|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-416 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 920.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 1 MSDAKAKITL-GGDTAIELDVLKGTLGQDVIDIRSL-GSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLA 78
Cdd:PRK05614 1 MADKKATLTLnGGEASVELPILKGTLGPDVIDIRKLyGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 79 TESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHR 158
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 159 EIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTST 238
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 239 VRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATV 318
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 319 MRETCHEVLKELGTKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNE 398
Cdd:PRK05614 321 MRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNE 400
|
410
....*....|....*....
gi 695765769 399 MHSD-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: 828.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 13 DTAIELDVLKGTLGQDVIDIRSLGS-KGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILL 91
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKqTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 92 NGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAYRLLSKMPT 171
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 172 MAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFA 251
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 252 CIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELG 331
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 332 TKDD-LLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSD-GMKIARP 409
Cdd:TIGR01798 321 LHDDpLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDpGQKIGRP 400
|
410
....*....|..
gi 695765769 410 RQLYTGYEKRDF 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: 808.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 18 LDVLKGTLGQDVIDIRSLGSK-GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKP 96
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKtGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 97 NQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAYRLLSKMPTMAAMC 176
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 177 YKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAG 256
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 257 IASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDL 336
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 337 LEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSD-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: 656.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 39 GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQI 118
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRND 191
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAhtgdlyqNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 192 LSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEA 271
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 272 ALKMLEEISSVEHIPEFVRRAKDKNdsFRLMGFGHRVYKNYDPRATVMRETCHEVLKELgTKDDLLEVAMELEHIALNDP 351
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEV-EKDPLLKVAMELERIALEDE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765769 352 YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSD-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 695765769 38 KGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQ 117
Cdd:COG0372 8 RAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 118 ITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGN 197
Cdd:COG0372 88 VKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD-IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 198 FLNMMFSTpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLE 277
Cdd:COG0372 167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 278 EISSVEHIPEFVRRAKDKndSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFIEKK 357
Cdd:COG0372 242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEYFIEKK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765769 358 LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:COG0372 319 LYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRADN-RIIRPRQIYVGPEDRDY 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: 548.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 46 GFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAF 125
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 126 RRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSt 205
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 206 pcetYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHI 285
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 286 PEFVRRAKDKNDsFRLMGFGHRVYKNYDPRATVMRETCHEVLKElGTKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFY 365
Cdd:pfam00285 236 EEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELAEE-GGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 695765769 366 SGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPR 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: 531.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 45 PGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHA 124
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 125 FRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFS 204
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARD-KSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 205 TpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:cd06118 160 E-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 285 IPEFVRraKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFieKKLYPNVDF 364
Cdd:cd06118 235 VEAYIW--KKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG-DDKLFEIAEELEEIALEVLGE--KGIYPNVDF 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 695765769 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARPRQLY 413
Cdd:cd06118 310 YSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
39-421 |
6.44e-180 |
|
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: 506.67 E-value: 6.44e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 39 GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQI 118
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNF 198
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 199 LNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEE 278
Cdd:cd06116 161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 279 ISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFIEKKL 358
Cdd:cd06116 241 IGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATG-RNPLLDIAVELEKIALEDEYFISRKL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765769 359 YPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSD-GMKIARPRQLYTGYEKRDF 421
Cdd:cd06116 318 YPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDpEQKIARPRQVYTGPRDRDY 381
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
11-415 |
2.21e-176 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 500.32 E-value: 2.21e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 11 GGDTAIELDVLKGTLGQDVIDIRSLG-SKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYI 89
Cdd:PLN02456 31 GKDYESPLSELGPVQAERLKKIKAGKdDLGLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 90 LLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHREIAA 162
Cdd:PLN02456 111 LLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYlrgqhkyKSWEVRDEDI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 163 YRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVR-T 241
Cdd:PLN02456 191 VRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 242 AGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRE 321
Cdd:PLN02456 271 VGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIRE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 322 TCHEVLKELGtKDDLLEVAMELEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHS 401
Cdd:PLN02456 349 FALEVFKHVG-DDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALG 427
|
410
....*....|....*
gi 695765769 402 D-GMKIARPRQLYTG 415
Cdd:PLN02456 428 LpDERIMRPKQVYTG 442
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
36-421 |
3.30e-163 |
|
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: 465.38 E-value: 3.30e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 36 GSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIH 115
Cdd:cd06115 18 DDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 116 EQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSldvnNP-------------RHREIaaYRLLSKMPTMAAMCYKYSIG 182
Cdd:cd06115 98 TGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEA----NPalagqdiyknkqvRDKQI--VRILGKAPTIAAAAYRRRAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 183 QPFVYPRNDLSYAGNFLNMMFSTPCETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWG 262
Cdd:cd06115 172 RPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 263 PAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAME 342
Cdd:cd06115 252 PLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVG-KDPLIEIAVA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 343 LEHIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSD-GMKIARPRQLYTGYEKRDF 421
Cdd:cd06115 329 LEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDpDTKIMRPQQLYTGVWLRHY 408
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
45-413 |
1.02e-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: 377.04 E-value: 1.02e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 45 PGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPnqeqynefktivtrhtmiheqitrlfha 124
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 125 frrdshpmavmcgitgalaafyhdsldvnnprhreiaayrllskmptmaamcykysigqpfvyprndlSYAGNFLNMMFS 204
Cdd:cd06101 53 --------------------------------------------------------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 205 TpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:cd06101 65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 285 IPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNDPYFieKKLYPNVDF 364
Cdd:cd06101 140 EPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG-LDPMFELAAELEKIAPEVLYE--KKLYPNVDF 216
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 695765769 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARPRQLY 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 |
2.70e-123 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and 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: 362.51 E-value: 2.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLF 122
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 123 HAFRRDSHPMAVMCGITGALAAFYHD-SLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM 201
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPKpEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 202 MFSTpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISS 281
Cdd:cd06112 161 LFGE-----EPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 282 VEHIPEFV--RRAKDKndsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELEHIALNdpYFIEKKLY 359
Cdd:cd06112 236 PENVKAYLdkKLANKQ----KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEE--LLGHKGVY 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765769 360 PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTG 415
Cdd:cd06112 310 PNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGDN-RIFRPTQIYIG 364
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
43-421 |
4.36e-120 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 354.26 E-value: 4.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLF 122
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 123 HAFRRDSHPMAVMCGITGALAAFYHDSlDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMM 202
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRR-ALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 203 FSTpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSV 282
Cdd:PRK14036 163 TER-----EPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 283 EHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIAlnDPYFIEKKLYPNV 362
Cdd:PRK14036 238 ENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFG-HDEYYEIALELERVA--EERLGPKGIYPNV 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765769 363 DFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:PRK14036 313 DFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGAN-RIFRPTQIYTGSHNRRY 370
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
52-421 |
1.99e-116 |
|
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.
Pssm-ID: 130859 Cd Length: 368 Bit Score: 344.73 E-value: 1.99e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 52 SCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHP 131
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 132 MAVMCGITGALAAFyHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTpcetyE 211
Cdd:TIGR01800 88 MDVLRTAVSYLGAL-DPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGE-----E 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 212 VNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:TIGR01800 162 PTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILK 371
Cdd:TIGR01800 242 ALENKE--RIMGFGHRVYKTYDPRAKILKEYA-KKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYY 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 695765769 372 AMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:TIGR01800 314 MMGIPTDLFTPIFAMSRVTGWTAHIIEQVENN-RLIRPRADYVGPEERKY 362
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
193-413 |
1.14e-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: 337.00 E-value: 1.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 193 SYAGNFLNMMFSTpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAA 272
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 273 LKMLEEISSVEHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELEHIALNDPY 352
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGD-DPMFELAAELEKIAEEVLY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765769 353 FieKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARPRQLY 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 |
1.43e-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: 331.93 E-value: 1.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 53 CESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPM 132
Cdd:cd06110 9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 133 AVMCGITGALAAfYHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMfstpceTYEV 212
Cdd:cd06110 89 DVLRTAVSALAL-YDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYML------TGEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 213 -NPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:cd06110 162 pSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILK 371
Cdd:cd06110 242 KLANKE--KIMGFGHRVYKTGDPRAKHLREMSRRLGKETG-EPKWYEMSEAIEQAMRD-----EKGLNPNVDFYSASVYY 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 695765769 372 AMGIPSSMFTVIFAMARTVGWIAHWNEMHsDGMKIARPRQLYTG 415
Cdd:cd06110 314 MLGIPVDLFTPIFAISRVSGWCAHILEQY-FNNRLIRPRAEYVG 356
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
54-422 |
4.34e-106 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 318.49 E-value: 4.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 54 ESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:NF041157 14 YTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 134 VMCGITGALAAFYHDSLDVNNPRHReiaAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVn 213
Cdd:NF041157 94 MMETAFSALASIENYKWNKENDREK---ALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATFGRKPSEEEI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 214 pvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRaK 293
Cdd:NF041157 170 ----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNE-N 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 294 DKNDSFRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDD---LLEVAMELEHIALNdpYFIEKKLYPNVDFYSGIIL 370
Cdd:NF041157 245 IINGKKRLMGFGHRVYKTYDPRAKIFK----EYAEKLASTNEakkYLEIAEKLEELGIK--HFGSKGIYPNTDFYSGIVF 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 695765769 371 KAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARPRQLYTGYEKRDFK 422
Cdd:NF041157 319 YSLGFPVYMFTSLFALSRVLGWLAHIIEYVEEQHRLIRPRALYVGPEKRDFV 370
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
54-421 |
3.10e-89 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 275.37 E-value: 3.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 54 ESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEF-KTIVTRHTM---IHEQITRLFHAfrrDS 129
Cdd:NF041301 16 ESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFsDAMAAEREVddgVLETVRALAAA---DE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 130 HPMAVMCGITGALAAfYHDSLDVNNPRHREIA---AYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTp 206
Cdd:NF041301 93 EPMAALRTAVSMLSA-YDPDADDADPTDREANlrkGRRITAKIPTILAAFARLRDGEDPVEPREDLSHAANFLYMLNGE- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 207 cetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIP 286
Cdd:NF041301 171 ----EPDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 287 -EFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELG-TKDDLLEVAMElEHIALndpyfiEKKLYPNVDF 364
Cdd:NF041301 247 vEWVKDALEEGR--RVPGFGHRVYNVKDPRAKILGEKSEELGEAAGdTKWYEYSVAIE-EYMTE------EKGLAPNVDF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765769 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:NF041301 318 YSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQYEDN-RLIRPRARYVGPKDREF 373
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
55-423 |
2.63e-86 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 267.77 E-value: 2.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 55 SKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAV 134
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 135 MCGITGALAAFYHDSLdvNNPRHREIAAyRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVNp 214
Cdd:PRK14037 96 MEAAFAALASIDKNFK--WKENDKEKAI-SIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTAEEIK- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 215 vlerAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRaKD 294
Cdd:PRK14037 172 ----AMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFND-KI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 295 KNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELEHIALNDpyFIEKKLYPNVDFYSGIILKAMG 374
Cdd:PRK14037 247 INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALG 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 695765769 375 IPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARPRQLYTGYEKRDFKS 423
Cdd:PRK14037 325 FPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEHREYVP 373
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
46-421 |
4.41e-85 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 264.70 E-value: 4.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 46 GFTSTASCESKITFIDGDEgiLLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAF 125
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 126 RRDS-HPMAVMCGITGALAAFYHDSLDVNNPRHREiAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFS 204
Cdd:PRK14035 84 STDHvHPMTALRTSVSYLAHFDPDAEEESDEARYE-RAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 205 TpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:PRK14035 163 E-----LPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14035 238 VDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRKITKGTG-REELFEMSVKIEKRMKE-----EKGLIPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765769 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:PRK14035 310 YSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKDN-RIMRPRAKYIGETNRKY 365
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
54-415 |
3.60e-83 |
|
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: 258.77 E-value: 3.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 54 ESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFrrdsHPMA 133
Cdd:cd06109 10 ETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL----AGLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 134 VMCGITGALAAFyhdsldvnNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCETYEVn 213
Cdd:cd06109 86 PMDALRALLALL--------PDSPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGEPPSEAHV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 214 pvleRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAK 293
Cdd:cd06109 157 ----RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 294 DKNDsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELEHIALN--DPYFIEKKLYPNVDFYSGIILK 371
Cdd:cd06109 233 ARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLGAPDERLEFAEAVEQAALAllREYKPGRPLETNVEFYTALLLE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 695765769 372 AMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTG 415
Cdd:cd06109 307 ALGLPREAFTPTFAAGRTAGWTAHVLEQARTG-RLIRPQSRYVG 349
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
54-420 |
1.05e-82 |
|
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: 258.11 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 54 ESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:cd06111 10 TTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 134 VMCGITGALAAFyHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTpcetyEVN 213
Cdd:cd06111 90 VLRTAVSVLGAE-DSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGE-----VPS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 214 PVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAK 293
Cdd:cd06111 164 PEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 294 DKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELehialndpyfiEKKLYPNVDFYSGI 368
Cdd:cd06111 244 ARKE--KVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKwlamyDALEDAMVA-----------AKGIKPNLDFPAGP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 695765769 369 ILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRD 420
Cdd:cd06111 311 AYYLMGFDIDFFTPIFVMARITGWTAHIMEQRADN-ALIRPLSEYNGPEQRP 361
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
46-423 |
7.72e-82 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 256.23 E-value: 7.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 46 GFTSTASCESKItfIDGdegILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAF 125
Cdd:PRK14034 9 GVVATTSSVSSI--IDD---TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 126 RRDS-HPMAVMcGITGALAAFYHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFS 204
Cdd:PRK14034 84 DLKKvHPMSVL-RTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 205 TpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEH 284
Cdd:PRK14034 163 E-----EPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14034 238 VESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKRLTVLLG-EEKWYNMSIKIEEIVTK-----EKGLPPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765769 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIaRPRQLYTGYEKRDFKS 423
Cdd:PRK14034 310 YSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYENNRLI-RPRADYVGPTHQVYVP 367
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
62-421 |
1.16e-79 |
|
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: 250.30 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 62 GDEGILLH-RGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITG 140
Cdd:cd06108 17 GKGGKGLTyRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 141 ALAAFYHDsldvNNPRHREIAAYRLLSKMPTMAAMCYKYS-IGQPFVYPRNDLSYAGNFLNMMFSTPCEtyevnPVLERA 219
Cdd:cd06108 97 MLGCLEPE----NEFSQQYEIAIRLLAIFPSILLYWYHYShSGKRIETETDEDSIAGHFLHLLHGKKPG-----ELEIKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsf 299
Cdd:cd06108 168 MDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLEKLERKE-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 300 RLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKAMGIPSSM 379
Cdd:cd06108 246 LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSASAYHFCGIPTEL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 695765769 380 FTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:cd06108 320 FTPIFVMSRVTGWAAHIMEQRANN-RLIRPSADYIGPEPRPF 360
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
42-415 |
3.68e-76 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 241.55 E-value: 3.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 42 TFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRL 121
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 122 FHAFRRDSHPM-AVMCGITgALAAF---YHD-SLDVNnpRHReiaAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAG 196
Cdd:PRK12349 84 LKALPKETHPMdGLRTGVS-ALAGYdndIEDrSLEVN--KSR---AYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 197 NFLNMMFSTpcetyEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKML 276
Cdd:PRK12349 158 NFLYMLTGK-----KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYML 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 277 EEISSVEHIPEFVRR---AKDKndsfrLMGFGHRVY-KNYDPRATVMRETchevLKELGTK---DDLLEVAMELEHIALN 349
Cdd:PRK12349 233 LEAGTVEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMKEA----LKQLCDVkgdYTLYEMCEAGEKIMEK 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765769 350 dpyfiEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTG 415
Cdd:PRK12349 304 -----EKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHANN-RLFRPRVNYIG 363
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
67-420 |
4.64e-75 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 238.70 E-value: 4.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 67 LLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFy 146
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 147 HDSLDVNNPRHREIAAYRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTpcetyEVNPVLERAMDRILIL 226
Cdd:PRK14033 112 DPEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFGE-----VPEPEVVRAFEVSLIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 227 HADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDsfRLMGFGH 306
Cdd:PRK14033 187 YAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKE--KVMGFGH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 307 RVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELehialndpyfiEKKLYPNVDFYSGIILKAMGIPSSMFT 381
Cdd:PRK14033 265 RVYKHGDSRVPTMKAALRRVAAVRDGQRwldiyEALEKAMAE-----------ATGIKPNLDFPAGPAYYLMGFDIDFFT 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 695765769 382 VIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRD 420
Cdd:PRK14033 334 PIFVMSRITGWTAHIMEQRASN-ALIRPLSEYNGPEQRE 371
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
67-421 |
2.60e-67 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 219.02 E-value: 2.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 67 LLHRGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVM---CGITGALA 143
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMrtgVSVLGCLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 144 AFYHDSldvNNPRHREIAAyRLLSKMPTMaaMCYKYSI---GQPFVYPRNDLSYAGNFLNMMF-STPCETYEvnpvleRA 219
Cdd:PRK12351 112 PEKEDH---NFSGARDIAD-RLLASLGSI--LLYWYHYshnGRRIEVETDDDSIGGHFLHLLHgKKPSESWV------KA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR---AKDKn 296
Cdd:PRK12351 180 MHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRrveNKEV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 297 dsfrLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKAMGIP 376
Cdd:PRK12351 259 ----VIGFGHPVYTISDPRNKVIKEVAKKLSKEAGD-TKLYDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 695765769 377 SSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 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 |
1.51e-61 |
|
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: 203.54 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 62 GDEGILLH-RGFPIDQLATESNYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITG 140
Cdd:cd06117 17 GRSGNDLHyRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 141 ALAAFYHDSLDVNNPRHREIAAyRLLSKMPTMAAMCYKYSI-GQPFVYPRNDLSYAGNFLNMMF-STPCETYEvnpvleR 218
Cdd:cd06117 97 VLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYSHnGKRIEVETDDDSIGGHFLHLLHgEKPSESWE------K 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 219 AMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRRAKDKNDS 298
Cdd:cd06117 170 AMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVENKEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 299 frLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKdDLLEVAMELEHIALNdpyfiEKKLYPNVDFYSGIILKAMGIPSS 378
Cdd:cd06117 250 --VIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDM-KMFDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTA 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 695765769 379 MFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:cd06117 322 MFTPLFVIARTTGWSAHIIEQRQDG-KIIRPSANYTGPEDLKF 363
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
63-409 |
8.92e-60 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 201.29 E-value: 8.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 63 DEGILLHRGFPIDQLATES------NYLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLF--HAFRRDshpmaV 134
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNGFlkekrfGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRDMilKAPSKD-----I 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 135 MCGITGALAAFYhdSLDVN----NPRHREIAAYRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLNMMfs 204
Cdd:PRK14032 139 MNSLARSVLALY--SYDDNpddtSIDNVLRQSISLIARFPTLAVYAYQayrhYHDGKSLYihPPKPELSTAENILYML-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 205 TPCETYEvnPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI---- 279
Cdd:PRK14032 215 RPDNKYT--ELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIkenv 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 280 ---SSVEHIPEFVRRAKDK---NDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELEHIAlndPYF 353
Cdd:PRK14032 293 kdwEDEDEIADYLTKILNKeafDKSGLIYGMGHAVYTISDPRAVILKKFAEKLAKEKG-REEEFNLYEKIEKLA---PEL 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765769 354 I--EKKLY----PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARP 409
Cdd:PRK14032 369 IaeERGIYkgvsANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGGKIIRP 430
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
43-415 |
1.47e-59 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 197.88 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATESNYLEVCYILLNGE----KPNQEQYNefktiVTRHTmiheqi 118
Cdd:PRK12350 1 FVPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRfgpgLPPAEPFP-----LPVHL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 119 trlfHAFRRDSHPMAVMCGITGALAAFyhdsLDVNNPRHRE--IAAyrllSKMPTMAAMCYKYSIGQPFVyPRNDLSYAG 196
Cdd:PRK12350 70 ----GDARVDVQAALAMLAPVWGFRPL----LDIDDLTARLdlARA----SVMALSAVAQSARGIGQPAV-PQREIDHAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 197 NFLNMMFSTpcETYEVNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKML 276
Cdd:PRK12350 137 TILERFMGR--WRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPML 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 277 EEISSVEHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETChevlKELGTkdDLLEVAMELEHIALNDpyFIEK 356
Cdd:PRK12350 215 DAVERTGDARGWVKGALDRGE--RLMGFGHRVYRAEDPRARVLRATA----KRLGA--PRYEVAEAVEQAALAE--LRER 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765769 357 K----LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGmKIARPRQLYTG 415
Cdd:PRK12350 285 RpdrpLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTG-RLVRPSARYVG 346
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
63-409 |
1.57e-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: 196.72 E-value: 1.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 63 DEGILLHRGFPIDQL---ATESN---YLEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMC 136
Cdd:cd06113 34 CPGKLYYRGYDVEDLvngAQKENrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 137 GITGALAAfYHDSLDVNNPRHREIAAYRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLNMMFSTPCETY 210
Cdd:cd06113 114 RSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrhYYDGESLYihHPQPELSTAENILSMLRPDKKYTE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 211 EVNPVLeramDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI-------SSV 282
Cdd:cd06113 193 LEAKLL----DLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIkenvkdwTDE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 283 EHIPEFVRRAKDK--NDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKELGTKD--DLLEVAMELEHIALNDPYFIEKK 357
Cdd:cd06113 269 DEVRAYLRKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEefALYERIERLAPEVIAEERGIGKT 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 695765769 358 LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIARP 409
Cdd:cd06113 349 VCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRP 400
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
57-415 |
1.36e-42 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 155.29 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 57 ITFIDGDEGILLhRGFPIDQL------ATESNY---LEVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRR 127
Cdd:PRK09569 52 ISYLDPQEGIRF-RGKTIPETfealpkAPGSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 128 DSHPMAVM-CGIT-----GALAAFYHDS----LDVNNPRHREiaAYRLLSKMPTMAAMCY--KYSIGQPfVYPRNDLSYA 195
Cdd:PRK09569 131 DSHPMVMLsVGILamqreSKFAKFYNEGkfnkMDAWEYMYED--ASDLVARIPVIAAYIYnlKYKGDKQ-IPSDPELDYG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 196 GNFLNMMfstpcetyEVNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL- 273
Cdd:PRK09569 208 ANFAHMI--------GQPKPYKDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 274 ---KMLEEISSVEHIPEFVRRA-KDKNDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLEVAMEL----- 343
Cdd:PRK09569 280 wiqQFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLFKLVAMIfevap 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765769 344 ----EHIALNDPyfiekklYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAHWNEMHSDGMKIARPRQLYTG 415
Cdd:PRK09569 356 gvltEHGKTKNP-------WPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTE 425
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
212-415 |
5.80e-42 |
|
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: 149.72 E-value: 5.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 212 VNPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVEHIPEFVRR 291
Cdd:cd06102 93 LDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKE-LGTKDDLLEVAMELEHialndpyfiekkLYPNVDFYSGIIL 370
Cdd:cd06102 173 RLRRGE--ALPGFGHPLYPDGDPRAAALLAALRPLGPAaPPAARALIEAARALTG------------ARPNIDFALAALT 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695765769 371 KAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIaRPRQLYTG 415
Cdd:cd06102 239 RALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLI-RPRARYVG 282
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
17-412 |
2.88e-35 |
|
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: 135.12 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 17 ELDVLKGTLGQDVIDIRSL-----GSKGVFTFdpgFTSTASCeskitfiDGDEGILLhRGFPIDQL------ATESNY-- 83
Cdd:cd06103 15 RIKELRKKYGNTKLGQITVdqvigGMRGMKGL---VYETSVL-------DPDEGIRF-RGKTIPECqellpkADGGGEpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 84 LEVC-YILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSHPMAVMCGitgALAAFYHDSL--------DVNN 154
Cdd:cd06103 84 PEGLfWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSA---AILALQSESKfakayaegKINK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 155 PRHREIA---AYRLLSKMPTMAAMCYKYSIGQ-PFVYPRN-DLSYAGNFLNMMfstpceTYEvNPVLERAMDRILILHAD 229
Cdd:cd06103 161 TTYWEYVyedAMDLIAKLPVVAAKIYRRKYRKgGEIGAIDsKLDWSANFAHML------GYE-DEEFTDLMRLYLTLHSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 230 HEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL----KMLEEISSVEHIPEFVRRAKDKNDSFRLM-G 303
Cdd:cd06103 234 HEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLkwllKMQKELGKDVSDEELEKYIWDTLNSGRVVpG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 304 FGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLEVAMELEHIAlndPYFIE-----KKLYPNVDFYSGIILKAMGIPS- 377
Cdd:cd06103 314 YGHAVLRKTDPRFTCQREFALKHLPD----DPLFKLVAQCYKII---PGVLKehgkvKNPYPNVDAHSGVLLQHYGMTEp 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 695765769 378 SMFTVIFAMARTVGWIAH--WNEMHsdGMKIARPRQL 412
Cdd:cd06103 387 QYYTVLFGVSRALGVLAQlvWSRAL--GLPIERPKSM 421
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
60-415 |
3.04e-28 |
|
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: 115.54 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 60 IDGDEGILLhRGFPI----DQLATESNYLE-----VCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRDSH 130
Cdd:cd06105 53 LDPEEGIRF-RGLSIpecqKLLPKAPGGEEplpegLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 131 PMA-VMCGITgAL---AAF-----------------YHDSLDvnnprhreiaayrLLSKMPTMAAMCYK--YSIGQpFVY 187
Cdd:cd06105 132 PMSqLSAAIT-ALnseSKFakayaegihkskyweyvYEDSMD-------------LIAKLPCVAAKIYRnlYRGGK-IIA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 188 PRNDLSYAGNFLNMMfstpceTYEvNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHG 266
Cdd:cd06105 197 IDSNLDWSANFANML------GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 267 GANEAAL----KMLEEIS---SVEHIPEFVRrakDKNDSFRLM-GFGHRVYKNYDPRATVMRETChevLKELgTKDDLLE 338
Cdd:cd06105 270 LANQEVLvwltKLQKEVGkdvSDEQLREYVW---KTLNSGRVVpGYGHAVLRKTDPRYTCQREFA---LKHL-PNDPLFK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 339 VAMELEHIAlnDPYFIE----KKLYPNVDFYSGIILKAMGIPS-SMFTVIFAMARTVGWIAH--WNEmhSDGMKIARPRQ 411
Cdd:cd06105 343 LVSQLYKIV--PPVLTEqgkaKNPWPNVDAHSGVLLQYYGLTEmNYYTVLFGVSRALGVLSQliWDR--ALGLPLERPKS 418
|
....
gi 695765769 412 LYTG 415
Cdd:cd06105 419 VSTD 422
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
58-412 |
3.73e-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: 112.21 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 58 TFIDGDEGILLHrGFPIDQLATE-------SNYL--EVCYILLNGEKPNQEQYNEFKTIVTRHTMIHEQITRLFHAFRRD 128
Cdd:cd06106 51 SVLDAEEGIRFH-GKTIPECQKElpkapigGEMLpeSMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 129 SHPMAvmcGITGALAAFYHDSL-------DVNNPRHREIA---AYRLLSKMPTMAAMCYKYS----IGQPFVYPRNDLSY 194
Cdd:cd06106 130 LHPMT---QLSIGVAALNHDSKfaaayekGIKKTEYWEPTledSLNLIARLPALAARIYRNVygegHGLGKIDPEVDWSY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 195 agNFLNMMfstpceTYEVNPVLERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL 273
Cdd:cd06106 207 --NFTSML------GYGDNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 274 K----MLEEISSVEHIPEFVRRAKDKNDSFRLM-GFGHRVYKNYDPRATVMRETChEVLKELgTKDDLLEVAMELEHIAl 348
Cdd:cd06106 279 RwileMQKNIGSKATDQDIRDYLWKTLKSGRVVpGYGHAVLRKPDPRFTALMEFA-QTRPEL-ENDPVVQLVQKLSEIA- 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765769 349 nDPYFIE----KKLYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAH--WNEMHsdGMKIARPRQL 412
Cdd:cd06106 356 -PGVLTEhgktKNPFPNVDAASGVLFYHYGIREFLYyTVIFGVSRALGPLTQlvWDRIL--GLPIERPKSL 423
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
218-408 |
5.89e-25 |
|
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: 101.88 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 218 RAMDRILILHADH-EQNASTSTVRTAGSSGANPF-ACIAAGIASLwGPAHGGANEAALKMLEEI-----SSVEHIPEFVR 290
Cdd:cd06100 32 RLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgdALDAAAAEFVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 291 RAKDKNdsFRLMGFGHRVYKNYDPRATVMretcHEVLKELGTKDDLLEVAMELEHIALNDPyfiEKKLYPNVDFYSGIIL 370
Cdd:cd06100 111 EYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGPAGPHLDYALAVEKALTAAK---GKPLPLNVDGAIAAIL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 695765769 371 KAMGIPSSMFTVIFAMARTVGWIAHWNEMHSDGMKIAR 408
Cdd:cd06100 182 LDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYR 219
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
213-421 |
2.53e-21 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 92.63 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 213 NPVLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEI----SSVEHIPEF 288
Cdd:PRK06224 51 TPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaaDAGADLDAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 289 VR------RAKDKndsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELEHIalndpyFIE---KKLY 359
Cdd:PRK06224 130 ARaivaeyRAAGK----RVPGFGHPLHKPVDPRAPRLL----ALAREAGVAGRHCRLAEALEAA------LAAakgKPLP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765769 360 PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAH-WNEMHS-DGMKIARPRQL---YTGYEKRDF 421
Cdd:PRK06224 196 LNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHvWEELQQpIGFRIWDPAEEaveYTGPPPREL 262
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
220-395 |
1.06e-06 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 50.97 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 220 MDRILILHADHEQNASTS--TVRTAgSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEISSVEHIP-EFVRRAKDKN 296
Cdd:PLN02522 403 IEMCIMLCADHGPCVSGAhnTIVTA-RAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMKKKG 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765769 297 dsFRLMGFGHRVYK--NYDPRATVMRETCHEVLKELgtkdDLLEVAMELEHIALNDpyfiEKKLYPNVDFYSGIILKAMG 374
Cdd:PLN02522 481 --IRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSV----KYMEYAVQVETYTLSK----ANNLVLNVDGAIGSLFLDLL 550
|
170 180 190
....*....|....*....|....*....|....*
gi 695765769 375 IPSSMFTV--------------IFAMARTVGWIAH 395
Cdd:PLN02522 551 AGSGMFTKqeideiveigylngLFVLARSIGLIGH 585
|
|
| |
