|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-416 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 929.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 1 MADTKAKLTLN-GDDAIELDVLKGTLGQDVIDIRTL-GSKGVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLA 78
Cdd:PRK05614 1 MADKKATLTLNgGEASVELPILKGTLGPDVIDIRKLyGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 79 TESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHR 158
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 159 DIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTST 238
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 239 VRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATV 318
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 319 MRETCHEVLKELGTKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNE 398
Cdd:PRK05614 321 MRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNE 400
|
410
....*....|....*....
gi 493862833 399 MHSE-GMKIARPRQLYTGY 416
Cdd:PRK05614 401 MHSDpEQKIGRPRQLYTGY 419
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
13-421 |
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: 830.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 13 DDAIELDVLKGTLGQDVIDIRTLGS-KGVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILL 91
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKqTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 92 NGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHRDIAAFRLLSKMPT 171
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 172 MAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFA 251
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 252 CIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELG 331
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 332 TKDD-LLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMKIARP 409
Cdd:TIGR01798 321 LHDDpLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDpGQKIGRP 400
|
410
....*....|..
gi 493862833 410 RQLYTGYEQRDF 421
Cdd:TIGR01798 401 RQLYTGETQRDY 412
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
18-415 |
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: 809.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 18 LDVLKGTLGQDVIDIRTLGSK-GVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKP 96
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKtGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 97 TQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMC 176
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 177 YKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAG 256
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 257 IASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDL 336
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 337 LEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMKIARPRQLYTG 415
Cdd:cd06114 321 LEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDpELKIGRPRQLYTG 400
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
39-415 |
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: 660.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 39 GVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQI 118
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRND 191
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAhtgdlyqNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 192 LSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEA 271
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 272 ALKMLEEISSVEHIPEFVRRAKDKNdsFRLMGFGHRVYKNYDPRATVMRETCHEVLKELgTKDDLLEVAMELEHIALNDP 351
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEV-EKDPLLKVAMELERIALEDE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493862833 352 YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMKIARPRQLYTG 415
Cdd:cd06107 318 YFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDpLQRIWRPRQVYTG 382
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
38-421 |
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: 654.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 38 KGVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQ 117
Cdd:COG0372 8 RAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 118 ITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGN 197
Cdd:COG0372 88 VKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD-IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 198 FLRMMFSTpceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLE 277
Cdd:COG0372 167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 278 EISSVEHIPEFVRRAKDKndSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFIEKK 357
Cdd:COG0372 242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEYFIEKK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493862833 358 LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHsEGMKIARPRQLYTGYEQRDF 421
Cdd:COG0372 319 LYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQR-ADNRIIRPRQIYVGPEDRDY 381
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
46-410 |
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: 550.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 46 GFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 126 RRDSHPMAVMCGITGALAAFYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSt 205
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 206 pceeYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHI 285
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 286 PEFVRRAKDKNDsFRLMGFGHRVYKNYDPRATVMRETCHEVLKElGTKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFY 365
Cdd:pfam00285 236 EEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELAEE-GGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 493862833 366 SGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPR 410
Cdd:pfam00285 314 SGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-413 |
0e+00 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.
Pssm-ID: 99871 [Multi-domain] Cd Length: 358 Bit Score: 532.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 45 PGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHA 124
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 125 FRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFS 204
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARD-KSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 205 TpceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:cd06118 160 E-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 285 IPEFVRraKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFieKKLYPNVDF 364
Cdd:cd06118 235 VEAYIW--KKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG-DDKLFEIAEELEEIALEVLGE--KGIYPNVDF 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 493862833 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARPRQLY 413
Cdd:cd06118 310 YSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
16-415 |
3.46e-179 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 507.64 E-value: 3.46e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 16 IELDVLKGTLGQDVIDIRTLG-SKGVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGE 94
Cdd:PLN02456 36 SPLSELGPVQAERLKKIKAGKdDLGLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 95 KPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHRDIAAFRLLS 167
Cdd:PLN02456 116 LPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYlrgqhkyKSWEVRDEDIVRLIG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 168 KMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVR-TAGSSG 246
Cdd:PLN02456 196 KLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSSG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 247 ANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEV 326
Cdd:PLN02456 276 VDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIREFALEV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 327 LKELGtKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMK 405
Cdd:PLN02456 354 FKHVG-DDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLpDER 432
|
410
....*....|
gi 493862833 406 IARPRQLYTG 415
Cdd:PLN02456 433 IMRPKQVYTG 442
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
39-421 |
2.01e-178 |
|
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: 502.82 E-value: 2.01e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 39 GVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQI 118
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNF 198
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 199 LRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEE 278
Cdd:cd06116 161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 279 ISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFIEKKL 358
Cdd:cd06116 241 IGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATG-RNPLLDIAVELEKIALEDEYFISRKL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493862833 359 YPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMKIARPRQLYTGYEQRDF 421
Cdd:cd06116 318 YPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDpEQKIARPRQVYTGPRDRDY 381
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
36-421 |
1.51e-164 |
|
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.
Pssm-ID: 99868 Cd Length: 410 Bit Score: 468.84 E-value: 1.51e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 36 GSKGVFTFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIH 115
Cdd:cd06115 18 DDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 116 EQITRLFHAFRRDSHPMAVMCGITGALAAFYHDS------LDV-NNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYP 188
Cdd:cd06115 98 TGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEAnpalagQDIyKNKQVRDKQIVRILGKAPTIAAAAYRRRAGRPPNLP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 189 RNDLSYAGNFLRMMFSTPCEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGA 268
Cdd:cd06115 178 SQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 269 NEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIAL 348
Cdd:cd06115 258 NEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVG-KDPLIEIAVALEKAAL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493862833 349 NDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSE-GMKIARPRQLYTGYEQRDF 421
Cdd:cd06115 335 SDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDpDTKIMRPQQLYTGVWLRHY 408
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-413 |
2.09e-130 |
|
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: 376.27 E-value: 2.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 45 PGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPtqaqydefkttvtrhtmiheqitrlfha 124
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 125 frrdshpmavmcgitgalaafyhdsldvnnprhrdiaafrllskmptmaamcykysigqpfvyprndlSYAGNFLRMMFS 204
Cdd:cd06101 53 --------------------------------------------------------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 205 TpceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:cd06101 65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 285 IPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFieKKLYPNVDF 364
Cdd:cd06101 140 EPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG-LDPMFELAAELEKIAPEVLYE--KKLYPNVDF 216
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 493862833 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARPRQLY 413
Cdd:cd06101 217 YSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
43-415 |
2.40e-125 |
|
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: 367.52 E-value: 2.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 43 FDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLF 122
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 123 HAFRRDSHPMAVMCGITGALAAFYHD-SLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRM 201
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPKpEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 202 MFstpceEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISS 281
Cdd:cd06112 161 LF-----GEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 282 VEHIPEFV--RRAKDKndsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELEHIALNdpYFIEKKLY 359
Cdd:cd06112 236 PENVKAYLdkKLANKQ----KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEE--LLGHKGVY 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 493862833 360 PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTG 415
Cdd:cd06112 310 PNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGDN-RIFRPTQIYIG 364
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
43-427 |
4.47e-122 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 359.27 E-value: 4.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 43 FDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLF 122
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 123 HAFRRDSHPMAVMCGITGALAAFYHDSlDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMM 202
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRR-ALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 203 FstpceEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSV 282
Cdd:PRK14036 163 T-----EREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 283 EHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIAlnDPYFIEKKLYPNV 362
Cdd:PRK14036 238 ENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFG-HDEYYEIALELERVA--EERLGPKGIYPNV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493862833 363 DFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQRDFKSDIKR 427
Cdd:PRK14036 313 DFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGAN-RIFRPTQIYTGSHNRRYIPLEER 376
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
52-421 |
8.33e-117 |
|
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.
Pssm-ID: 130859 Cd Length: 368 Bit Score: 345.50 E-value: 8.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 52 SCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHP 131
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 132 MAVMCGITGALAAFYHDSLDVNNPRHRDIAAfRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTpceeyE 211
Cdd:TIGR01800 88 MDVLRTAVSYLGALDPEKFGHTPEEARDIAI-RLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGE-----E 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 212 VNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:TIGR01800 162 PTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILK 371
Cdd:TIGR01800 242 ALENKE--RIMGFGHRVYKTYDPRAKILKEYA-KKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYY 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 493862833 372 AMGIPSSMFTVIFAMARTVGWIAHWNEmHSEGMKIARPRQLYTGYEQRDF 421
Cdd:TIGR01800 314 MMGIPTDLFTPIFAMSRVTGWTAHIIE-QVENNRLIRPRADYVGPEERKY 362
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
193-413 |
7.95e-115 |
|
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: 334.69 E-value: 7.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 193 SYAGNFLRMMFSTpceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAA 272
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 273 LKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELEHIALNDPY 352
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGD-DPMFELAAELEKIAEEVLY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493862833 353 FieKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARPRQLY 413
Cdd:cd06099 155 E--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
53-415 |
1.72e-111 |
|
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: 331.55 E-value: 1.72e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 53 CESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPM 132
Cdd:cd06110 9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 133 AVMCGITGALAAfYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTpceeyEV 212
Cdd:cd06110 89 DVLRTAVSALAL-YDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTGE-----KP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 213 NPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRA 292
Cdd:cd06110 163 SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVKDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 293 KDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKA 372
Cdd:cd06110 243 LANKE--KIMGFGHRVYKTGDPRAKHLREMSRRLGKETG-EPKWYEMSEAIEQAMRD-----EKGLNPNVDFYSASVYYM 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 493862833 373 MGIPSSMFTVIFAMARTVGWIAHWNEMHSeGMKIARPRQLYTG 415
Cdd:cd06110 315 LGIPVDLFTPIFAISRVSGWCAHILEQYF-NNRLIRPRAEYVG 356
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
54-422 |
1.34e-105 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 317.33 E-value: 1.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 54 ESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:NF041157 14 YTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 134 VMCGITGALAAFYHDSLDVNNPRHRdiaAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVn 213
Cdd:NF041157 94 MMETAFSALASIENYKWNKENDREK---ALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATFGRKPSEEEI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 214 pvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRaK 293
Cdd:NF041157 170 ----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNE-N 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 294 DKNDSFRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDD---LLEVAMELEHIALNdpYFIEKKLYPNVDFYSGIIL 370
Cdd:NF041157 245 IINGKKRLMGFGHRVYKTYDPRAKIFK----EYAEKLASTNEakkYLEIAEKLEELGIK--HFGSKGIYPNTDFYSGIVF 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493862833 371 KAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARPRQLYTGYEQRDFK 422
Cdd:NF041157 319 YSLGFPVYMFTSLFALSRVLGWLAHIIEYVEEQHRLIRPRALYVGPEKRDFV 370
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
54-421 |
1.14e-89 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 276.52 E-value: 1.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 54 ESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRH----TMIHEQITRLFHAfrrDS 129
Cdd:NF041301 16 ESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFSDAMAAErevdDGVLETVRALAAA---DE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 130 HPMAVMCGITGALAAfYHDSLDVNNPRHRDIA---AFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTp 206
Cdd:NF041301 93 EPMAALRTAVSMLSA-YDPDADDADPTDREANlrkGRRITAKIPTILAAFARLRDGEDPVEPREDLSHAANFLYMLNGE- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 207 ceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIP 286
Cdd:NF041301 171 ----EPDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 287 -EFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELG-TKDDLLEVAMElEHIALndpyfiEKKLYPNVDF 364
Cdd:NF041301 247 vEWVKDALEEGR--RVPGFGHRVYNVKDPRAKILGEKSEELGEAAGdTKWYEYSVAIE-EYMTE------EKGLAPNVDF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 493862833 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHsEGMKIARPRQLYTGYEQRDF 421
Cdd:NF041301 318 YSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQY-EDNRLIRPRARYVGPKDREF 373
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
55-427 |
9.27e-87 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 268.92 E-value: 9.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 55 SKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAV 134
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 135 MCGITGALAAFYHDSLdvNNPRHRDIAAfRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVNp 214
Cdd:PRK14037 96 MEAAFAALASIDKNFK--WKENDKEKAI-SIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTAEEIK- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 215 vlerAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRaKD 294
Cdd:PRK14037 172 ----AMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFND-KI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 295 KNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELEHIALNDpyFIEKKLYPNVDFYSGIILKAMG 374
Cdd:PRK14037 247 INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALG 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 493862833 375 IPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARPRQLYTGYEQRDFKSDIKR 427
Cdd:PRK14037 325 FPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
54-415 |
5.17e-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: 266.09 E-value: 5.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 54 ESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFrrdsHPMA 133
Cdd:cd06109 10 ETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL----AGLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 134 VMCGITGALAAFyhdsldvnNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTPCEEYEVn 213
Cdd:cd06109 86 PMDALRALLALL--------PDSPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGEPPSEAHV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 214 pvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAK 293
Cdd:cd06109 157 ----RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 294 DKNDsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELEHIALN--DPYFIEKKLYPNVDFYSGIILK 371
Cdd:cd06109 233 ARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLGAPDERLEFAEAVEQAALAllREYKPGRPLETNVEFYTALLLE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 493862833 372 AMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTG 415
Cdd:cd06109 307 ALGLPREAFTPTFAAGRTAGWTAHVLEQARTG-RLIRPQSRYVG 349
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
46-421 |
2.53e-84 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 262.77 E-value: 2.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 46 GFTSTASCESKITYIDGDEgiLLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 126 RRDS-HPMAVMCGITGALAAFYHDSLDVNNPRHRDiAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFS 204
Cdd:PRK14035 84 STDHvHPMTALRTSVSYLAHFDPDAEEESDEARYE-RAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 205 TPCEEYEVnpvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:PRK14035 163 ELPTDIEV-----EAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14035 238 VDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRKITKGTG-REELFEMSVKIEKRMKE-----EKGLIPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 493862833 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQRDF 421
Cdd:PRK14035 310 YSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKDN-RIMRPRAKYIGETNRKY 365
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
54-420 |
4.01e-83 |
|
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: 259.27 E-value: 4.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 54 ESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:cd06111 10 TTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 134 VMCGITGALAAFyHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTpceeyEVN 213
Cdd:cd06111 90 VLRTAVSVLGAE-DSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGE-----VPS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 214 PVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAK 293
Cdd:cd06111 164 PEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 294 DKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELehialndpyfiEKKLYPNVDFYSGI 368
Cdd:cd06111 244 ARKE--KVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKwlamyDALEDAMVA-----------AKGIKPNLDFPAGP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493862833 369 ILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHsEGMKIARPRQLYTGYEQRD 420
Cdd:cd06111 311 AYYLMGFDIDFFTPIFVMARITGWTAHIMEQR-ADNALIRPLSEYNGPEQRP 361
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
54-421 |
3.13e-80 |
|
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: 251.84 E-value: 3.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 54 ESKITYIdGDEGILLH-RGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPM 132
Cdd:cd06108 10 QTAISTV-GKGGKGLTyRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 133 AVMCGITGALAAFYHDsldvNNPRHRDIAAFRLLSKMPTMAAMCYKYS-IGQPFVYPRNDLSYAGNFLRMMFSTPCEEYE 211
Cdd:cd06108 89 DVMRTGCSMLGCLEPE----NEFSQQYEIAIRLLAIFPSILLYWYHYShSGKRIETETDEDSIAGHFLHLLHGKKPGELE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 212 VnpvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:cd06108 165 I-----KAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILK 371
Cdd:cd06108 240 KLERKE--LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSASAYH 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 493862833 372 AMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQRDF 421
Cdd:cd06108 312 FCGIPTELFTPIFVMSRVTGWAAHIMEQRANN-RLIRPSADYIGPEPRPF 360
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
46-423 |
4.66e-80 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 251.61 E-value: 4.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 46 GFTSTASCESKItyIDGdegILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:PRK14034 9 GVVATTSSVSSI--IDD---TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 126 RRDS-HPMAVMcGITGALAAFYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFS 204
Cdd:PRK14034 84 DLKKvHPMSVL-RTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 205 TpceeyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:PRK14034 163 E-----EPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14034 238 VESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKRLTVLLG-EEKWYNMSIKIEEIVTK-----EKGLPPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 493862833 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIaRPRQLYTGYEQRDFKS 423
Cdd:PRK14034 310 YSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYENNRLI-RPRADYVGPTHQVYVP 367
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
67-420 |
1.75e-76 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 242.55 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 67 LLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFy 146
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 147 HDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLRMMFSTpceeyEVNPVLERAMDRILIL 226
Cdd:PRK14033 112 DPEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFGE-----VPEPEVVRAFEVSLIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 227 HADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGH 306
Cdd:PRK14033 187 YAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKE--KVMGFGH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 307 RVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELehialndpyfiEKKLYPNVDFYSGIILKAMGIPSSMFT 381
Cdd:PRK14033 265 RVYKHGDSRVPTMKAALRRVAAVRDGQRwldiyEALEKAMAE-----------ATGIKPNLDFPAGPAYYLMGFDIDFFT 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 493862833 382 VIFAMARTVGWIAHWNEMHsEGMKIARPRQLYTGYEQRD 420
Cdd:PRK14033 334 PIFVMSRITGWTAHIMEQR-ASNALIRPLSEYNGPEQRE 371
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
42-415 |
1.16e-74 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 237.70 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 42 TFDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRL 121
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 122 FHAFRRDSHPM-AVMCGITgALAAF---YHD-SLDVNnpRHRdiaAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAG 196
Cdd:PRK12349 84 LKALPKETHPMdGLRTGVS-ALAGYdndIEDrSLEVN--KSR---AYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 197 NFLRMMfstpcEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKML 276
Cdd:PRK12349 158 NFLYML-----TGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYML 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 277 EEISSVEHIPEFVRR---AKDKndsfrLMGFGHRVY-KNYDPRATVMRETchevLKELGTK---DDLLEVAMELEHIALN 349
Cdd:PRK12349 233 LEAGTVEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMKEA----LKQLCDVkgdYTLYEMCEAGEKIMEK 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493862833 350 dpyfiEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTG 415
Cdd:PRK12349 304 -----EKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHANN-RLFRPRVNYIG 363
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
67-421 |
3.86e-70 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 226.34 E-value: 3.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 67 LLHRGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVM---CGITGALA 143
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMrtgVSVLGCLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 144 AFYHDSldvNNPRHRDIAAfRLLSKMPTMaaMCYKYSI---GQPFVYPRNDLSYAGNFLRMMF-STPCEEYEvnpvleRA 219
Cdd:PRK12351 112 PEKEDH---NFSGARDIAD-RLLASLGSI--LLYWYHYshnGRRIEVETDDDSIGGHFLHLLHgKKPSESWV------KA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR---AKDKn 296
Cdd:PRK12351 180 MHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRrveNKEV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 297 dsfrLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKAMGIP 376
Cdd:PRK12351 259 ----VIGFGHPVYTISDPRNKVIKEVAKKLSKEAGD-TKLYDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 493862833 377 SSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQRDF 421
Cdd:PRK12351 329 TAMFTPLFVISRTTGWAAHVIEQRQDN-KIIRPSANYTGPEDRKF 372
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
62-421 |
8.71e-63 |
|
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: 206.62 E-value: 8.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 62 GDEGILLH-RGFPIDQLATESNYLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITG 140
Cdd:cd06117 17 GRSGNDLHyRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 141 ALAAFYHDSLDVNNPRHRDIAAfRLLSKMPTMAAMCYKYSI-GQPFVYPRNDLSYAGNFLRMMFSTPCEEyevnpVLERA 219
Cdd:cd06117 97 VLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYSHnGKRIEVETDDDSIGGHFLHLLHGEKPSE-----SWEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSf 299
Cdd:cd06117 171 MHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVENKEV- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 300 rLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKdDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKAMGIPSSM 379
Cdd:cd06117 250 -VIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDM-KMFDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTAM 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493862833 380 FTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQRDF 421
Cdd:cd06117 323 FTPLFVIARTTGWSAHIIEQRQDG-KIIRPSANYTGPEDLKF 363
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
17-409 |
3.30e-61 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 204.75 E-value: 3.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 17 ELDVLKGtlgqdvidIRTLGSKGVFTfdpGFTSTASCESKItYIDG----DEGILLHRGFPIDQLATES------NYLEV 86
Cdd:PRK14032 26 KYDVKRG--------LRNEDGTGVLV---GLTNIGDVHGYE-IDDGekipDEGKLYYRGYDIKDLVNGFlkekrfGFEEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 87 CYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLF--HAFRRDshpmaVMCGITGALAAFYhdSLDVNnPRHRDI---- 160
Cdd:PRK14032 94 AYLLLFGELPTKEELAEFTELLGDYRELPDGFTRDMilKAPSKD-----IMNSLARSVLALY--SYDDN-PDDTSIdnvl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 161 -AAFRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLRMMfsTPCEEYEvnPVLERAMDRILILHADHEQ- 232
Cdd:PRK14032 166 rQSISLIARFPTLAVYAYQayrhYHDGKSLYihPPKPELSTAENILYML--RPDNKYT--ELEARLLDLALVLHAEHGGg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 233 NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI-------SSVEHIPEFVRRAKDK---NDSFRLM 302
Cdd:PRK14032 242 NNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIkenvkdwEDEDEIADYLTKILNKeafDKSGLIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 303 GFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIAlndPYFI--EKKLY----PNVDFYSGIILKAMGIP 376
Cdd:PRK14032 322 GMGHAVYTISDPRAVILKKFAEKLAKEKG-REEEFNLYEKIEKLA---PELIaeERGIYkgvsANVDFYSGFVYDMLGIP 397
|
410 420 430
....*....|....*....|....*....|...
gi 493862833 377 SSMFTVIFAMARTVGWIAHWNEMHSEGMKIARP 409
Cdd:PRK14032 398 EELYTPLFAIARIVGWSAHRIEELVNGGKIIRP 430
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
43-419 |
2.11e-60 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 200.19 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 43 FDPGFTSTASCESKITYIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGE-KPTQAQYDEFKttVTRHTmiheqitrl 121
Cdd:PRK12350 1 FVPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRfGPGLPPAEPFP--LPVHL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 122 fHAFRRDSHPMAVMCGITGALAAFyhdsLDVNNPRHRD--IAAfrllSKMPTMAAMCYKYSIGQPFVyPRNDLSYAGNFL 199
Cdd:PRK12350 70 -GDARVDVQAALAMLAPVWGFRPL----LDIDDLTARLdlARA----SVMALSAVAQSARGIGQPAV-PQREIDHAATIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 200 RMMFSTpcEEYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI 279
Cdd:PRK12350 140 ERFMGR--WRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 280 SSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETChevlKELGTkdDLLEVAMELEHIALNDpyFIEKK-- 357
Cdd:PRK12350 218 ERTGDARGWVKGALDRGE--RLMGFGHRVYRAEDPRARVLRATA----KRLGA--PRYEVAEAVEQAALAE--LRERRpd 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493862833 358 --LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGmKIARPRQLYTGYEQR 419
Cdd:PRK12350 288 rpLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTG-RLVRPSARYVGPAPR 350
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
63-409 |
5.54e-58 |
|
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: 195.18 E-value: 5.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 63 DEGILLHRGFPIDQL---ATESN---YLEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMC 136
Cdd:cd06113 34 CPGKLYYRGYDVEDLvngAQKENrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 137 GITGALAAfYHDSLDVNNPRHRDIAAFRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLRMMfsTPCEEY 210
Cdd:cd06113 114 RSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrhYYDGESLYihHPQPELSTAENILSML--RPDKKY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 211 evNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI-------SSV 282
Cdd:cd06113 191 --TELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIkenvkdwTDE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 283 EHIPEFVRRAKDK--NDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKELGTKD--DLLEVAMELEHIALNDPYFIEKK 357
Cdd:cd06113 269 DEVRAYLRKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEefALYERIERLAPEVIAEERGIGKT 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493862833 358 LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIARP 409
Cdd:cd06113 349 VCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRP 400
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
57-419 |
1.59e-46 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 165.69 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 57 ITYIDGDEGILLhRGFPIDQL------ATESNY---LEVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRR 127
Cdd:PRK09569 52 ISYLDPQEGIRF-RGKTIPETfealpkAPGSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 128 DSHPMAVM-CGIT-----GALAAFYHDS----LDVNNPRHRDiaAFRLLSKMPTMAAMCY--KYSIGQPfVYPRNDLSYA 195
Cdd:PRK09569 131 DSHPMVMLsVGILamqreSKFAKFYNEGkfnkMDAWEYMYED--ASDLVARIPVIAAYIYnlKYKGDKQ-IPSDPELDYG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 196 GNFLRMMfstpceeyEVNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL- 273
Cdd:PRK09569 208 ANFAHMI--------GQPKPYKDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 274 ---KMLEEISSVEHIPEFVRRA-KDKNDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLEVAMEL----- 343
Cdd:PRK09569 280 wiqQFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLFKLVAMIfevap 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 344 ----EHIALNDPyfiekklYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAHWNEMHSEGMKIARPRQLYTGYEQ 418
Cdd:PRK09569 356 gvltEHGKTKNP-------WPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTEMLE 428
|
.
gi 493862833 419 R 419
Cdd:PRK09569 429 K 429
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
212-415 |
1.40e-41 |
|
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: 148.56 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 212 VNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:cd06102 93 LDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKE-LGTKDDLLEVAMELEHialndpyfiekkLYPNVDFYSGIIL 370
Cdd:cd06102 173 RLRRGE--ALPGFGHPLYPDGDPRAAALLAALRPLGPAaPPAARALIEAARALTG------------ARPNIDFALAALT 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493862833 371 KAMGIPSSMFTVIFAMARTVGWIAHWNEMHSEGMKIaRPRQLYTG 415
Cdd:cd06102 239 RALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLI-RPRARYVG 282
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
17-412 |
4.70e-36 |
|
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: 137.05 E-value: 4.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 17 ELDVLKGTLGQDVIDIRTL-----GSKGVFTFdpgFTSTasceskiTYIDGDEGILLhRGFPIDQL------ATESNY-- 83
Cdd:cd06103 15 RIKELRKKYGNTKLGQITVdqvigGMRGMKGL---VYET-------SVLDPDEGIRF-RGKTIPECqellpkADGGGEpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 84 LEVC-YILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGitgALAAFYHDSL--------DVNN 154
Cdd:cd06103 84 PEGLfWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSA---AILALQSESKfakayaegKINK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 155 PRHRDIA---AFRLLSKMPTMAAMCYKYSIGQ-PFVYPRN-DLSYAGNFLRMMfstpceEYEvNPVLERAMDRILILHAD 229
Cdd:cd06103 161 TTYWEYVyedAMDLIAKLPVVAAKIYRRKYRKgGEIGAIDsKLDWSANFAHML------GYE-DEEFTDLMRLYLTLHSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 230 HEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL----KMLEEISSVEHIPEFVRRAKDKNDSFRLM-G 303
Cdd:cd06103 234 HEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLkwllKMQKELGKDVSDEELEKYIWDTLNSGRVVpG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 304 FGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLEVAMELEHIAlndPYFIE-----KKLYPNVDFYSGIILKAMGIPS- 377
Cdd:cd06103 314 YGHAVLRKTDPRFTCQREFALKHLPD----DPLFKLVAQCYKII---PGVLKehgkvKNPYPNVDAHSGVLLQHYGMTEp 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 493862833 378 SMFTVIFAMARTVGWIAH--WNEmhSEGMKIARPRQL 412
Cdd:cd06103 387 QYYTVLFGVSRALGVLAQlvWSR--ALGLPIERPKSM 421
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
60-415 |
2.46e-29 |
|
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99858 Cd Length: 427 Bit Score: 118.62 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 60 IDGDEGILLhRGFPI----DQLATESNYLE-----VCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRDSH 130
Cdd:cd06105 53 LDPEEGIRF-RGLSIpecqKLLPKAPGGEEplpegLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 131 PMA-VMCGITgAL---AAF-----------------YHDSLDvnnprhrdiaafrLLSKMPTMAAMCYK--YSIGQpFVY 187
Cdd:cd06105 132 PMSqLSAAIT-ALnseSKFakayaegihkskyweyvYEDSMD-------------LIAKLPCVAAKIYRnlYRGGK-IIA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 188 PRNDLSYAGNFLRMMfstpceEYEvNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHG 266
Cdd:cd06105 197 IDSNLDWSANFANML------GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 267 GANEAAL----KMLEEIS---SVEHIPEFVRrakDKNDSFRLM-GFGHRVYKNYDPRATVMRETChevLKELgTKDDLLE 338
Cdd:cd06105 270 LANQEVLvwltKLQKEVGkdvSDEQLREYVW---KTLNSGRVVpGYGHAVLRKTDPRYTCQREFA---LKHL-PNDPLFK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 339 VAMELEHIAlnDPYFIE----KKLYPNVDFYSGIILKAMGIPS-SMFTVIFAMARTVGWIAH--WNEmhSEGMKIARPRQ 411
Cdd:cd06105 343 LVSQLYKIV--PPVLTEqgkaKNPWPNVDAHSGVLLQYYGLTEmNYYTVLFGVSRALGVLSQliWDR--ALGLPLERPKS 418
|
....
gi 493862833 412 LYTG 415
Cdd:cd06105 419 VSTD 422
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
58-412 |
2.24e-27 |
|
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99859 Cd Length: 428 Bit Score: 112.98 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 58 TYIDGDEGILLHrGFPIDQLATE-------SNYL--EVCYILLNGEKPTQAQYDEFKTTVTRHTMIHEQITRLFHAFRRD 128
Cdd:cd06106 51 SVLDAEEGIRFH-GKTIPECQKElpkapigGEMLpeSMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 129 SHPMAvmcGITGALAAFYHDSLDVNN------------PRHRDiaAFRLLSKMPTMAAMCYKYS----IGQPFVYPRNDL 192
Cdd:cd06106 130 LHPMT---QLSIGVAALNHDSKFAAAyekgikkteywePTLED--SLNLIARLPALAARIYRNVygegHGLGKIDPEVDW 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 193 SYagNFLRMMfstpceEYEVNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEA 271
Cdd:cd06106 205 SY--NFTSML------GYGDNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 272 ALK----MLEEISSVEHIPEFVRRAKDKNDSFRLM-GFGHRVYKNYDPRATVMRETChEVLKELgTKDDLLEVAMELEHI 346
Cdd:cd06106 277 VLRwileMQKNIGSKATDQDIRDYLWKTLKSGRVVpGYGHAVLRKPDPRFTALMEFA-QTRPEL-ENDPVVQLVQKLSEI 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493862833 347 AlnDPYFIE----KKLYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAH--WNEMHseGMKIARPRQL 412
Cdd:cd06106 355 A--PGVLTEhgktKNPFPNVDAASGVLFYHYGIREFLYyTVIFGVSRALGPLTQlvWDRIL--GLPIERPKSL 423
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
218-398 |
1.59e-24 |
|
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 100.72 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 218 RAMDRILILHADH-EQNASTSTVRTAGSSGANPF-ACIAAGIASLwGPAHGGANEAALKMLEEI-----SSVEHIPEFVR 290
Cdd:cd06100 32 RLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgdALDAAAAEFVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 291 RAKDKNdsFRLMGFGHRVYKNYDPRATVMretcHEVLKELGTKDDLLEVAMELEHIALNDPyfiEKKLYPNVDFYSGIIL 370
Cdd:cd06100 111 EYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGPAGPHLDYALAVEKALTAAK---GKPLPLNVDGAIAAIL 181
|
170 180
....*....|....*....|....*...
gi 493862833 371 KAMGIPSSMFTVIFAMARTVGWIAHWNE 398
Cdd:cd06100 182 LDLGFPPGALRGLFVLGRSPGLIAHALE 209
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
213-421 |
2.90e-22 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 95.32 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 213 NPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEI----SSVEHIPEF 288
Cdd:PRK06224 51 TPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaaDAGADLDAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 289 VR------RAKDKndsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELEHIalndpyFIE---KKLY 359
Cdd:PRK06224 130 ARaivaeyRAAGK----RVPGFGHPLHKPVDPRAPRLL----ALAREAGVAGRHCRLAEALEAA------LAAakgKPLP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862833 360 PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAH-WNEMHSE-GMKIARPRQL---YTGYEQRDF 421
Cdd:PRK06224 196 LNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHvWEELQQPiGFRIWDPAEEaveYTGPPPREL 262
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
220-395 |
1.05e-06 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 50.97 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 220 MDRILILHADHEQNASTS--TVRTAgSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEISSVEHIP-EFVRRAKDKN 296
Cdd:PLN02522 403 IEMCIMLCADHGPCVSGAhnTIVTA-RAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMKKKG 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862833 297 dsFRLMGFGHRVYK--NYDPRATVMRETCHEVLKELgtkdDLLEVAMELEHIALNDpyfiEKKLYPNVDFYSGIILKAMG 374
Cdd:PLN02522 481 --IRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSV----KYMEYAVQVETYTLSK----ANNLVLNVDGAIGSLFLDLL 550
|
170 180 190
....*....|....*....|....*....|....*
gi 493862833 375 IPSSMFTV--------------IFAMARTVGWIAH 395
Cdd:PLN02522 551 AGSGMFTKqeideiveigylngLFVLARSIGLIGH 585
|
|
| |
