgfRRDAHP-MAMLCGVTGalsafYQDSLDVNDPRHRE-IAAyrlVSKMPTIAAMCYKYSSGQPFVyPRNDLSYAG 196
Cdd:PRK12350 73 -------RVDVQAaLAMLAPVWG-----FRPLLDIDDLTARLdLAR---ASVMALSAVAQSARGIGQPAV-PQREIDHAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 197 NFLSMMFAVPCEEykVNPIVERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQML 276
Cdd:PRK12350 137 TILERFMGRWRGE--PDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPML 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 277 EEIGSVDRIPEFIARAKDKNDpfRLMGFGHRVYKNFDPRAKVMRETChevlKELKVqdPLLDVAMELERIALED--EYFI 354
Cdd:PRK12350 215 DAVERTGDARGWVKGALDRGE--RLMGFGHRVYRAEDPRARVLRATA----KRLGA--PRYEVAEAVEQAALAElrERRP 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499384458 355 SKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTGETAR 420
Cdd:PRK12350 287 DRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILE--QKRTGRLVRPSARYVGPAPR 350
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
62-425 |
1.48e-51 |
|
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: 177.34 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 62 GDQGILLH-RGYPIEQLAVDSDYLDLCYLLLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPM-AMLCGVT 139
Cdd:cd06117 17 GRSGNDLHyRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMdVMRTGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 140 gALSAFYQDSLDVNDPRHREIAAyRLVSKMPTIAAMCYKYS-SGQPFVYPRNDLSYAGNFLSMMFAVPCEEykvnpIVER 218
Cdd:cd06117 97 -VLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYShNGKRIEVETDDDSIGGHFLHLLHGEKPSE-----SWEK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 219 AMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFI-ARAKDKNd 297
Cdd:cd06117 170 AMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIrRRVENKE- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 298 pfRLMGFGHRVYKNFDPRAKVMRETCHEVLKELKVQDpLLDVAMELERIALEdeyfiSKKLYPNVDFYSGIIMKAIGIPT 377
Cdd:cd06117 249 --VVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMK-MFDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 499384458 378 SMFTVLFALSRTVGWIAHWKEmlDQPGHKISRPRQLYTGETARDFVDL 425
Cdd:cd06117 321 AMFTPLFVIARTTGWSAHIIE--QRQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
63-410 |
8.02e-51 |
|
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: 176.30 E-value: 8.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 63 DQGILLHRGYPIEQLaVDSDYLDLCYLLL-------YGELPTKEQYAEFVHTVKTHTMVHEqiafffrGFRRD------- 128
Cdd:cd06113 34 CPGKLYYRGYDVEDL-VNGAQKENRFGFEetaylllFGYLPNKEELEEFCEILSSYRTLPD-------NFVEDvilkaps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 129 AHPMAMLCGVTGALSAfYQDSLDVNDPRHREIAAYRLVSKMPTIAAMCYK----YSSGQPFV--YPRNDLSYAGNFLSMM 202
Cdd:cd06113 106 KDIMNKLQRSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrhYYDGESLYihHPQPELSTAENILSML 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 203 faVPCEEYkvNPIVERAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEI-- 279
Cdd:cd06113 185 --RPDKKY--TELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIke 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 280 -----GSVDRIPEFIARAKDK--NDPFRLM-GFGHRVYKNFDPRAKVMRETCHEVLKElKVQDPLLDVAMELERIA---L 348
Cdd:cd06113 261 nvkdwTDEDEVRAYLRKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKE-KGREEEFALYERIERLApevI 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499384458 349 EDEYFISKKLYPNVDFYSGIIMKAIGIPTSMFTVLFALSRTVGWIAHWKEMLDQPGhKISRP 410
Cdd:cd06113 340 AEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSG-RIIRP 400
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
57-416 |
3.34e-47 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 167.62 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 57 ITYIDGDQGILLhRGYPIEQL------AVDSDYLDLCYL---LLYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRR 127
Cdd:PRK09569 52 ISYLDPQEGIRF-RGKTIPETfealpkAPGSEYPTVESFwyfLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 128 DAHPMAML-CGVT--------------------GALSAFYQDSLDvndprhreiaayrLVSKMPTIAAMCY--KYSSGQP 184
Cdd:PRK09569 131 DSHPMVMLsVGILamqreskfakfynegkfnkmDAWEYMYEDASD-------------LVARIPVIAAYIYnlKYKGDKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 185 fVYPRNDLSYAGNFLSMMfAVPcEEYKvnpiveRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGP 263
Cdd:PRK09569 198 -IPSDPELDYGANFAHMI-GQP-KPYK------DVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 264 AHGGANEACL----QMLEEIGSVDRIPEFIARA-KDKNDPFRLM-GFGHRVYKNFDPRAKVMRETCHEVLKElkvqDPLL 337
Cdd:PRK09569 269 LHGLANQEVLgwiqQFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 338 DVAMELERIA---LEdEYFISKKLYPNVDFYSGIIMKAIGIPTSMF-TVLFALSRTVGWIAH--WKEMLdqpGHKISRPR 411
Cdd:PRK09569 345 KLVAMIFEVApgvLT-EHGKTKNPWPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANitWDRGL---GYAIERPK 420
|
....*
gi 499384458 412 QLYTG 416
Cdd:PRK09569 421 SVTTE 425
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
57-413 |
7.91e-39 |
|
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: 144.75 E-value: 7.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 57 ITYIDGDQGILLhRGYPIEQL------AVDSDYLDLCYLL---LYGELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRR 127
Cdd:cd06103 50 TSVLDPDEGIRF-RGKTIPECqellpkADGGGEPLPEGLFwllLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 128 DAHPMAMLCGvtgALSAFYQDSL--------DVNDPRHREIA---AYRLVSKMPTIAAMCY--KYSSGQPFVYPRNDLSY 194
Cdd:cd06103 129 NLHPMTQLSA---AILALQSESKfakayaegKINKTTYWEYVyedAMDLIAKLPVVAAKIYrrKYRKGGEIGAIDSKLDW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 195 AGNFLSMMfavpceEYKvNPIVERAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACL 273
Cdd:cd06103 206 SANFAHML------GYE-DEEFTDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 274 ----QMLEEIG---SVDRIPEFiarAKDKNDPFRLM-GFGHRVYKNFDPRAKVMRETCHEVLKElkvqDPLLD-VAMELE 344
Cdd:cd06103 279 kwllKMQKELGkdvSDEELEKY---IWDTLNSGRVVpGYGHAVLRKTDPRFTCQREFALKHLPD----DPLFKlVAQCYK 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499384458 345 RI--ALEdEYFISKKLYPNVDFYSGIIMKAIGIP-TSMFTVLFALSRTVGWIAH--WKEMLDQPghkISRPRQL 413
Cdd:cd06103 352 IIpgVLK-EHGKVKNPYPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQlvWSRALGLP---IERPKSM 421
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
217-416 |
9.39e-37 |
|
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: 135.47 E-value: 9.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 217 ERAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQMLEEIGSVDRIPEFIARAKDKN 296
Cdd:cd06102 98 ADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 297 DPfrLMGFGHRVYKNFDPRAKVMRETCHEVLKELkvqDPLLDVAMELERIALEDeyfiskklYPNVDFYSGIIMKAIGIP 376
Cdd:cd06102 178 EA--LPGFGHPLYPDGDPRAAALLAALRPLGPAA---PPAARALIEAARALTGA--------RPNIDFALAALTRALGLP 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499384458 377 TSMFTVLFALSRTVGWIAHWKEMLDQPghKISRPRQLYTG 416
Cdd:cd06102 245 AGAAFALFALGRSAGWIAHALEQRAQG--KLIRPRARYVG 282
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
93-416 |
2.03e-31 |
|
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: 124.40 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 93 GELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAML-CGVTgAL---SAF-----------------YQDSLD 151
Cdd:cd06105 94 GEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLsAAIT-ALnseSKFakayaegihkskyweyvYEDSMD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 152 vndprhreiaayrLVSKMPTIAAMCYK--YSSGQpFVYPRNDLSYAGNFLSMMfavpceEYKVNPIVEraMDRIFI-LHA 228
Cdd:cd06105 173 -------------LIAKLPCVAAKIYRnlYRGGK-IIAIDSNLDWSANFANML------GYTDPQFTE--LMRLYLtIHS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 229 DHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACL----QMLEEIG---SVDRIPEFIarAKDKNDPFR 300
Cdd:cd06105 231 DHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltKLQKEVGkdvSDEQLREYV--WKTLNSGRV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 301 LMGFGHRVYKNFDPRAKVMRETChevLKELKvQDPLLDVAMELERIALE--DEYFISKKLYPNVDFYSGIIMKAIGIpTS 378
Cdd:cd06105 309 VPGYGHAVLRKTDPRYTCQREFA---LKHLP-NDPLFKLVSQLYKIVPPvlTEQGKAKNPWPNVDAHSGVLLQYYGL-TE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499384458 379 M--FTVLFALSRTVGWIAH--WKEMLdqpGHKISRPRQLYTG 416
Cdd:cd06105 384 MnyYTVLFGVSRALGVLSQliWDRAL---GLPLERPKSVSTD 422
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
93-413 |
1.30e-27 |
|
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99859 Cd Length: 428 Bit Score: 113.75 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 93 GELPTKEQYAEFVHTVKTHTMVHEQIAFFFRGFRRDAHPMAMLCGVTGAL----------------SAFYQDSLDvndpr 156
Cdd:cd06106 94 GKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALnhdskfaaayekgikkTEYWEPTLE----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 157 hreiAAYRLVSKMPTIAAMCYKYSSGQ----PFVYPRNDLSYagNFLSMMfavpceEYKVNPIVERAMDRIFILHADHEQ 232
Cdd:cd06106 169 ----DSLNLIARLPALAARIYRNVYGEghglGKIDPEVDWSY--NFTSML------GYGDNLDFVDLLRLYIALHGDHEG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 233 -NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLQ----MLEEIGSVDRIPEFIARAKDKNDPFRLM-GFGH 306
Cdd:cd06106 237 gNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRwileMQKNIGSKATDQDIRDYLWKTLKSGRVVpGYGH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 307 RVYKNFDPRAKVMRETChEVLKELKvQDPLLDVAMELERIA--LEDEYFISKKLYPNVDFYSGIIMKAIGI-PTSMFTVL 383
Cdd:cd06106 317 AVLRKPDPRFTALMEFA-QTRPELE-NDPVVQLVQKLSEIApgVLTEHGKTKNPFPNVDAASGVLFYHYGIrEFLYYTVI 394
|
330 340 350
....*....|....*....|....*....|..
gi 499384458 384 FALSRTVGWIAH--WKEMLDQPghkISRPRQL 413
Cdd:cd06106 395 FGVSRALGPLTQlvWDRILGLP---IERPKSL 423
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
218-398 |
3.07e-24 |
|
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: 99.95 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 218 RAMDRIFILHADH-EQNASTSTVRLAGSSGANPF-ACIAAGIASLwGPAHGGANEACLQMLEEI----GSVDRIP-EFIA 290
Cdd:cd06100 32 RLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgDALDAAAaEFVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 291 RAKDKNdpFRLMGFGHRVYKNFDPRAKVMretcHEVLKELKVQDPLLDVAMELERIALEDeyfiSKKLYP-NVDFYSGII 369
Cdd:cd06100 111 EYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGPAGPHLDYALAVEKALTAA----KGKPLPlNVDGAIAAI 180
|
170 180
....*....|....*....|....*....
gi 499384458 370 MKAIGIPTSMFTVLFALSRTVGWIAHWKE 398
Cdd:cd06100 181 LLDLGFPPGALRGLFVLGRSPGLIAHALE 209
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
218-422 |
7.50e-24 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 99.94 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 218 RAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIASLwGPAHGGANEACLQMLEEI-------GSVDRIPEFIA 290
Cdd:PRK06224 56 RLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaadagADLDAAARAIV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 291 ---RAKDKndpfRLMGFGHRVYKNFDPRAKVMRetchEVLKELKVQDPLLDVAMELERIALEDEyfiSKKLYPNVDFYSG 367
Cdd:PRK06224 135 aeyRAAGK----RVPGFGHPLHKPVDPRAPRLL----ALAREAGVAGRHCRLAEALEAALAAAK---GKPLPLNVDGAIA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499384458 368 IIMKAIGIPTSMFTVLFALSRTVGWIAH-WKEMLDQPGHKISRPRQL---YTGETARDF 422
Cdd:PRK06224 204 AILADLGFPPALARGLFVISRAAGLVAHvWEELQQPIGFRIWDPAEEaveYTGPPPREL 262
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
220-403 |
9.29e-05 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 44.81 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 220 MDRIFILHADHE---QNASTSTVrlAGSSGANPFACIAAGIASLwGPAHGGANEACLQMLEEIGSVDRIP-EFIARAKDK 295
Cdd:PLN02522 403 IEMCIMLCADHGpcvSGAHNTIV--TARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMKKK 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499384458 296 NdpFRLMGFGHRVYK--NFDPRAKVMRETCHEVLKELKVqdplLDVAMELErialedEYFISKK--LYPNVDFYSGIIMK 371
Cdd:PLN02522 480 G--IRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSVKY----MEYAVQVE------TYTLSKAnnLVLNVDGAIGSLFL 547
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499384458 372 AIGIPTSMFTV--------------LFALSRTVGWIAHW--KEMLDQP 403
Cdd:PLN02522 548 DLLAGSGMFTKqeideiveigylngLFVLARSIGLIGHTfdQKRLKQP 595
|
|
| |
