|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-418 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 941.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 1 MTDQSATIKI--GDKSVDLAVKSGTIGPSVIDIGALYKNTASFTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLA 78
Cdd:PRK05614 1 MADKKATLTLngGEASVELPILKGTLGPDVIDIRKLYGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 79 EHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQR 158
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 159 MVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTST 238
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 239 VRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARAKDKNDPFRLMGFGHRVYKNYDPRAKI 318
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 319 MQKTTHEVLGELGIkDDPLLEVAMELERIALTDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWN 398
Cdd:PRK05614 321 MRETCHEVLKELGL-NDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWN 399
|
410 420
....*....|....*....|
gi 502303569 399 EMIEDPEQRIGRPRQLYVGE 418
Cdd:PRK05614 400 EMHSDPEQKIGRPRQLYTGY 419
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
12-423 |
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: 819.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 12 DKSVDLAVKSGTIGPSVIDIGALYKNTASFTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLL 91
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKQTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 92 YGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPT 171
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 172 LAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 251
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 252 CIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELG 331
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 332 IKDDPLLEVAMELERIALTDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRP 411
Cdd:TIGR01798 321 LHDDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGRP 400
|
410
....*....|..
gi 502303569 412 RQLYVGEPKRDY 423
Cdd:TIGR01798 401 RQLYTGETQRDY 412
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
17-417 |
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: 816.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 17 LAVKSGTIGPSVIDIGALYKNTASFTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELP 96
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 97 TTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMA 176
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 177 YKYHIGQPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAG 256
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 257 IACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGiKDDP 336
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELG-KDDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 337 LLEVAMELERIALTDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRPRQLYV 416
Cdd:cd06114 320 LLEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYT 399
|
.
gi 502303569 417 G 417
Cdd:cd06114 400 G 400
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
38-429 |
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: 669.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 38 TASFTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQ 117
Cdd:COG0372 8 RAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 118 MSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDItDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASN 197
Cdd:COG0372 88 VKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDI-DPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 198 FLRMCFAVpceeyVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLT 277
Cdd:COG0372 167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 278 EIGTVDRIPEYVARAKDKndPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDEYFIEK 357
Cdd:COG0372 242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG--DDPLLEIAEELEEVALEDEYFIEK 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303569 358 KLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:COG0372 318 KLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRAD--NRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
41-417 |
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: 612.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 41 FTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSR 120
Cdd:cd06107 3 RVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 121 FFTGFRRDAHPMAVMCGCVGALSAFYHDSTDIT-------DPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLD 193
Cdd:cd06107 83 LIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHtgdlyqnNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRANLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 194 YASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAAL 273
Cdd:cd06107 163 YIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 NMLTEIGTVDRIPEYVARAKDKNdpFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELgiKDDPLLEVAMELERIALTDEY 353
Cdd:cd06107 243 KMLREIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEV--EKDPLLKVAMELERIALEDEY 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303569 354 FIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRPRQLYVG 417
Cdd:cd06107 319 FVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
46-412 |
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: 551.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 46 GFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGF 125
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 126 RRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAv 205
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 206 pceeYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRI 285
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 286 PEYVARAKDKNDpFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDEYFIEKKLYPNIDF 365
Cdd:pfam00285 236 EEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELAEEGG--DDPLLELAEELEEVAPEDLYFVEKNLYPNVDF 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502303569 366 YSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPR 412
Cdd:pfam00285 313 YSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLAD--NRIIRPR 357
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
42-426 |
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: 541.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 42 TYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRF 121
Cdd:cd06116 4 TYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 122 FTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRM 201
Cdd:cd06116 84 MDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNFLSM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 202 CFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGT 281
Cdd:cd06116 164 LFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 282 VDRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDEYFIEKKLYP 361
Cdd:cd06116 244 PKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATG--RNPLLDIAVELEKIALEDEYFISRKLYP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 362 NIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRPRQLYVGEPKRDYIPV 426
Cdd:cd06116 320 NVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
42-429 |
0e+00 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 534.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 42 TYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRF 121
Cdd:PLN02456 63 TVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 122 FTGFRRDAHPMAVMCGCVGALSAFYHDSTDI-------TDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDY 194
Cdd:PLN02456 143 IDALPHDAHPMTQLVSGVMALSTFSPDANAYlrgqhkyKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 195 ASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVR-LAGSSGANPFACIAAGIACLWGPAHGGANEAAL 273
Cdd:PLN02456 223 AENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 NMLTEIGTVDRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDEY 353
Cdd:PLN02456 303 KMLKEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIREFALEVFKHVG--DDPLFKVASALEEVALLDEY 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303569 354 FIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PLN02456 379 FKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-415 |
0e+00 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) 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: 507.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 45 PGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTG 124
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 125 FRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVAsLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFA 204
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARDKSPEARYEKA-IRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 205 VPceeyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDR 284
Cdd:cd06118 160 EE-----PDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 285 IPEYVarAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALtdEYFIEKKLYPNID 364
Cdd:cd06118 235 VEAYI--WKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG--DDKLFEIAEELEEIAL--EVLGEKGIYPNVD 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502303569 365 FYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPeQRIGRPRQLY 415
Cdd:cd06118 309 FYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENN-QRLIRPRAEY 358
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
30-425 |
3.83e-171 |
|
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: 485.41 E-value: 3.83e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 30 DIGALYKNTASFTYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVT 109
Cdd:cd06115 12 KIKAGKDDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 110 HHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDST------DITDPHQRMVAS-LRMIAKMPTLAAMAYKYHIG 182
Cdd:cd06115 92 QHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEANpalagqDIYKNKQVRDKQiVRILGKAPTIAAAAYRRRAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 183 QPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWG 262
Cdd:cd06115 172 RPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 263 PAHGGANEAALNMLTEIGTVDRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGIkdDPLLEVAM 342
Cdd:cd06115 252 PLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGK--DPLIEIAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 343 ELERIALTDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEQRIGRPRQLYVGEPKRD 422
Cdd:cd06115 328 ALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLYTGVWLRH 407
|
...
gi 502303569 423 YIP 425
Cdd:cd06115 408 YVP 410
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
43-426 |
5.40e-127 |
|
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: 371.76 E-value: 5.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 43 YDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFF 122
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 123 TGFRRDAHPMAVMCGCVGALSAFYHDST-DITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRM 201
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPKPEvLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 202 CFAvpcEEyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGT 281
Cdd:cd06112 161 LFG---EE--PDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 282 VDRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGiKDDPLLEVAMELERIALtdEYFIEKKLYP 361
Cdd:cd06112 236 PENVKAYLDKKLANKQ--KIWGFGHRVYKTKDPRATILQKLAEDLFAKMG-ELSKLYEIALEVERLCE--ELLGHKGVYP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 362 NIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPV 426
Cdd:cd06112 311 NVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGD--NRIFRPTQIYIGEIDRKYVPL 373
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
43-429 |
1.41e-126 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 370.83 E-value: 1.41e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 43 YDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFF 122
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 123 TGFRRDAHPMAVMCGCVGALSAFYHDsTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMC 202
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSR-RALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 203 FavpceEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTV 282
Cdd:PRK14036 163 T-----EREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 283 DRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGIkdDPLLEVAMELERIAltDEYFIEKKLYPN 362
Cdd:PRK14036 238 ENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFGH--DEYYEIALELERVA--EERLGPKGIYPN 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303569 363 IDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PRK14036 312 VDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGA--NRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-415 |
2.94e-123 |
|
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: 358.16 E-value: 2.94e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 45 PGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPttvqkkdfdyrvthhtmvheqmsrfftg 124
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 125 frrdahpmavmcgcvgalsafyhdstditdphqrmvaslrmiakmptlaamaykyhigqpfvypkndlDYASNFLRMCFA 204
Cdd:cd06101 53 --------------------------------------------------------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 205 VPceeyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDR 284
Cdd:cd06101 65 EE-----PDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 285 IPEYVARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDEYFieKKLYPNID 364
Cdd:cd06101 140 EPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG--LDPMFELAAELEKIAPEVLYE--KKLYPNVD 215
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502303569 365 FYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPeQRIGRPRQLY 415
Cdd:cd06101 216 FYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDG-QRIIRPRAEY 265
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
52-429 |
3.39e-117 |
|
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: 346.66 E-value: 3.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 52 SCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHP 131
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 132 MAVMCGCVGALSAFYHDSTDITDPHQRMVASlRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAvpcEEyv 211
Cdd:TIGR01800 88 MDVLRTAVSYLGALDPEKFGHTPEEARDIAI-RLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHG---EE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 212 VNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVAR 291
Cdd:TIGR01800 162 PTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 292 AKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTdeyfiEKKLYPNIDFYSGITL 371
Cdd:TIGR01800 242 ALENKE--RIMGFGHRVYKTYDPRAKILKEYAKKLSAKEG--SSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303569 372 KALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:TIGR01800 313 YMMGIPTDLFTPIFAMSRVTGWTAHIIEQVEN--NRLIRPRADYVGPEERKYVPIEER 368
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
54-429 |
3.16e-116 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 344.68 E-value: 3.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 54 ESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMA 133
Cdd:NF041157 14 YTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 134 VMCGCVGALSAFYHDSTDITDPHQRmvaSLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFA-VPCEEYVv 212
Cdd:NF041157 94 MMETAFSALASIENYKWNKENDREK---ALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATFGrKPSEEEI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 213 npvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARa 292
Cdd:NF041157 170 -----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNE- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 293 KDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGIKDdpLLEVAMELERIALtdEYFIEKKLYPNIDFYSGITLK 372
Cdd:NF041157 244 NIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKK--YLEIAEKLEELGI--KHFGSKGIYPNTDFYSGIVFY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303569 373 ALGFPTTMFTVLFALARTVGWIAQWNEMIEDpEQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:NF041157 320 SLGFPVYMFTSLFALSRVLGWLAHIIEYVEE-QHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
193-415 |
1.02e-104 |
|
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: 309.27 E-value: 1.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 193 DYASNFLRMCFAvpcEEyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAA 272
Cdd:cd06099 1 SYAENFLYMLGG---EE--PDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 273 LNMLTEIGTVDRIPEYVARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTDE 352
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDG--DDPMFELAAELEKIAEEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303569 353 YFieKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPeQRIGRPRQLY 415
Cdd:cd06099 154 YE--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDN-FKIIRPRSEY 213
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
53-417 |
2.51e-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: 308.43 E-value: 2.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 53 CESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPM 132
Cdd:cd06110 9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 133 AVMCGCVGALSAfYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCF-AVPCEEYV 211
Cdd:cd06110 89 DVLRTAVSALAL-YDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTgEKPSEEAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 212 vnpvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVAR 291
Cdd:cd06110 168 ------RAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 292 AKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIAltdeyFIEKKLYPNIDFYSGITL 371
Cdd:cd06110 242 KLANKE--KIMGFGHRVYKTGDPRAKHLREMSRRLGKETG--EPKWYEMSEAIEQAM-----RDEKGLNPNVDFYSASVY 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502303569 372 KALGFPTTMFTVLFALARTVGWIAQWNEMIEDPeqRIGRPRQLYVG 417
Cdd:cd06110 313 YMLGIPVDLFTPIFAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
55-429 |
1.70e-95 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 291.65 E-value: 1.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 55 SKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAV 134
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 135 MCGCVGALSAFYHDST-DITDphqRMVAsLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFA-VPCEEYVv 212
Cdd:PRK14037 96 MEAAFAALASIDKNFKwKEND---KEKA-ISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFArEPTAEEI- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 213 npvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVara 292
Cdd:PRK14037 171 -----KAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWF--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 293 KDK--NDPFRLMGFGHRVYKNYDPRAKIMqKTTHEVLGELGIKDDPLLEVAMELERIALtdEYFIEKKLYPNIDFYSGIT 370
Cdd:PRK14037 243 NDKiiNGKKRLMGFGHRVYKTYDPRAKIF-KELAETLIERNSEAKKYFEIAQKLEELGI--KQFGSKGIYPNTDFYSGIV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303569 371 LKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpEQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PRK14037 320 FYALGFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
54-429 |
3.70e-88 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 272.67 E-value: 3.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 54 ESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDF-DYRVTHHTM---VHEQMSRFFTgfrRDA 129
Cdd:NF041301 16 ESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFsDAMAAEREVddgVLETVRALAA---ADE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 130 HPMAVMCGCVGALSAfYHDSTDITDPHQRMVA---SLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMcfaVP 206
Cdd:NF041301 93 EPMAALRTAVSMLSA-YDPDADDADPTDREANlrkGRRITAKIPTILAAFARLRDGEDPVEPREDLSHAANFLYM---LN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 207 CEEyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIP 286
Cdd:NF041301 169 GEE--PDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 287 -EYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEvLGELGiKDDPLLEVAMELErialtdEYFIEKK-LYPNID 364
Cdd:NF041301 247 vEWVKDALEEGR--RVPGFGHRVYNVKDPRAKILGEKSEE-LGEAA-GDTKWYEYSVAIE------EYMTEEKgLAPNVD 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 365 FYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:NF041301 317 FYSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQYED--NRLIRPRARYVGPKDREFVPLDER 379
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
54-422 |
1.42e-86 |
|
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: 268.12 E-value: 1.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 54 ESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMA 133
Cdd:cd06111 10 TTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 134 VMCGCVGALSAFyHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFA-VPCEEYVv 212
Cdd:cd06111 90 VLRTAVSVLGAE-DSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGeVPSPEVV- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 213 npvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARA 292
Cdd:cd06111 168 -----RAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 293 KDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVlgeLGIKDDPLLEVAMEleriALTDEYFIEKKLYPNIDFYSGITLK 372
Cdd:cd06111 243 LARKE--KVMGFGHRVYKSGDSRVPTMEKALRRV---AAVHDGQKWLAMYD----ALEDAMVAAKGIKPNLDFPAGPAYY 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 502303569 373 ALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRD 422
Cdd:cd06111 314 LMGFDIDFFTPIFVMARITGWTAHIMEQRAD--NALIRPLSEYNGPEQRP 361
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
46-429 |
2.03e-84 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 262.77 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 46 GFTSTASCESKITYIDGDEgvLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGF 125
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 126 RRD-AHPMAVMCGCVGALSAFYHDSTDITDpHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCF- 203
Cdd:PRK14035 84 STDhVHPMTALRTSVSYLAHFDPDAEEESD-EARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 204 AVPCEEYVvnpvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVD 283
Cdd:PRK14035 163 ELPTDIEV------EAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 284 RIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTdeyfiEKKLYPNI 363
Cdd:PRK14035 237 DVDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRKITKGTG--REELFEMSVKIEKRMKE-----EKGLIPNV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303569 364 DFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PRK14035 308 DFYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKD--NRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
67-425 |
4.04e-83 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 259.50 E-value: 4.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 67 LLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFy 146
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 147 HDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCF-AVPCEEYVvnpvlsRAMDRIFI 225
Cdd:PRK14033 112 DPEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFgEVPEPEVV------RAFEVSLI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 226 LHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVARAKDKNDpfRLMGFG 305
Cdd:PRK14033 186 LYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKE--KVMGFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 306 HRVYKNYDPRAKIMQKTTHEVLGELGIKDdpLLEVAMELERiALTDeyfiEKKLYPNIDFYSGITLKALGFPTTMFTVLF 385
Cdd:PRK14033 264 HRVYKHGDSRVPTMKAALRRVAAVRDGQR--WLDIYEALEK-AMAE----ATGIKPNLDFPAGPAYYLMGFDIDFFTPIF 336
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502303569 386 ALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIP 425
Cdd:PRK14033 337 VMSRITGWTAHIMEQRAS--NALIRPLSEYNGPEQREVPP 374
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
46-429 |
1.32e-80 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 253.15 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 46 GFTSTASCESKItyIDGdegVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGF 125
Cdd:PRK14034 9 GVVATTSSVSSI--IDD---TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 126 RRD-AHPMAVMCGCVGALsAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMcfa 204
Cdd:PRK14034 84 DLKkVHPMSVLRTAISML-GLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYM--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 205 VPCEEyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDR 284
Cdd:PRK14034 160 LNGEE--PDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 285 IPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTdeyfiEKKLYPNID 364
Cdd:PRK14034 238 VESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKRLTVLLG--EEKWYNMSIKIEEIVTK-----EKGLPPNVD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 365 FYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PRK14034 309 FYSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYEN--NRLIRPRADYVGPTHQVYVPIEER 371
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
54-417 |
9.94e-78 |
|
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: 244.91 E-value: 9.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 54 ESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFdyrvthHTMVHEQMSRFF--TGFRRDAHP 131
Cdd:cd06109 10 ETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEF------RAALAAARALPDvvAALLPALAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 132 MAVMCGCVGALSAfYHDSTDITDphqrmvaSLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFA-VPCEEY 210
Cdd:cd06109 84 LDPMDALRALLAL-LPDSPDLAT-------ALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGePPSEAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 211 VvnpvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVA 290
Cdd:cd06109 156 V------RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 291 RAKDKNDpfRLMGFGHRVYKNYDPRAKIMQktthEVLGELGiKDDPLLEVAMELER--IALTDEYFIEKKLYPNIDFYSG 368
Cdd:cd06109 230 EALARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLG-APDERLEFAEAVEQaaLALLREYKPGRPLETNVEFYTA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502303569 369 ITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVG 417
Cdd:cd06109 303 LLLEALGLPREAFTPTFAAGRTAGWTAHVLEQART--GRLIRPQSRYVG 349
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
54-426 |
1.85e-71 |
|
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: 229.11 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 54 ESKITYIdGDEGVLLH-RGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPM 132
Cdd:cd06108 10 QTAISTV-GKGGKGLTyRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 133 AVM---CGCVGALSAfyhdstDITDPHQRMVAsLRMIAKMPtlAAMAYKYHI---GQPFVYPKNDLDYASNFLRMCFAVP 206
Cdd:cd06108 89 DVMrtgCSMLGCLEP------ENEFSQQYEIA-IRLLAIFP--SILLYWYHYshsGKRIETETDEDSIAGHFLHLLHGKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 207 CEEYVVnpvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIP 286
Cdd:cd06108 160 PGELEI-----KAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 287 EYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTThEVLGELGiKDDPLLEVAMELERIALTdeyfiEKKLYPNIDFY 366
Cdd:cd06108 235 QGLLEKLERKE--LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEG-GDPLLYQISERIEEVMWE-----EKKLFPNLDFY 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 367 SGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPV 426
Cdd:cd06108 306 SASAYHFCGIPTELFTPIFVMSRVTGWAAHIMEQRAN--NRLIRPSADYIGPEPRPFVPI 363
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
42-418 |
1.52e-67 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 219.21 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 42 TYDPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRF 121
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 122 FTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVAsLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRM 201
Cdd:PRK12349 84 LKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSRA-YKLLSKVPNIVANSYHILNNEEPIEPLKELSYSANFLYM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 202 cfavpCEEYVVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGT 281
Cdd:PRK12349 163 -----LTGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 282 VDRIPEYVAR---AKDKndpfrLMGFGHRVY-KNYDPRAKIMQktthEVLGELGIK--DDPLLEVAMELERIALTdeyfi 355
Cdd:PRK12349 238 VEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMK----EALKQLCDVkgDYTLYEMCEAGEKIMEK----- 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303569 356 EKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGE 418
Cdd:PRK12349 304 EKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHAN--NRLFRPRVNYIGE 364
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
67-429 |
7.46e-63 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 207.47 E-value: 7.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 67 LLHRGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDfdYRVTHHTM---------VHEQMSRfftgfrrDAHPMAVMCG 137
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAA--YKTKLKALrglpaavktVLEAIPA-------AAHPMDVMRT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 138 CVGALSAFYHDSTDITDPHQRMVASlRMIAKMPtlAAMAYKYHIGQPFVYPKNDLDYAS---NFLRMCFAV-PCEEYVvn 213
Cdd:PRK12351 103 GVSVLGCLLPEKEDHNFSGARDIAD-RLLASLG--SILLYWYHYSHNGRRIEVETDDDSiggHFLHLLHGKkPSESWV-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 214 pvlsRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDR----IPEYV 289
Cdd:PRK12351 178 ----KAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEaeadIRRRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 290 ARaKDKndpfrLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTdeyfiEKKLYPNIDFYSGI 369
Cdd:PRK12351 254 EN-KEV-----VIGFGHPVYTISDPRNKVIKEVAKKLSKEAG--DTKLYDIAERLETVMWE-----EKKMFPNLDWFSAV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 370 TLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPVSKR 429
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQD--NKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
63-429 |
9.61e-62 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 206.29 E-value: 9.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 63 DEGVLLHRGYPIEQLAE-------HGdFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEqmsrfftGFRRD------- 128
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNgflkekrFG-FEEVAYLLLFGELPTKEELAEFTELLGDYRELPD-------GFTRDmilkaps 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 129 AHPMAVMCGCVGALSAfYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYK----YHIGQPFV--YPKNDLDYASNFLRMC 202
Cdd:PRK14032 136 KDIMNSLARSVLALYS-YDDNPDDTSIDNVLRQSISLIARFPTLAVYAYQayrhYHDGKSLYihPPKPELSTAENILYML 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 203 faVPCEEYvvNPVLSRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEI-- 279
Cdd:PRK14032 215 --RPDNKY--TELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIke 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 280 -----GTVDRIPEYVARAKDKnDPF----RLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGIKDDplLEVAMELERIA-- 348
Cdd:PRK14032 291 nvkdwEDEDEIADYLTKILNK-EAFdksgLIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEE--FNLYEKIEKLApe 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 349 -LTDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPEqRIGRPRQLYVGEPkRDYIPVS 427
Cdd:PRK14032 368 lIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGG-KIIRPAYKSVLER-REYVPLE 445
|
..
gi 502303569 428 KR 429
Cdd:PRK14032 446 ER 447
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
63-417 |
2.16e-61 |
|
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: 204.42 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 63 DEGVLLHRGYPIEQLA----EHGDFL--EVCYLLLYGELPTTVQKKDFDYRVTHHtmvhEQMSRFFTgfrRD-------A 129
Cdd:cd06113 34 CPGKLYYRGYDVEDLVngaqKENRFGfeETAYLLLFGYLPNKEELEEFCEILSSY----RTLPDNFV---EDvilkapsK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 130 HPMAVMCGCVGALSAfYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYK----YHIGQPFV--YPKNDLDYASNFLRMCf 203
Cdd:cd06113 107 DIMNKLQRSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrhYYDGESLYihHPQPELSTAENILSML- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 204 aVPCEEYvvNPVLSRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEI--- 279
Cdd:cd06113 185 -RPDKKY--TELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIken 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 280 ----GTVDRIPEYVARAKDK--NDPFRLM-GFGHRVYKNYDPRAKIMQKTTHEVLGELGIKDDplLEVAMELERIA---L 349
Cdd:cd06113 262 vkdwTDEDEVRAYLRKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEE--FALYERIERLApevI 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303569 350 TDEYFIEKKLYPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDpEQRIGRPRQLYVG 417
Cdd:cd06113 340 AEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLN-SGRIIRPAYKYVG 406
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
44-417 |
1.90e-57 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 192.49 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 44 DPGFTSTASCESKITYIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGEL-PTTVQKKDFDYRVThhtmvheqmsrff 122
Cdd:PRK12350 2 VPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRFgPGLPPAEPFPLPVH------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 123 TG-FRRDAHPMAVMCGCVGALSAFYhDSTDITDpHQRMVASLRMIAkmPTLAAMAYKyhIGQPFVyPKNDLDYASNFLRM 201
Cdd:PRK12350 69 LGdARVDVQAALAMLAPVWGFRPLL-DIDDLTA-RLDLARASVMAL--SAVAQSARG--IGQPAV-PQREIDHAATILER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 202 CFAVPCEEyvVNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGT 281
Cdd:PRK12350 142 FMGRWRGE--PDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVER 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 282 VDRIPEYVARAKDKNDpfRLMGFGHRVYKNYDPRAKIMQKTthevLGELGikdDPLLEVAMELERIALTD--EYFIEKKL 359
Cdd:PRK12350 220 TGDARGWVKGALDRGE--RLMGFGHRVYRAEDPRARVLRAT----AKRLG---APRYEVAEAVEQAALAElrERRPDRPL 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303569 360 YPNIDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEmiedpEQRIG---RPRQLYVG 417
Cdd:PRK12350 291 ETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILE-----QKRTGrlvRPSARYVG 346
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
62-426 |
1.37e-53 |
|
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: 182.74 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 62 GDEGVLLH-RGYPIEQLAEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVG 140
Cdd:cd06117 17 GRSGNDLHyRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 141 ALSAFYHDSTDITDPHQRMVASlRMIAKMPTLAAMAYKY-HIGQPFVYPKNDLDYASNFLRMCFAVPCEEyvvnpVLSRA 219
Cdd:cd06117 97 VLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYsHNGKRIEVETDDDSIGGHFLHLLHGEKPSE-----SWEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 220 MDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRiPEYVARAKDKNDPF 299
Cdd:cd06117 171 MHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADE-AEADIRRRVENKEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 300 rLMGFGHRVYKNYDPRAKIMQKTTHEVLGELGikDDPLLEVAMELERIALTdeyfiEKKLYPNIDFYSGITLKALGFPTT 379
Cdd:cd06117 250 -VIGFGHPVYTIADPRNQVIKEVAKQLSKEGG--DMKMFDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTA 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502303569 380 MFTVLFALARTVGWIAQWNEMIEDpeQRIGRPRQLYVGEPKRDYIPV 426
Cdd:cd06117 322 MFTPLFVIARTTGWSAHIIEQRQD--GKIIRPSANYTGPEDLKFVPI 366
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
212-417 |
8.80e-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: 135.85 E-value: 8.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 212 VNPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAALNMLTEIGTVDRIPEYVAR 291
Cdd:cd06102 93 LDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 292 AKDKNDPfrLMGFGHRVYKNYDPRAKimqktthEVLGELGIKDDPLLEVAMELERIA--LTDEyfiekklYPNIDFYSGI 369
Cdd:cd06102 173 RLRRGEA--LPGFGHPLYPDGDPRAA-------ALLAALRPLGPAAPPAARALIEAAraLTGA-------RPNIDFALAA 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502303569 370 TLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPeQRIgRPRQLYVG 417
Cdd:cd06102 237 LTRALGLPAGAAFALFALGRSAGWIAHALEQRAQG-KLI-RPRARYVG 282
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
57-417 |
1.48e-35 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 136.03 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 57 ITYIDGDEGvLLHRGYPIEQL---------AEHGDFLEVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRR 127
Cdd:PRK09569 52 ISYLDPQEG-IRFRGKTIPETfealpkapgSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 128 DAHPMAVMCGCVGAL------SAFYHDS-----TDITDPHQRmvaSLRMIAKMPTLAAMAYKYHIGQPFVYPKN-DLDYA 195
Cdd:PRK09569 131 DSHPMVMLSVGILAMqreskfAKFYNEGkfnkmDAWEYMYED---ASDLVARIPVIAAYIYNLKYKGDKQIPSDpELDYG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 196 SNFLRMcFAVPcEEYvvnpvlSRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAAL- 273
Cdd:PRK09569 208 ANFAHM-IGQP-KPY------KDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 ---NMLTEIGTVDRIPEYVARA-KDKNDPFRLM-GFGHRVYKNYDPRAKIMQKTTHEVLgelgiKDDPLLEVAMELERIA 348
Cdd:PRK09569 280 wiqQFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHL-----PDDPLFKLVAMIFEVA 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 349 ---LTdEYFIEKKLYPNIDFYSGITLKALGFPTTMF-TVLFALARTVGWIAQ--WNEMIEDPeqrIGRPRQLYVG 417
Cdd:PRK09569 355 pgvLT-EHGKTKNPWPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANitWDRGLGYA---IERPKSVTTE 425
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
57-405 |
2.54e-34 |
|
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: 132.42 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 57 ITYIDGDEGVLLhRGYPIEQLAEHGDFLE---------VCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRR 127
Cdd:cd06103 50 TSVLDPDEGIRF-RGKTIPECQELLPKADgggeplpegLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 128 DAHPMAVMCGCVGAL---SAF---YHDSTDITDPHQRMVA--SLRMIAKMPTLAAMAY--KYHIGQPFVYPKNDLDYASN 197
Cdd:cd06103 129 NLHPMTQLSAAILALqseSKFakaYAEGKINKTTYWEYVYedAMDLIAKLPVVAAKIYrrKYRKGGEIGAIDSKLDWSAN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 198 FLRMcFAVPCEEYVvnpvlsRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAAL--- 273
Cdd:cd06103 209 FAHM-LGYEDEEFT------DLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLkwl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 -NMLTEIG---TVDRIPEYVaraKDKNDPFRLM-GFGHRVYKNYDPRakimqkttHEVLGELG---IKDDPLLE-VAMEL 344
Cdd:cd06103 282 lKMQKELGkdvSDEELEKYI---WDTLNSGRVVpGYGHAVLRKTDPR--------FTCQREFAlkhLPDDPLFKlVAQCY 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303569 345 ERI-ALTDEYFIEKKLYPNIDFYSGITLKALGFP-TTMFTVLFALARTVGWIAQ--WNEM----IEDPE 405
Cdd:cd06103 351 KIIpGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQlvWSRAlglpIERPK 419
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
58-414 |
3.96e-29 |
|
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: 117.99 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 58 TYIDGDEGVLLHrGYPIEQLAEH-------GDFL--EVCYLLLYGELPTTVQKKDFDYRVTHHTMVHEQMSRFFTGFRRD 128
Cdd:cd06106 51 SVLDAEEGIRFH-GKTIPECQKElpkapigGEMLpeSMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 129 AHPMAVMCGCVGALSafyHDS------------TDITDPhqRMVASLRMIAKMPTLAAMAYK--YHIGQPFVYPKNDLDY 194
Cdd:cd06106 130 LHPMTQLSIGVAALN---HDSkfaaayekgikkTEYWEP--TLEDSLNLIARLPALAARIYRnvYGEGHGLGKIDPEVDW 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 195 ASNFLRMCfavpceEYVVNPVLSRAMDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANEAAL 273
Cdd:cd06106 205 SYNFTSML------GYGDNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 N----MLTEIGTVDRIPEYVARAKDKNDPFRLM-GFGHRVYKNYDPRAKIMQ---KTTHEvlgelgIKDDPLLEVAMELE 345
Cdd:cd06106 279 RwileMQKNIGSKATDQDIRDYLWKTLKSGRVVpGYGHAVLRKPDPRFTALMefaQTRPE------LENDPVVQLVQKLS 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303569 346 RIA---LTdEYFIEKKLYPNIDFYSGITLKALGFPTTMF-TVLFALARTVGWIAQ--WNEMIEDPeqrIGRPRQL 414
Cdd:cd06106 353 EIApgvLT-EHGKTKNPFPNVDAASGVLFYHYGIREFLYyTVIFGVSRALGPLTQlvWDRILGLP---IERPKSL 423
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
60-414 |
7.10e-29 |
|
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: 117.08 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 60 IDGDEGVLLhRGYPI--------------EQLAEhGDFlevcYLLLYGELPTTVQ----KKDFDYRVTHHTMVHEQMSRF 121
Cdd:cd06105 53 LDPEEGIRF-RGLSIpecqkllpkapggeEPLPE-GLF----WLLLTGEVPTKEQvsalSKEWAARAALPSHVVTMLDNF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 122 FTgfrrDAHPMAVMCGCVGAL---SAF-----------------YHDSTDItdphqrmvaslrmIAKMPTLAAMAYK--Y 179
Cdd:cd06105 127 PT----NLHPMSQLSAAITALnseSKFakayaegihkskyweyvYEDSMDL-------------IAKLPCVAAKIYRnlY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 180 HIGQpFVYPKNDLDYASNFLRMC-FAvpceeyvvNPVLSRAMdRIFI-LHADHEQ-NASTSTVRLAGSSGANPFACIAAG 256
Cdd:cd06105 190 RGGK-IIAIDSNLDWSANFANMLgYT--------DPQFTELM-RLYLtIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 257 IACLWGPAHGGANEAALNMLT----EIG---TVDRIPEYVarAKDKNDPFRLMGFGHRVYKNYDPRAKIMQktthevlgE 329
Cdd:cd06105 260 MNGLAGPLHGLANQEVLVWLTklqkEVGkdvSDEQLREYV--WKTLNSGRVVPGYGHAVLRKTDPRYTCQR--------E 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 330 LGIK---DDPLLEVAMELERIA---LTdEYFIEKKLYPNIDFYSGITLKALGFpTTM--FTVLFALARTVGWIAQ--WNE 399
Cdd:cd06105 330 FALKhlpNDPLFKLVSQLYKIVppvLT-EQGKAKNPWPNVDAHSGVLLQYYGL-TEMnyYTVLFGVSRALGVLSQliWDR 407
|
410
....*....|....*
gi 502303569 400 MIEDPeqrIGRPRQL 414
Cdd:cd06105 408 ALGLP---LERPKSV 419
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
217-412 |
1.36e-20 |
|
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: 89.93 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 217 SRAMDRIFILHADH-EQNASTSTVRLAGSSGANPF-ACIAAGiACLWGPAHGGANEAALNMLTEI----GTVDRIP-EYV 289
Cdd:cd06100 31 ARLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAG-LLGIGDRFGGAGEGAARLFKEAvdsgDALDAAAaEFV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 290 ARAKDKNdpFRLMGFGHRVYKNYDPRAKIMqkttHEVLGELGIkDDPLLEVAMELERIALTDEyfiEKKLYPNIDFYSGI 369
Cdd:cd06100 110 AEYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGP-AGPHLDYALAVEKALTAAK---GKPLPLNVDGAIAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502303569 370 TLKALGFPTTMFTVLFALARTVGWIAQWNEmiedpEQRIGRPR 412
Cdd:cd06100 180 ILLDLGFPPGALRGLFVLGRSPGLIAHALE-----EKRLGQPL 217
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
213-422 |
2.06e-18 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 84.54 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 213 NPVLSRAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIaCLWGPAHGGANEAALNMLTEI-------GTVDRI 285
Cdd:PRK06224 51 TPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGL-LALGSVHGGAGEQAAELLQEIaaaadagADLDAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 286 PEYVA---RAKDKndpfRLMGFGHRVYKNYDPRA-KIMqktthEVLGELGIKDDP---LLEVAMELERIAltdeyfiEKK 358
Cdd:PRK06224 130 ARAIVaeyRAAGK----RVPGFGHPLHKPVDPRApRLL-----ALAREAGVAGRHcrlAEALEAALAAAK-------GKP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303569 359 LYPNIDfysGIT---LKALGFPTTMFTVLFALARTVGWIAQ-WNEMIEDPEQRIGRPRQL---YVGEPKRD 422
Cdd:PRK06224 194 LPLNVD---GAIaaiLADLGFPPALARGLFVISRAAGLVAHvWEELQQPIGFRIWDPAEEaveYTGPPPRE 261
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
194-394 |
5.03e-05 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 45.58 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 194 YASNFLRMCFAVpCEEYvvNPVLSRAMDRIfilhadheqnaststvrLAGSSGANPFACIAAGIACLwGPAHGGANEAAL 273
Cdd:PLN02522 398 YCTKFIEMCIML-CADH--GPCVSGAHNTI-----------------VTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303569 274 NMLTEIGTVDRIP-EYVARAKDKNdpFRLMGFGHRVYK--NYDPRAKIMQKTTHEVLgelgiKDDPLLEVAMELERIALT 350
Cdd:PLN02522 457 RYFKDAYDRGLTPyEFVEGMKKKG--IRVPGIGHRIKSrdNRDKRVELLQKYARTHF-----PSVKYMEYAVQVETYTLS 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303569 351 DEyfieKKLYPNIDFYSGITLKALGFPTTMFTV--------------LFALARTVGWI 394
Cdd:PLN02522 530 KA----NNLVLNVDGAIGSLFLDLLAGSGMFTKqeideiveigylngLFVLARSIGLI 583
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
313-374 |
1.03e-03 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 40.14 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303569 313 DPRAKIMQKTTHEVLGELGIKDDPLLEVameLERIALTDEYFIEKKLYPNID---FYS---GITLKAL 374
Cdd:cd01878 132 DPDREEQIETVEEVLKELGADDIPIILV---LNKIDLLDDEELEERLRAGRPdavFISaktGEGLDLL 196
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