|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-416 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 774.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 1 MTDVK--LEHPGGQLS--MPVNPAVEGPAGIGVGKLLAETGHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELA 76
Cdd:PRK05614 1 MADKKatLTLNGGEASveLPILKGTLGPDVIDIRKLYGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 77 GKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQV 156
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 157 EISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTST 236
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 237 VRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDAASFVRRVKAKEQGVKLMGFGHRVYKNYDPRAA 316
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEI-GSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 317 IVKQAAQDVLSRMAKPDPLLDIAMKLEEIALADDFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWR 396
Cdd:PRK05614 320 IMRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWN 399
|
410 420
....*....|....*....|
gi 2039919926 397 EMINDPETKIGRPRQLYVGS 416
Cdd:PRK05614 400 EMHSDPEQKIGRPRQLYTGY 419
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
15-415 |
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: 744.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 15 MPVNPAVEGPAGIGVGKLLAETGHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELP 94
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 95 TTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEISTVRLMAKVPTIASYA 174
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 175 YKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAG 254
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 255 VHALSGPLHGGANEAVLQMLGAIQADgGDAASFVRRVKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKPDP 334
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSV-GNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 335 LLDIAMKLEEIALADDFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGRPRQLYV 414
Cdd:cd06114 320 LLEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYT 399
|
.
gi 2039919926 415 G 415
Cdd:cd06114 400 G 400
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
36-427 |
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: 635.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 36 TGHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHED 115
Cdd:COG0372 8 RAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 116 FKRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPfDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDN 195
Cdd:COG0372 88 VKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDI-DPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 196 FLRMTFGVpaasyDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLG 275
Cdd:COG0372 167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 276 AIQaDGGDAASFVRRVKAKeqGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIALADDFFVSR 355
Cdd:COG0372 242 EIG-SPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELGD-DPLLEIAEELEEVALEDEYFIEK 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039919926 356 KLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:COG0372 318 KLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRAD--NRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
10-421 |
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: 580.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 10 GGQLSMPVNPAVEGPAGIGVGKLLAETGHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLI 89
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKQTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 90 YGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEISTVRLMAKVPT 169
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 170 IASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFA 249
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 250 SVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDAASFVRRVKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRM 329
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEI-GSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 330 AKPD-PLLDIAMKLEEIALADDFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGR 408
Cdd:TIGR01798 320 GLHDdPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGR 399
|
410
....*....|...
gi 2039919926 409 PRQLYVGSPEREF 421
Cdd:TIGR01798 400 PRQLYTGETQRDY 412
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
37-427 |
0e+00 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 531.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 37 GHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDF 116
Cdd:PLN02456 60 GLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 117 KRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSD-------QVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNT 189
Cdd:PLN02456 140 LDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLRGQhkyksweVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 190 RSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVR-LVGSGQANLFASVSAGVHALSGPLHGGANE 268
Cdd:PLN02456 220 LDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 269 AVLQMLGAI-QADGgdAASFVRRVKAKeqGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIAL 347
Cdd:PLN02456 300 AVLKMLKEIgTVEN--IPEYVEGVKNS--KKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGD-DPLFKVASALEEVAL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 348 ADDFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:PLN02456 375 LDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
44-410 |
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: 529.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 44 GFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGF 123
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 124 PRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGv 203
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 204 paasYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQaDGGD 283
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIG-SPDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 284 AASFVRRVKAKEqGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIALADDFFVSRKLYPNVDF 363
Cdd:pfam00285 235 VEEYIRKVLNKG-KERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGD-DPLLELAEELEEVAPEDLYFVEKNLYPNVDF 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2039919926 364 YTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPR 410
Cdd:pfam00285 313 YSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLAD--NRIIRPR 357
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
37-424 |
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: 513.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 37 GHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDF 116
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 117 KRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNF 196
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 197 LRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGA 276
Cdd:cd06116 161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 277 IqADGGDAASFVRRVKAKEQgvKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIALADDFFVSRK 356
Cdd:cd06116 241 I-GSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATGR-NPLLDIAVELEKIALEDEYFISRK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039919926 357 LYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGRPRQLYVGSPEREFVPI 424
Cdd:cd06116 317 LYPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
37-415 |
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: 512.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 37 GHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDF 116
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 117 KRFFDGFPRDAHPMPVLSSAVSALSTFYQDSLDPF-------DSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNT 189
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHtgdlyqnNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 190 RSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEA 269
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 270 VLQMLGAIqadGG--DAASFVRRVKAKEqgVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIAL 347
Cdd:cd06107 241 ALKMLREI---GTpeNVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEK-DPLLKVAMELERIAL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039919926 348 ADDFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGRPRQLYVG 415
Cdd:cd06107 315 EDEYFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
37-423 |
1.94e-167 |
|
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: 476.16 E-value: 1.94e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 37 GHVTYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDF 116
Cdd:cd06115 21 GLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 117 KRFFDGFPRDAHPMPVLSSAVSALSTFYQDS------LDPFDSDQV-EISTVRLMAKVPTIASYAYKTSIGQPLLYPDNT 189
Cdd:cd06115 101 LDMIKSFPHDAHPMGMLVSAISALSAFHPEAnpalagQDIYKNKQVrDKQIVRILGKAPTIAAAAYRRRAGRPPNLPSQD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 190 RSYVDNFLRMTFGVPAASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEA 269
Cdd:cd06115 181 LSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 270 VLQMLGAIqADGGDAASFVRRVKAKEQgvKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIALAD 349
Cdd:cd06115 261 VLRMLAEI-GTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGK-DPLIEIAVALEKAALSD 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039919926 350 DFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIGRPRQLYVGSPEREFVP 423
Cdd:cd06115 337 EYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLYTGVWLRHYVP 410
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
43-413 |
1.99e-163 |
|
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: 463.61 E-value: 1.99e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 43 PGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDG 122
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 123 FPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEIStVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFG 202
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARDKSPEARYEKA-IRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 203 VPAasydvDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADGG 282
Cdd:cd06118 160 EEP-----DPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 283 DAASFVRRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRmAKPDPLLDIAMKLEEIALADdfFVSRKLYPNVD 362
Cdd:cd06118 235 VEAYIWKKLANKR---RIMGFGHRVYKTYDPRAKILKELAEELAEE-KGDDKLFEIAEELEEIALEV--LGEKGIYPNVD 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 363 FYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPEtKIGRPRQLY 413
Cdd:cd06118 309 FYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQ-RLIRPRAEY 358
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
41-424 |
2.06e-129 |
|
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: 377.92 E-value: 2.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 41 YDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFF 120
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 121 DGFPRDAHPMPVLSSAVSALSTFY-QDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRM 199
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYpKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 200 TFGvpaasYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQA 279
Cdd:cd06112 161 LFG-----EEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 280 DGGDAASFVRRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKPDPLLDIAMKLEEIALadDFFVSRKLYP 359
Cdd:cd06112 236 PENVKAYLDKKLANKQ---KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCE--ELLGHKGVYP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039919926 360 NVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPI 424
Cdd:cd06112 311 NVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGD--NRIFRPTQIYIGEIDRKYVPL 373
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
41-427 |
3.63e-123 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 362.35 E-value: 3.63e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 41 YDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFF 120
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 121 DGFPRDAHPMPVLSSAVSALSTFYQD-SLDpfDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRM 199
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRrALD--DPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 200 TFGvpaasYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqA 279
Cdd:PRK14036 162 LTE-----REPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEI-G 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 280 DGGDAASFV-RRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIalADDFFVSRKLY 358
Cdd:PRK14036 236 SVENVRPYLdERLANKQ---KIMGFGHREYKVKDPRATILQKLAEELFARFGH-DEYYEIALELERV--AEERLGPKGIY 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2039919926 359 PNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:PRK14036 310 PNVDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGA--NRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
50-427 |
1.30e-116 |
|
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: 345.12 E-value: 1.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 50 ACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHP 129
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 130 MPVLSSAVSALSTFyQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAasyd 209
Cdd:TIGR01800 88 MDVLRTAVSYLGAL-DPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGEEP---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 210 vDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDAASFVR 289
Cdd:TIGR01800 163 -TKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEI-GDPDKAEAWIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 290 rvKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIALAddffvSRKLYPNVDFYTGLIY 369
Cdd:TIGR01800 241 --KALENKERIMGFGHRVYKTYDPRAKILKEYAKK-LSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2039919926 370 KAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:TIGR01800 313 YMMGIPTDLFTPIFAMSRVTGWTAHIIEQVEN--NRLIRPRADYVGPEERKYVPIEER 368
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
50-415 |
8.38e-113 |
|
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: 335.01 E-value: 8.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 50 ACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHP 129
Cdd:cd06110 8 AADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 130 MPVLSSAVSALSTFYQDSLDPFDSDQVEIStVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFG-VPaasy 208
Cdd:cd06110 88 MDVLRTAVSALALYDPEADDMSREANLRKA-IRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTGeKP---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 209 dvDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADgGDAASFV 288
Cdd:cd06110 163 --SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSV-DNVAAYV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 289 RrvKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIALADdffvsRKLYPNVDFYTGLI 368
Cdd:cd06110 240 K--DKLANKEKIMGFGHRVYKTGDPRAKHLREMSRR-LGKETGEPKWYEMSEAIEQAMRDE-----KGLNPNVDFYSASV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2039919926 369 YKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPetKIGRPRQLYVG 415
Cdd:cd06110 312 YYMLGIPVDLFTPIFAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
42-427 |
1.25e-112 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 335.44 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 42 DPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFD 121
Cdd:NF041157 4 SKGLENVFIKYTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 122 GFPRDAHPMPVLSSAVSALSTFYQDSLD-PFDSDQVeistVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMT 200
Cdd:NF041157 84 SLPRDSDALAMMETAFSALASIENYKWNkENDREKA----LKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 201 FGVPAASYDVdpafaKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQAD 280
Cdd:NF041157 160 FGRKPSEEEI-----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 281 GGDAASFVRRVKAKEQgvKLMGFGHRVYKNYDPRAAIVKQAAqDVLSRMAKPDPLLDIAMKLEEIALadDFFVSRKLYPN 360
Cdd:NF041157 235 DNVEKWFNENIINGKK--RLMGFGHRVYKTYDPRAKIFKEYA-EKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPN 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2039919926 361 VDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIgRPRQLYVGSPEREFVPIEKR 427
Cdd:NF041157 310 TDFYSGIVFYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEEQHRLI-RPRALYVGPEKRDFVPIDER 375
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
43-413 |
3.01e-108 |
|
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: 320.03 E-value: 3.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 43 PGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPttdqlaaftekvqlhtmlhedfkrffdg 122
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 123 fprdahpmpvlssavsalstfyqdsldpfdsdqveistvrlmakvptiasyayktsigqpllypdntrSYVDNFLRMTFG 202
Cdd:cd06101 53 --------------------------------------------------------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 203 VpaasyDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADGG 282
Cdd:cd06101 65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 283 DAAsFVRRVKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKpDPLLDIAMKLEEIALADDFFvsRKLYPNVD 362
Cdd:cd06101 140 EPA-EAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGL-DPMFELAAELEKIAPEVLYE--KKLYPNVD 215
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 363 FYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPeTKIGRPRQLY 413
Cdd:cd06101 216 FYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDG-QRIIRPRAEY 265
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
53-427 |
9.27e-95 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 289.62 E-value: 9.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 53 SKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKV----QLHTMLHEDFKRFFDgfpRDAH 128
Cdd:NF041301 17 SELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFSDAMaaerEVDDGVLETVRALAA---ADEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 129 PMPVLSSAVSALSTF--YQDSLDPFDSDQVEISTVRLMAKVPTI-ASYAyKTSIGQPLLYPDNTRSYVDNFLRMTFG-VP 204
Cdd:NF041301 94 PMAALRTAVSMLSAYdpDADDADPTDREANLRKGRRITAKIPTIlAAFA-RLRDGEDPVEPREDLSHAANFLYMLNGeEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 205 aasydvDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADGGDA 284
Cdd:NF041301 173 ------DEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 285 ASFVRRvkAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEialaddFFVSRK-LYPNVDF 363
Cdd:NF041301 247 VEWVKD--ALEEGRRVPGFGHRVYNVKDPRAKILGEKSEE-LGEAAGDTKWYEYSVAIEE------YMTEEKgLAPNVDF 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039919926 364 YTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:NF041301 318 YSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQYED--NRLIRPRARYVGPKDREFVPLDER 379
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
191-413 |
4.47e-93 |
|
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: 279.22 E-value: 4.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 191 SYVDNFLRMTFGVpaasyDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAV 270
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 271 LQMLGAIQADGGDAAsFVRRVKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAqDVLSRMAKPDPLLDIAMKLEEIALADD 350
Cdd:cd06099 76 LKMLEEIGTPKNEPA-EAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFA-EELLKEDGDDPMFELAAELEKIAEEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2039919926 351 FFvsRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPeTKIGRPRQLY 413
Cdd:cd06099 154 YE--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDN-FKIIRPRSEY 213
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
53-427 |
1.08e-89 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 276.63 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 53 SKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPV 132
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 133 LSSAVSALSTFYqdslDPF-----DSDQveisTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAAS 207
Cdd:PRK14037 96 MEAAFAALASID----KNFkwkenDKEK----AISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 208 YDVdpafaKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDAASF 287
Cdd:PRK14037 168 EEI-----KAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEI-GDPNNVEMW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 288 VRRvKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKPDPLLDIAMKLEEIALadDFFVSRKLYPNVDFYTGL 367
Cdd:PRK14037 242 FND-KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGI--KQFGSKGIYPNTDFYSGI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 368 IYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPETKIgRPRQLYVGSPEREFVPIEKR 427
Cdd:PRK14037 319 VFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLI-RPRALYVGPEHREYVPIDKR 377
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
65-424 |
8.51e-87 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 269.13 E-value: 8.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 65 LRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPVLSSAVSALSTFY 144
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 145 QDSLDPfDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFGVPAASYDVDpAFakvlDTLLVL 224
Cdd:PRK14033 113 PEADDS-SPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFGEVPEPEVVR-AF----EVSLIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 225 HADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDAASFVRR-VKAKEqgvKLMGF 303
Cdd:PRK14033 187 YAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEI-GDPARAAEWLRDaLARKE---KVMGF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 304 GHRVYKNYDPRAAIVKQAAQDVLSRMAKPDpLLDIAMKLEEIaladdfFVSRK-LYPNVDFYTGLIYKAMGFPTKMFTVL 382
Cdd:PRK14033 263 GHRVYKHGDSRVPTMKAALRRVAAVRDGQR-WLDIYEALEKA------MAEATgIKPNLDFPAGPAYYLMGFDIDFFTPI 335
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2039919926 383 FALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPI 424
Cdd:PRK14033 336 FVMSRITGWTAHIMEQRAS--NALIRPLSEYNGPEQREVPPI 375
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
43-415 |
4.04e-86 |
|
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: 266.48 E-value: 4.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 43 PGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFteKVQLHTMlhedfKRFFDG 122
Cdd:cd06109 1 PGLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEF--RAALAAA-----RALPDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 123 FPR------DAHPMPVLSSAVSALStfyqdsldpfDSDQVEiSTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNF 196
Cdd:cd06109 74 VAAllpalaGLDPMDALRALLALLP----------DSPDLA-TALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 197 LRMTFGVPAasydvDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGA 276
Cdd:cd06109 143 LRMLTGEPP-----SEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 277 IQAdGGDAASFVRRvkAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQdvlsRMAKPDPLLDIAMKLEEIALA--DDFFVS 354
Cdd:cd06109 218 IGT-PENAEAWLRE--ALARGERLMGFGHRVYRVRDPRADVLKAAAE----RLGAPDERLEFAEAVEQAALAllREYKPG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 355 RKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVG 415
Cdd:cd06109 291 RPLETNVEFYTALLLEALGLPREAFTPTFAAGRTAGWTAHVLEQART--GRLIRPQSRYVG 349
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
60-424 |
9.14e-86 |
|
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: 266.09 E-value: 9.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 60 GDAGI-LRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAHPMPVLSSAVS 138
Cdd:cd06108 17 GKGGKgLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 139 ALSTFYQDSldpFDSDQVEIStVRLMAKVPTIASYAYKTSIGQPLLYPD-NTRSYVDNFLRMTFGVPAAsydvdPAFAKV 217
Cdd:cd06108 97 MLGCLEPEN---EFSQQYEIA-IRLLAIFPSILLYWYHYSHSGKRIETEtDEDSIAGHFLHLLHGKKPG-----ELEIKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 218 LDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQaDGGDAASFVR-RVKAKEq 296
Cdd:cd06108 168 MDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-SPEEAEQGLLeKLERKE- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 297 gvKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIaladdFFVSRKLYPNVDFYTGLIYKAMGFPT 376
Cdd:cd06108 246 --LIMGFGHRVYKEGDPRSDIIKKWSKK-LSEEGGDPLLYQISERIEEV-----MWEEKKLFPNLDFYSASAYHFCGIPT 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2039919926 377 KMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPI 424
Cdd:cd06108 318 ELFTPIFVMSRVTGWAAHIMEQRAN--NRLIRPSADYIGPEPRPFVPI 363
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
44-420 |
9.48e-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: 265.81 E-value: 9.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 44 GFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGF 123
Cdd:cd06111 2 GLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 124 PRDAHPMPVLSSAVSALSTFyqdSLDPFDSDQVEI--STVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTF 201
Cdd:cd06111 82 PKNCHPMDVLRTAVSVLGAE---DSETDDSSPDANlaKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 202 G-VPAasydvdPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqAD 280
Cdd:cd06111 159 GeVPS------PEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEI-DD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 281 GGDAASFVRrvKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRMAKPDpLLDIAMKLEEIALAddffvSRKLYPN 360
Cdd:cd06111 232 PEKAAQWML--DALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQK-WLAMYDALEDAMVA-----AKGIKPN 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 361 VDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPERE 420
Cdd:cd06111 304 LDFPAGPAYYLMGFDIDFFTPIFVMARITGWTAHIMEQRAD--NALIRPLSEYNGPEQRP 361
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
44-427 |
4.42e-85 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 264.70 E-value: 4.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 44 GFVNTAACSSKITYIDGDAgiLRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGF 123
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 124 PRD-AHPMPVLSSAVSALSTFYQDSLDPFDSDQVEIStVRLMAKVPT-IASYAyKTSIGQPLLYPDNTRSYVDNFLRMTF 201
Cdd:PRK14035 84 STDhVHPMTALRTSVSYLAHFDPDAEEESDEARYERA-IRIQAKVASlVTAFA-RVRQGKEPLKPRPDLSYAANFLYMLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 202 GVPAASYDVDpAFAKVLdtllVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADG 281
Cdd:PRK14035 162 GELPTDIEVE-AFNKAL----VLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 282 GDAASFVRRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEeialadDFFVSRK-LYPN 360
Cdd:PRK14035 237 DVDAYLDEKFANKE---KIMGFGHRVYKDGDPRAKYLREMSRK-ITKGTGREELFEMSVKIE------KRMKEEKgLIPN 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2039919926 361 VDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:PRK14035 307 VDFYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKD--NRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
44-427 |
8.37e-78 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 245.83 E-value: 8.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 44 GFVNTAACSSKITYIDGDagILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGF 123
Cdd:PRK14034 6 GLEGVVATTSSVSSIIDD--TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 124 PRD-AHPMPVLSSAVSALStFYQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRMTFG 202
Cdd:PRK14034 84 DLKkVHPMSVLRTAISMLG-LYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 203 VPAASYDVDpAFAKVLdtllVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGG 282
Cdd:PRK14034 163 EEPDEVEVE-AFNKAL----VLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEI-GEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 283 DAASFVRrvKAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIALADdffvsRKLYPNVD 362
Cdd:PRK14034 237 NVESYIH--NKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKR-LTVLLGEEKWYNMSIKIEEIVTKE-----KGLPPNVD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039919926 363 FYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:PRK14034 309 FYSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYEN--NRLIRPRADYVGPTHQVYVPIEER 371
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
47-427 |
5.13e-77 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 244.06 E-value: 5.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 47 NTAACSSKITYIDgdagiLRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRD 126
Cdd:PRK12351 19 NTALCTVGKSGND-----LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 127 AHPMPVLSSAVSALSTFYQDSLDPFDSDQVEIsTVRLMAKVPTIASYAYKTSigqpllyPDNTRSYVDN--------FLR 198
Cdd:PRK12351 94 AHPMDVMRTGVSVLGCLLPEKEDHNFSGARDI-ADRLLASLGSILLYWYHYS-------HNGRRIEVETdddsigghFLH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 199 MTFGVPAAsydvdPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMlgaIQ 278
Cdd:PRK12351 166 LLHGKKPS-----ESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEI---QQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 279 --ADGGDA-ASFVRRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIaLADdffvSR 355
Cdd:PRK12351 238 ryDTPDEAeADIRRRVENKE---VVIGFGHPVYTISDPRNKVIKEVAKK-LSKEAGDTKLYDIAERLETV-MWE----EK 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039919926 356 KLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPIEKR 427
Cdd:PRK12351 309 KMFPNLDWFSAVSYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQD--NKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
40-415 |
3.32e-73 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 233.84 E-value: 3.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 40 TYDPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRF 119
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 120 FDGFPRDAHPMPVLSSAVSALSTFYQDSLDPFDSDQVEiSTVRLMAKVPTIASYAYKTSIGQPLLYPDNTRSYVDNFLRM 199
Cdd:PRK12349 84 LKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKS-RAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSANFLYM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 200 TFGVPAASYDVdpafaKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLgaiqA 279
Cdd:PRK12349 163 LTGKKPTELEE-----KIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYML----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 280 DGGDAASFV----RRVKAKEqgvKLMGFGHRVY-KNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIALADdffvs 354
Cdd:PRK12349 234 EAGTVEKFEellqKKLYNKE---KIMGFGHRVYmKKMDPRALMMKEALKQ-LCDVKGDYTLYEMCEAGEKIMEKE----- 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 355 RKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVG 415
Cdd:PRK12349 305 KGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHAN--NRLFRPRVNYIG 363
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
47-424 |
4.80e-67 |
|
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: 217.79 E-value: 4.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 47 NTAACSSKITYIDgdagiLRYRGYPIDELAGKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRD 126
Cdd:cd06117 10 NTALCTVGRSGND-----LHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 127 AHPMPVLSSAVSALSTFYQDSLDPFDSDQVEISTvRLMAKVPTIASYAYKTSI-GQPLLYPDNTRSYVDNFLRMTFGVPA 205
Cdd:cd06117 85 AHPMDVMRTGVSVLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYSHnGKRIEVETDDDSIGGHFLHLLHGEKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 206 ASydvdpAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQmlgaIQADGGDA- 284
Cdd:cd06117 164 SE-----SWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFE----IQQRYESAd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 285 ---ASFVRRVKAKEqgvKLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIaladdFFVSRKLYPNV 361
Cdd:cd06117 235 eaeADIRRRVENKE---VVIGFGHPVYTIADPRNQVIKEVAKQ-LSKEGGDMKMFDIAERLETV-----MWEEKKMFPNL 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2039919926 362 DFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDpeTKIGRPRQLYVGSPEREFVPI 424
Cdd:cd06117 306 DWFSAVSYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQD--GKIIRPSANYTGPEDLKFVPI 366
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
61-415 |
4.27e-66 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) 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: 216.36 E-value: 4.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 61 DAGILRYRGYPIDELAGKAS------FLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKR-FFDGFPrDAHPMPVL 133
Cdd:cd06113 34 CPGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVEdVILKAP-SKDIMNKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 134 SSAVSALSTfYQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSI----GQPLL--YPDNTRSYVDNFLRMTfgVPAAS 207
Cdd:cd06113 113 QRSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQAKRhyydGESLYihHPQPELSTAENILSML--RPDKK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 208 YDVDPAfaKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQADGGDA-- 284
Cdd:cd06113 190 YTELEA--KLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIKENVKDWtd 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 285 ----ASFVRRVKAKEQGVK---LMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEIA---LADDFFVS 354
Cdd:cd06113 268 edevRAYLRKILNKEAFDKsglIYGMGHAVYTLSDPRAVVLKKYARS-LAKEKGREEEFALYERIERLApevIAEERGIG 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039919926 355 RKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIA-QWREMINDpeTKIGRPRQLYVG 415
Cdd:cd06113 347 KTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAhRIEELLNS--GRIIRPAYKYVG 406
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
42-415 |
2.84e-62 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 204.81 E-value: 2.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 42 DPGFVNTAACSSKITYIDGDAGILRYRGYPIDELAGKASFLETSYLLIYGelpttdqlaaftekvqlhtmlhedfkRFFD 121
Cdd:PRK12350 2 VPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDG--------------------------RFGP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 122 GFP-RDAHPMPVLSSAV-----SALSTF-----YQDSLDPFDSDQVEistvRLMAKVPTIASYAYKTS--IGQPLLyPDN 188
Cdd:PRK12350 56 GLPpAEPFPLPVHLGDArvdvqAALAMLapvwgFRPLLDIDDLTARL----DLARASVMALSAVAQSArgIGQPAV-PQR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 189 TRSYVDNFLRMTFGVPAAsyDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANE 268
Cdd:PRK12350 131 EIDHAATILERFMGRWRG--EPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 269 AVLQMLGAIQADgGDAASFVRRVKAKeqGVKLMGFGHRVYKNYDPRAaivkqaaqDVLSRMAKP--DPLLDIAMKLEEIA 346
Cdd:PRK12350 209 RVLPMLDAVERT-GDARGWVKGALDR--GERLMGFGHRVYRAEDPRA--------RVLRATAKRlgAPRYEVAEAVEQAA 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 347 LAD--DFFVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINdpETKIGRPRQLYVG 415
Cdd:PRK12350 278 LAElrERRPDRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKR--TGRLVRPSARYVG 346
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
61-427 |
1.37e-61 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 205.91 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 61 DAGILRYRGYPIDELA------GKASFLETSYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRffdGFPRDAHP---MP 131
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVngflkeKRFGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTR---DMILKAPSkdiMN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 132 VLSSAVSALSTfYQDSLDPFDSDQVEISTVRLMAKVPTIASYAYKTSI----GQPLL--YPDNTRSYVDNFLRMTFGvpa 205
Cdd:PRK14032 141 SLARSVLALYS-YDDNPDDTSIDNVLRQSISLIARFPTLAVYAYQAYRhyhdGKSLYihPPKPELSTAENILYMLRP--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 206 asydvDPAF----AKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIQA- 279
Cdd:PRK14032 217 -----DNKYteleARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKEn 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 280 -----DGGDAASFVRRVKAKE----QGVkLMGFGHRVYKNYDPRAAIVKQAAQDvLSRMAKPDPLLDIAMKLEEiaLADD 350
Cdd:PRK14032 292 vkdweDEDEIADYLTKILNKEafdkSGL-IYGMGHAVYTISDPRAVILKKFAEK-LAKEKGREEEFNLYEKIEK--LAPE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 351 FFV-SRKLY----PNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQwR--EMINDpeTKIGRPRQLYVGSPeREFVP 423
Cdd:PRK14032 368 LIAeERGIYkgvsANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAH-RieELVNG--GKIIRPAYKSVLER-REYVP 443
|
....
gi 2039919926 424 IEKR 427
Cdd:PRK14032 444 LEER 447
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
55-427 |
4.40e-44 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 159.15 E-value: 4.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 55 ITYIDGDAGIlRYRGYPIDEL-------AGKASFLETS--YLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPR 125
Cdd:PRK09569 52 ISYLDPQEGI-RFRGKTIPETfealpkaPGSEYPTVESfwYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 126 DAHPMPVLSSAVSAL---STF------------------YQDSLDpfdsdqveistvrLMAKVPTIASYAY-------KT 177
Cdd:PRK09569 131 DSHPMVMLSVGILAMqreSKFakfynegkfnkmdaweymYEDASD-------------LVARIPVIAAYIYnlkykgdKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 178 SIGQPLLypdntrSYVDNFLRMtFGVPaasydvdPAFAKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVH 256
Cdd:PRK09569 198 IPSDPEL------DYGANFAHM-IGQP-------KPYKDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 257 ALSGPLHGGANEAVLQMLGAIQADGGDAASfvrrvkAKEQGVKLM-----------GFGHRVYKNYDPRAAIVKQAAQDV 325
Cdd:PRK09569 264 GLAGPLHGLANQEVLGWIQQFQEKLGGEEP------TKEQVEQALwdtlnagqvipGYGHAVLRKTDPRYTAQREFCLKH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 326 LsrmaKPDPLLDIAMKLEEIA---LADDFFVSRKlYPNVDFYTGLIYKAMGFPTKMF-TVLFALGRLPGWIAQ--WREMI 399
Cdd:PRK09569 338 L----PDDPLFKLVAMIFEVApgvLTEHGKTKNP-WPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANitWDRGL 412
|
410 420
....*....|....*....|....*...
gi 2039919926 400 NDPetkIGRPRQLYVGSPErEFVPIEKR 427
Cdd:PRK09569 413 GYA---IERPKSVTTEMLE-KWAAEGGR 436
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
55-394 |
7.37e-40 |
|
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: 147.45 E-value: 7.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 55 ITYIDGDAGIlRYRGYPIDEL-------AGKASFLETS--YLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPR 125
Cdd:cd06103 50 TSVLDPDEGI-RFRGKTIPECqellpkaDGGGEPLPEGlfWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 126 DAHPMPVLSSAVSALST---------------------FYQDSLDpfdsdqveistvrLMAKVPTIASYAYKTSIGQ-PL 183
Cdd:cd06103 129 NLHPMTQLSAAILALQSeskfakayaegkinkttyweyVYEDAMD-------------LIAKLPVVAAKIYRRKYRKgGE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 184 LYP-DNTRSYVDNFLRMtFGVPaasydvDPAFAKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVHALSGP 261
Cdd:cd06103 196 IGAiDSKLDWSANFAHM-LGYE------DEEFTDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 262 LHGGANEAVLQMLGAIQADGGDAAS------FVRRVKAKEQGVKlmGFGHRVYKNYDPRAAivkqAAQDVLSRMAKPDPL 335
Cdd:cd06103 269 LHGLANQEVLKWLLKMQKELGKDVSdeelekYIWDTLNSGRVVP--GYGHAVLRKTDPRFT----CQREFALKHLPDDPL 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039919926 336 LDIAMKLEEIA--LADDFFVSRKLYPNVDFYTGLIYKAMGFP-TKMFTVLFALGRLPGWIAQ 394
Cdd:cd06103 343 FKLVAQCYKIIpgVLKEHGKVKNPYPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQ 404
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
58-412 |
1.51e-39 |
|
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: 146.74 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 58 IDGDAGIlRYRGYPIDEL--------AGKASFLET-SYLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRDAH 128
Cdd:cd06105 53 LDPEEGI-RFRGLSIPECqkllpkapGGEEPLPEGlFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 129 PMPVLSSAVSAL---STF-----------------YQDSLDpfdsdqveistvrLMAKVPTIASYAYK-TSIGQPLLYPD 187
Cdd:cd06105 132 PMSQLSAAITALnseSKFakayaegihkskyweyvYEDSMD-------------LIAKLPCVAAKIYRnLYRGGKIIAID 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 188 NTRSYVDNFLRMTfgvpaaSYDvDPAFAKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGA 266
Cdd:cd06105 199 SNLDWSANFANML------GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 267 NEAVLQMLGAIQADGGDAASfvrrvkaKEQ-----------GVKLMGFGHRVYKNYDPRAAIVKQAAQDVLSRmakpDPL 335
Cdd:cd06105 272 NQEVLVWLTKLQKEVGKDVS-------DEQlreyvwktlnsGRVVPGYGHAVLRKTDPRYTCQREFALKHLPN----DPL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 336 LDIAMKLEEIA---LADDFFVsRKLYPNVDFYTGLIYKAMGFpTKM--FTVLFALGRLPGWIAQ--WREMINDPetkIGR 408
Cdd:cd06105 341 FKLVSQLYKIVppvLTEQGKA-KNPWPNVDAHSGVLLQYYGL-TEMnyYTVLFGVSRALGVLSQliWDRALGLP---LER 415
|
....
gi 2039919926 409 PRQL 412
Cdd:cd06105 416 PKSV 419
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
205-415 |
1.51e-35 |
|
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: 132.38 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 205 AASYDVDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGANEAVLQMLGAIqADGGDA 284
Cdd:cd06102 88 ARAWGLDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEA-LRAGDA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 285 ASFVRRVKAkeQGVKLMGFGHRVYKNYDPRAAivkqAAQDVLSRMAKPDPllDIAMKLEEIALADDffvsrKLYPNVDFY 364
Cdd:cd06102 167 EAAVRERLR--RGEALPGFGHPLYPDGDPRAA----ALLAALRPLGPAAP--PAARALIEAARALT-----GARPNIDFA 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2039919926 365 TGLIYKAMGFPTKMFTVLFALGRLPGWIAQWREMINDPetKIGRPRQLYVG 415
Cdd:cd06102 234 LAALTRALGLPAGAAFALFALGRSAGWIAHALEQRAQG--KLIRPRARYVG 282
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
56-412 |
1.73e-35 |
|
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: 135.71 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 56 TYIDGDAGIlRYRGYPIDEL-------AGKASFLETS--YLLIYGELPTTDQLAAFTEKVQLHTMLHEDFKRFFDGFPRD 126
Cdd:cd06106 51 SVLDAEEGI-RFHGKTIPECqkelpkaPIGGEMLPESmlWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 127 AHPMPVLSSAVSALST----------------FYQDSLDpfDSdqveistVRLMAKVPTIASYAYKTSI--GQPLLYPDN 188
Cdd:cd06106 130 LHPMTQLSIGVAALNHdskfaaayekgikkteYWEPTLE--DS-------LNLIARLPALAARIYRNVYgeGHGLGKIDP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 189 TRSYVDNFLRMTfgvpaaSYDVDPAFAKVLDTLLVLHADHEQ-NCSTSTVRLVGSGQANLFASVSAGVHALSGPLHGGAN 267
Cdd:cd06106 201 EVDWSYNFTSML------GYGDNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 268 EAVLQMLGAIQADGGDAASF--VRRV--KAKEQGVKLMGFGHRVYKNYDPRAAIVKQAAQdvlSR-MAKPDPLLDIAMKL 342
Cdd:cd06106 275 QEVLRWILEMQKNIGSKATDqdIRDYlwKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQ---TRpELENDPVVQLVQKL 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039919926 343 EEIA--LADDFFVSRKLYPNVDFYTGLIYKAMGF-PTKMFTVLFALGRLPGWIAQ--WREMINDPetkIGRPRQL 412
Cdd:cd06106 352 SEIApgVLTEHGKTKNPFPNVDAASGVLFYHYGIrEFLYYTVIFGVSRALGPLTQlvWDRILGLP---IERPKSL 423
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
191-421 |
2.12e-25 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 104.18 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 191 SYVDNFLRMTFG-VPaasydvDPAFAKVLDTLLVLHADHEQNCSTSTVRLVGSGQANLFASVSAGVHALsGPLHGGANEA 269
Cdd:PRK06224 36 SFTDMIFLLLRGrLP------TPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 270 VLQMLGAIQADGGDAASF---VRRV--KAKEQGVKLMGFGHRVYKNYDPRAaivkqaaqDVLSRMAKPDPL----LDIAM 340
Cdd:PRK06224 109 AAELLQEIAAAADAGADLdaaARAIvaEYRAAGKRVPGFGHPLHKPVDPRA--------PRLLALAREAGVagrhCRLAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 341 KLEEIALADdffVSRKLYPNVDFYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQ-WREMINDPETKIGRPRQL---YVGS 416
Cdd:PRK06224 181 ALEAALAAA---KGKPLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHvWEELQQPIGFRIWDPAEEaveYTGP 257
|
....*
gi 2039919926 417 PEREF 421
Cdd:PRK06224 258 PPREL 262
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
211-397 |
5.21e-23 |
|
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: 96.48 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 211 DPAFAKVLDTLLVLHADH-EQNCSTSTVRLVGS-GQANLFASVSAGVHALsGPLHGGANEAVLQMLGAIQADGG----DA 284
Cdd:cd06100 27 TPYEARLLEALLVALADHgPATPSAHAARLTASaGPEDLQSAVAAGLLGI-GDRFGGAGEGAARLFKEAVDSGDaldaAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 285 ASFVRRVKAKEQgvKLMGFGHRVYKNYDPRAAIVKQaaqdvLSRMAKPD-PLLDIAMKLEEIALADdffvSRKLYP-NVD 362
Cdd:cd06100 106 AEFVAEYRAAKK--RIPGFGHPVHKNPDPRVPRLLE-----LARELGPAgPHLDYALAVEKALTAA----KGKPLPlNVD 174
|
170 180 190
....*....|....*....|....*....|....*
gi 2039919926 363 FYTGLIYKAMGFPTKMFTVLFALGRLPGWIAQWRE 397
Cdd:cd06100 175 GAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALE 209
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
212-392 |
9.41e-04 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 41.34 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 212 PAFA-KVLDTLLVLHADHEQNCSTSTVRLVGS-GQANLFASVSAGVHALsGPLHGGANEAVLQMLGAIQADGGDAASFVR 289
Cdd:PLN02522 396 PRYCtKFIEMCIMLCADHGPCVSGAHNTIVTArAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPYEFVE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039919926 290 RVKAKeqGVKLMGFGHRVYK--NYDPRAAIVKQAAQDVLSrmakpdplldiAMKLEEIALADDFFVSRK---LYPNVDFY 364
Cdd:PLN02522 475 GMKKK--GIRVPGIGHRIKSrdNRDKRVELLQKYARTHFP-----------SVKYMEYAVQVETYTLSKannLVLNVDGA 541
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2039919926 365 TGLIYKAMGFPTKMFTV--------------LFALGRLPGWI 392
Cdd:PLN02522 542 IGSLFLDLLAGSGMFTKqeideiveigylngLFVLARSIGLI 583
|
|
| |
