|
Name |
Accession |
Description |
Interval |
E-value |
| gltA |
PRK05614 |
citrate synthase; |
1-416 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 922.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 1 MADTKAKLTLN-GDTAVELDVLKGTLGQDVIDIRTL-GSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLA 78
Cdd:PRK05614 1 MADKKATLTLNgGEASVELPILKGTLGPDVIDIRKLyGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 79 TDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHR 158
Cdd:PRK05614 81 EKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 159 EIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTST 238
Cdd:PRK05614 161 EIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 239 VRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATV 318
Cdd:PRK05614 241 VRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 319 MRETCHEVLKELGTKDDLLEVAMELENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSE 398
Cdd:PRK05614 321 MRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNE 400
|
410
....*....|....*....
gi 16128695 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: 839.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 13 DTAVELDVLKGTLGQDVIDIRTLGS-KGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILL 91
Cdd:TIGR01798 1 NKSVELPIYSGTLGPDVIDIRKLYKqTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 92 NGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPT 171
Cdd:TIGR01798 81 YGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 172 MAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFA 251
Cdd:TIGR01798 161 LAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 252 CIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELG 331
Cdd:TIGR01798 241 CIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 332 TKDD-LLEVAMELENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD-GMKIARP 409
Cdd:TIGR01798 321 LHDDpLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDpGQKIGRP 400
|
410
....*....|..
gi 16128695 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: 811.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 18 LDVLKGTLGQDVIDIRTLGSK-GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKP 96
Cdd:cd06114 1 LPVLEGTEGEKVIDISSLRKKtGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 97 TQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMC 176
Cdd:cd06114 81 TAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 177 YKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAG 256
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 257 IASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDL 336
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 337 LEVAMELENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD-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: 668.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 39 GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQI 118
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRND 191
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAhtgdlyqNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 192 LSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEA 271
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 272 ALKMLEEISSVKHIPEFVRRAKDKNdsFRLMGFGHRVYKNYDPRATVMRETCHEVLKELgTKDDLLEVAMELENIALNDP 351
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEV-EKDPLLKVAMELERIALEDE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128695 352 YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD-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: 652.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 38 KGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQ 117
Cdd:COG0372 8 RAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 118 ITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGN 197
Cdd:COG0372 88 VKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD-IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 198 FLNMMFSTpcepyEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLE 277
Cdd:COG0372 167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 278 EISSVKHIPEFVRRAKDKndSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNDPYFIEKK 357
Cdd:COG0372 242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEYFIEKK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128695 358 LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 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 16128695 46 GFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 126 RRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSt 205
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 206 pcepYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHI 285
Cdd:pfam00285 160 ----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 286 PEFVRRAKDKNDsFRLMGFGHRVYKNYDPRATVMRETCHEVLKElGTKDDLLEVAMELENIALNDPYFIEKKLYPNVDFY 365
Cdd:pfam00285 236 EEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELAEE-GGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16128695 366 SGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPR 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: 538.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 45 PGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHA 124
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 125 FRRDSHPMAVMCGITGALAAFYHDSLDvNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFS 204
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARD-KSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 205 TpcepyEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKH 284
Cdd:cd06118 160 E-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 285 IPEFVRraKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNDPYFieKKLYPNVDF 364
Cdd:cd06118 235 VEAYIW--KKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG-DDKLFEIAEELEEIALEVLGE--KGIYPNVDF 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16128695 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLY 413
Cdd:cd06118 310 YSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
39-421 |
1.89e-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: 508.21 E-value: 1.89e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 39 GVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQI 118
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 119 TRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNF 198
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 199 LNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEE 278
Cdd:cd06116 161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 279 ISSVKHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNDPYFIEKKL 358
Cdd:cd06116 241 IGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATG-RNPLLDIAVELEKIALEDEYFISRKL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128695 359 YPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD-GMKIARPRQLYTGYEKRDF 421
Cdd:cd06116 318 YPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDpEQKIARPRQVYTGPRDRDY 381
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
13-415 |
4.13e-178 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 504.94 E-value: 4.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 13 DTAVELDVLKGTLGQDVIDIRTLG-SKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILL 91
Cdd:PLN02456 33 DYESPLSELGPVQAERLKKIKAGKdDLGLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 92 NGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDV-------NNPRHREIAAFR 164
Cdd:PLN02456 113 YGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYlrgqhkyKSWEVRDEDIVR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 165 LLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVR-TAG 243
Cdd:PLN02456 193 LIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 244 SSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETC 323
Cdd:PLN02456 273 SSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIREFA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 324 HEVLKELGtKDDLLEVAMELENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD- 402
Cdd:PLN02456 351 LEVFKHVG-DDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLp 429
|
410
....*....|...
gi 16128695 403 GMKIARPRQLYTG 415
Cdd:PLN02456 430 DERIMRPKQVYTG 442
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
36-421 |
8.05e-164 |
|
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.
Pssm-ID: 99868 Cd Length: 410 Bit Score: 466.92 E-value: 8.05e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 36 GSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIH 115
Cdd:cd06115 18 DDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 116 EQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSldvnNP-------------RHREIaaFRLLSKMPTMAAMCYKYSIG 182
Cdd:cd06115 98 TGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEA----NPalagqdiyknkqvRDKQI--VRILGKAPTIAAAAYRRRAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 183 QPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWG 262
Cdd:cd06115 172 RPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 263 PAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAME 342
Cdd:cd06115 252 PLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVG-KDPLIEIAVA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 343 LENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSD-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 |
3.00e-133 |
|
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: 383.59 E-value: 3.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 45 PGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPtqeqydefkttvtrhtmiheqitrlfha 124
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 125 frrdshpmavmcgitgalaafyhdsldvnnprhreiaafrllskmptmaamcykysigqpfvyprndlSYAGNFLNMMFS 204
Cdd:cd06101 53 --------------------------------------------------------------------SYAENFLYMLGG 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 205 TpcepyEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKH 284
Cdd:cd06101 65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 285 IPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNDPYFieKKLYPNVDF 364
Cdd:cd06101 140 EPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG-LDPMFELAAELEKIAPEVLYE--KKLYPNVDF 216
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16128695 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLY 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 |
2.43e-124 |
|
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: 365.21 E-value: 2.43e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLF 122
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 123 HAFRRDSHPMAVMCGITGALAAFYHD-SLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM 201
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPKpEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 202 MFSTpcEPYevnPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISS 281
Cdd:cd06112 161 LFGE--EPD---PATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 282 VKHIPEFV--RRAKDKndsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNdpYFIEKKLY 359
Cdd:cd06112 236 PENVKAYLdkKLANKQ----KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEE--LLGHKGVY 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128695 360 PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTG 415
Cdd:cd06112 310 PNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGDN-RIFRPTQIYIG 364
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
43-427 |
1.11e-120 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 355.80 E-value: 1.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLF 122
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 123 HAFRRDSHPMAVMCGITGALAAFYHDSlDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMM 202
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRR-ALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 203 fsTPCEPyevNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSV 282
Cdd:PRK14036 163 --TEREP---DPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 283 KHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIAlnDPYFIEKKLYPNV 362
Cdd:PRK14036 238 ENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFG-HDEYYEIALELERVA--EERLGPKGIYPNV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128695 363 DFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDFKSDIKR 427
Cdd:PRK14036 313 DFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGAN-RIFRPTQIYTGSHNRRYIPLEER 376
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
52-421 |
5.73e-119 |
|
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: 351.28 E-value: 5.73e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 52 SCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHP 131
Cdd:TIGR01800 8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 132 MAVMCGITGALAAFyHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTpcEPye 211
Cdd:TIGR01800 88 MDVLRTAVSYLGAL-DPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGE--EP-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 212 vNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRR 291
Cdd:TIGR01800 163 -TKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELENIALNdpyfiEKKLYPNVDFYSGIILK 371
Cdd:TIGR01800 242 ALENKE--RIMGFGHRVYKTYDPRAKILKEYA-KKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYY 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16128695 372 AMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 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 |
1.46e-117 |
|
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: 341.62 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 193 SYAGNFLNMMFSTpcepyEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAA 272
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 273 LKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELENIALNDPY 352
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGD-DPMFELAAELEKIAEEVLY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128695 353 FieKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLY 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 |
1.62e-113 |
|
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99863 [Multi-domain] Cd Length: 356 Bit Score: 336.94 E-value: 1.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 53 CESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPM 132
Cdd:cd06110 9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 133 AVMCGITGALAAfYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMfsTPCEPyev 212
Cdd:cd06110 89 DVLRTAVSALAL-YDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYML--TGEKP--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 213 NPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRA 292
Cdd:cd06110 163 SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVKDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 293 KDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNdpyfiEKKLYPNVDFYSGIILKA 372
Cdd:cd06110 243 LANKE--KIMGFGHRVYKTGDPRAKHLREMSRRLGKETG-EPKWYEMSEAIEQAMRD-----EKGLNPNVDFYSASVYYM 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16128695 373 MGIPSSMFTVIFAMARTVGWIAHWSEMHsDGMKIARPRQLYTG 415
Cdd:cd06110 315 LGIPVDLFTPIFAISRVSGWCAHILEQY-FNNRLIRPRAEYVG 356
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
54-422 |
9.89e-106 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 317.72 E-value: 9.89e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 54 ESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:NF041157 14 YTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 134 VMCGITGALAAFYHDSLDVNNPRHReiaAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVn 213
Cdd:NF041157 94 MMETAFSALASIENYKWNKENDREK---ALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATFGRKPSEEEI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 214 pileRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRaK 293
Cdd:NF041157 170 ----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKWFNE-N 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 294 DKNDSFRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDD---LLEVAMELENIALNdpYFIEKKLYPNVDFYSGIIL 370
Cdd:NF041157 245 IINGKKRLMGFGHRVYKTYDPRAKIFK----EYAEKLASTNEakkYLEIAEKLEELGIK--HFGSKGIYPNTDFYSGIVF 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16128695 371 KAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTGYEKRDFK 422
Cdd:NF041157 319 YSLGFPVYMFTSLFALSRVLGWLAHIIEYVEEQHRLIRPRALYVGPEKRDFV 370
|
|
| Cit_synth_Halo_CitZ |
NF041301 |
citrate synthase; |
54-421 |
1.25e-89 |
|
citrate synthase;
Pssm-ID: 469198 Cd Length: 379 Bit Score: 276.52 E-value: 1.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 54 ESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRH----TMIHEQITRLFHAfrrDS 129
Cdd:NF041301 16 ESELSYIDGDAGRLVYRGYDIEDLAREASYEEVLYLLWHGELPTEEELAEFSDAMAAErevdDGVLETVRALAAA---DE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 130 HPMAVMCGITGALAAfYHDSLDVNNPRHREIA---AFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMfsTP 206
Cdd:NF041301 93 EPMAALRTAVSMLSA-YDPDADDADPTDREANlrkGRRITAKIPTILAAFARLRDGEDPVEPREDLSHAANFLYML--NG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 207 CEPYEVnpiLERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIP 286
Cdd:NF041301 170 EEPDEV---LAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLSGSLHGGANQDVMRMLKEVDESDKDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 287 -EFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETchevLKELG-TKDDL--LEVAMELENialndpYFIEKK-LYPN 361
Cdd:NF041301 247 vEWVKDALEEGR--RVPGFGHRVYNVKDPRAKILGEK----SEELGeAAGDTkwYEYSVAIEE------YMTEEKgLAPN 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 362 VDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:NF041301 315 VDFYSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQYEDN-RLIRPRARYVGPKDREF 373
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
46-421 |
7.11e-87 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 269.32 E-value: 7.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 46 GFTSTASCESKITFIDGDEgiLLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:PRK14035 6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 126 RRDS-HPMAVMCGITGALAAFYHDSLDVNNPRHREiAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFS 204
Cdd:PRK14035 84 STDHvHPMTALRTSVSYLAHFDPDAEEESDEARYE-RAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 205 TpcEPYEVNpilERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKH 284
Cdd:PRK14035 163 E--LPTDIE---VEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14035 238 VDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRKITKGTG-REELFEMSVKIEKRMKE-----EKGLIPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128695 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:PRK14035 310 YSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKDN-RIMRPRAKYIGETNRKY 365
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
55-427 |
9.72e-86 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 266.61 E-value: 9.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 55 SKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAV 134
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 135 MCGITGALAAFYHDSLdvNNPRHREIAAfRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNp 214
Cdd:PRK14037 96 MEAAFAALASIDKNFK--WKENDKEKAI-SIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTAEEIK- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 215 ilerAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRaKD 294
Cdd:PRK14037 172 ----AMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFND-KI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 295 KNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDpyFIEKKLYPNVDFYSGIILKAMG 374
Cdd:PRK14037 247 INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALG 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16128695 375 IPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTGYEKRDFKSDIKR 427
Cdd:PRK14037 325 FPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
54-415 |
6.93e-84 |
|
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: 260.70 E-value: 6.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 54 ESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFrrdsHPMA 133
Cdd:cd06109 10 ETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL----AGLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 134 VMCGITGALAAFyhdsldvnNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVn 213
Cdd:cd06109 86 PMDALRALLALL--------PDSPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGEPPSEAHV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 214 pileRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAK 293
Cdd:cd06109 157 ----RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 294 DKNDsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELENIALN--DPYFIEKKLYPNVDFYSGIILK 371
Cdd:cd06109 233 ARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLGAPDERLEFAEAVEQAALAllREYKPGRPLETNVEFYTALLLE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16128695 372 AMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTG 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 |
7.90e-83 |
|
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. DsCS, compared with CS from the hyperthermophile Pyrococcus furiosus (not included in this group), has an increase in the size of surface loops, a higher proline content in the loop regions, a more accessible active site, and a higher number of intramolecular ion pairs. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. For example, included in this group are Corynebacterium glutamicum (Cg) PrpC1 and -2, which are only synthesized during growth on propionate-containing medium, can use PrCoA, AcCoA and butyryl-CoA as substrates, and have comparable catalytic activity with AcCoA as the major CgCS (GltA, not included in this group).
Pssm-ID: 99864 [Multi-domain] Cd Length: 362 Bit Score: 258.49 E-value: 7.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 54 ESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMA 133
Cdd:cd06111 10 TTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 134 VMCGITGALAAFyHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVn 213
Cdd:cd06111 90 VLRTAVSVLGAE-DSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGEVPSPEVV- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 214 pileRAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAK 293
Cdd:cd06111 168 ----RAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 294 DKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELenialndpyfiEKKLYPNVDFYSGI 368
Cdd:cd06111 244 ARKE--KVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKwlamyDALEDAMVA-----------AKGIKPNLDFPAGP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16128695 369 ILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRD 420
Cdd:cd06111 311 AYYLMGFDIDFFTPIFVMARITGWTAHIMEQRADN-ALIRPLSEYNGPEQRP 361
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
46-423 |
2.32e-82 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 257.77 E-value: 2.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 46 GFTSTASCESKItfIDGdegILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAF 125
Cdd:PRK14034 9 GVVATTSSVSSI--IDD---TLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 126 RRDS-HPMAVMcGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMfs 204
Cdd:PRK14034 84 DLKKvHPMSVL-RTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYML-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 205 TPCEPyevNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKH 284
Cdd:PRK14034 161 NGEEP---DEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 285 IPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIALNdpyfiEKKLYPNVDF 364
Cdd:PRK14034 238 VESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKRLTVLLG-EEKWYNMSIKIEEIVTK-----EKGLPPNVDF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128695 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIaRPRQLYTGYEKRDFKS 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 |
1.55e-81 |
|
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: 255.31 E-value: 1.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 62 GDEGILLH-RGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITG 140
Cdd:cd06108 17 GKGGKGLTyRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 141 ALAAFYHDsldvNNPRHREIAAFRLLSKMPTMAAMCYKYS-IGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVnpileRA 219
Cdd:cd06108 97 MLGCLEPE----NEFSQQYEIAIRLLAIFPSILLYWYHYShSGKRIETETDEDSIAGHFLHLLHGKKPGELEI-----KA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDsf 299
Cdd:cd06108 168 MDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLEKLERKE-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 300 RLMGFGHRVYKNYDPRATVMRETChEVLKELGTKDDLLEVAMELENIALNdpyfiEKKLYPNVDFYSGIILKAMGIPSSM 379
Cdd:cd06108 246 LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSASAYHFCGIPTEL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16128695 380 FTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:cd06108 320 FTPIFVMSRVTGWAAHIMEQRANN-RLIRPSADYIGPEPRPF 360
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
42-415 |
8.35e-76 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 240.39 E-value: 8.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 42 TFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRL 121
Cdd:PRK12349 4 KFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 122 FHAFRRDSHPM-AVMCGITgALAAF---YHD-SLDVNnpRHReiaAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAG 196
Cdd:PRK12349 84 LKALPKETHPMdGLRTGVS-ALAGYdndIEDrSLEVN--KSR---AYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 197 NFLNMMfsTPCEPyevNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKML 276
Cdd:PRK12349 158 NFLYML--TGKKP---TELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYML 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 277 EEISSVKHIPEFVRR---AKDKndsfrLMGFGHRVY-KNYDPRATVMRETchevLKELGTK---DDLLEVAMELENIALN 349
Cdd:PRK12349 233 LEAGTVEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMKEA----LKQLCDVkgdYTLYEMCEAGEKIMEK 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128695 350 dpyfiEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTG 415
Cdd:PRK12349 304 -----EKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHANN-RLFRPRVNYIG 363
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
67-420 |
8.73e-76 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 240.62 E-value: 8.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 67 LLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFy 146
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 147 HDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVnpileRAMDRILIL 226
Cdd:PRK14033 112 DPEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCFGEVPEPEVV-----RAFEVSLIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 227 HADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDsfRLMGFGH 306
Cdd:PRK14033 187 YAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKE--KVMGFGH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 307 RVYKNYDPRATVMRETCHEVLKELGTKD-----DLLEVAMELenialndpyfiEKKLYPNVDFYSGIILKAMGIPSSMFT 381
Cdd:PRK14033 265 RVYKHGDSRVPTMKAALRRVAAVRDGQRwldiyEALEKAMAE-----------ATGIKPNLDFPAGPAYYLMGFDIDFFT 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 16128695 382 VIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRD 420
Cdd:PRK14033 334 PIFVMSRITGWTAHIMEQRASN-ALIRPLSEYNGPEQRE 371
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
67-421 |
6.25e-68 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 220.57 E-value: 6.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 67 LLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVM---CGITGALA 143
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMrtgVSVLGCLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 144 AFYHDSldvNNPRHREIAAfRLLSKMPTMaaMCYKYSI---GQPFVYPRNDLSYAGNFLNMMF-STPCEPYEvnpileRA 219
Cdd:PRK12351 112 PEKEDH---NFSGARDIAD-RLLASLGSI--LLYWYHYshnGRRIEVETDDDSIGGHFLHLLHgKKPSESWV------KA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRR---AKDKn 296
Cdd:PRK12351 180 MHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRrveNKEV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 297 dsfrLMGFGHRVYKNYDPRATVMRETCHEVLKELGTkDDLLEVAMELENIALNdpyfiEKKLYPNVDFYSGIILKAMGIP 376
Cdd:PRK12351 259 ----VIGFGHPVYTISDPRNKVIKEVAKKLSKEAGD-TKLYDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16128695 377 SSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 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 |
3.96e-63 |
|
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate, but has a partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate, prefer PrCoA as substrate, but can also can use AcCoA. Re 2-MCS1 at a low rate can use butyryl-CoA and valeryl-CoA. A second Ralstonia eutropha 2MCS is also found in this group, Re 2-MCS2, which is induced on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99870 [Multi-domain] Cd Length: 366 Bit Score: 207.78 E-value: 3.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 62 GDEGILLH-RGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITG 140
Cdd:cd06117 17 GRSGNDLHyRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 141 ALAAFYHDSLDVNNPRHREIAAfRLLSKMPTMAAMCYKYSI-GQPFVYPRNDLSYAGNFLNMMFSTPcePYEvnpILERA 219
Cdd:cd06117 97 VLGCVLPEKEDHPVSGARDIAD-RLMASLGSILLYWYHYSHnGKRIEVETDDDSIGGHFLHLLHGEK--PSE---SWEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 220 MDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSf 299
Cdd:cd06117 171 MHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVENKEV- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 300 rLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKdDLLEVAMELENIALNdpyfiEKKLYPNVDFYSGIILKAMGIPSSM 379
Cdd:cd06117 250 -VIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDM-KMFDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTAM 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16128695 380 FTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTGYEKRDF 421
Cdd:cd06117 323 FTPLFVIARTTGWSAHIIEQRQDG-KIIRPSANYTGPEDLKF 363
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
43-415 |
4.45e-60 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 199.42 E-value: 4.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 43 FDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGE----KPTQEQYDefkttVTRHTmiheqi 118
Cdd:PRK12350 1 FVPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRfgpgLPPAEPFP-----LPVHL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 119 trlfHAFRRDSHPMAVMCGITGALAAFyhdsLDVNNPRHRE--IAAfrllSKMPTMAAMCYKYSIGQPFVyPRNDLSYAG 196
Cdd:PRK12350 70 ----GDARVDVQAALAMLAPVWGFRPL----LDIDDLTARLdlARA----SVMALSAVAQSARGIGQPAV-PQREIDHAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 197 NFLNM-MFSTPCEPyevNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKM 275
Cdd:PRK12350 137 TILERfMGRWRGEP---DPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 276 LEEISSVKHIPEFVRRAKDKNDsfRLMGFGHRVYKNYDPRATVMRETChevlKELGTkdDLLEVAMELENIALNDpyFIE 355
Cdd:PRK12350 214 LDAVERTGDARGWVKGALDRGE--RLMGFGHRVYRAEDPRARVLRATA----KRLGA--PRYEVAEAVEQAALAE--LRE 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128695 356 KK----LYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGmKIARPRQLYTG 415
Cdd:PRK12350 284 RRpdrpLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTG-RLVRPSARYVG 346
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
63-427 |
3.28e-59 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 199.75 E-value: 3.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 63 DEGILLHRGFPIDQLATDS------NYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLF--HAFRRDshpmaV 134
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNGFlkekrfGFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRDMilKAPSKD-----I 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 135 MCGITGALAAFYhdSLDVN----NPRHREIAAFRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLNMMfs 204
Cdd:PRK14032 139 MNSLARSVLALY--SYDDNpddtSIDNVLRQSISLIARFPTLAVYAYQayrhYHDGKSLYihPPKPELSTAENILYML-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 205 TPCEPYEvnPILERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI---- 279
Cdd:PRK14032 215 RPDNKYT--ELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIkenv 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 280 ---SSVKHIPEFVRRAKDK---NDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGtKDDLLEVAMELENIAlndPYF 353
Cdd:PRK14032 293 kdwEDEDEIADYLTKILNKeafDKSGLIYGMGHAVYTISDPRAVILKKFAEKLAKEKG-REEEFNLYEKIEKLA---PEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 354 I--EKKLY----PNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTGyEKRDFKSDIKR 427
Cdd:PRK14032 369 IaeERGIYkgvsANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGGKIIRPAYKSVL-ERREYVPLEER 447
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
63-409 |
1.30e-56 |
|
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: 191.71 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 63 DEGILLHRGFPIDQLATDSN------YLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMC 136
Cdd:cd06113 34 CPGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSKDIMNKLQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 137 GITGALAAfYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYK----YSIGQPFV--YPRNDLSYAGNFLNMMFS----TP 206
Cdd:cd06113 114 RSVLALYS-YDDKPDDISLENVLRQSIQLIARLPTIAVYAYQakrhYYDGESLYihHPQPELSTAENILSMLRPdkkyTE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 207 CEPyevnpileRAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEI------ 279
Cdd:cd06113 193 LEA--------KLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIkenvkd 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 280 -SSVKHIPEFVRRAKDK--NDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKELGTKD--DLLEVAMELENIALNDPYF 353
Cdd:cd06113 265 wTDEDEVRAYLRKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEefALYERIERLAPEVIAEERG 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128695 354 IEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARP 409
Cdd:cd06113 345 IGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRP 400
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
57-415 |
1.94e-43 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 157.60 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 57 ITFIDGDEGILLhRGFPIDQL------ATDSNY---LEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRR 127
Cdd:PRK09569 52 ISYLDPQEGIRF-RGKTIPETfealpkAPGSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 128 DSHPMAVM-CGIT-----GALAAFYHDS----LDVNNPRHREiaAFRLLSKMPTMAAMCY--KYSIGQPfVYPRNDLSYA 195
Cdd:PRK09569 131 DSHPMVMLsVGILamqreSKFAKFYNEGkfnkMDAWEYMYED--ASDLVARIPVIAAYIYnlKYKGDKQ-IPSDPELDYG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 196 GNFLNMMfsTPCEPYevnpilERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL- 273
Cdd:PRK09569 208 ANFAHMI--GQPKPY------KDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 274 ---KMLEEISSVKHIPEFVRRA-KDKNDSFRLM-GFGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLEVAMELENIAl 348
Cdd:PRK09569 280 wiqQFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLFKLVAMIFEVA- 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128695 349 ndPYFIE-----KKLYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTG 415
Cdd:PRK09569 355 --PGVLTehgktKNPWPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTE 425
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
212-415 |
2.23e-41 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99856 [Multi-domain] Cd Length: 282 Bit Score: 147.79 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 212 VNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRR 291
Cdd:cd06102 93 LDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 292 AKDKNDsfRLMGFGHRVYKNYDPRATVMRETCHEVLKE-LGTKDDLLEVAMELENialndpyfiekkLYPNVDFYSGIIL 370
Cdd:cd06102 173 RLRRGE--ALPGFGHPLYPDGDPRAAALLAALRPLGPAaPPAARALIEAARALTG------------ARPNIDFALAALT 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128695 371 KAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIaRPRQLYTG 415
Cdd:cd06102 239 RALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLI-RPRARYVG 282
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
17-412 |
3.83e-37 |
|
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: 140.13 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 17 ELDVLKGTLGQDVIDIRTL-----GSKGVFTFdpgFTSTASCeskitfiDGDEGILLhRGFPIDQL--------ATDSNY 83
Cdd:cd06103 15 RIKELRKKYGNTKLGQITVdqvigGMRGMKGL---VYETSVL-------DPDEGIRF-RGKTIPECqellpkadGGGEPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 84 LEVC-YILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGitgALAAFYHDSL--------DVNN 154
Cdd:cd06103 84 PEGLfWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSA---AILALQSESKfakayaegKINK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 155 PRHREIA---AFRLLSKMPTMAAMCYKYSIGQ-PFVYPRN-DLSYAGNFLNMMfstpcePYEvNPILERAMDRILILHAD 229
Cdd:cd06103 161 TTYWEYVyedAMDLIAKLPVVAAKIYRRKYRKgGEIGAIDsKLDWSANFAHML------GYE-DEEFTDLMRLYLTLHSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 230 HEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL----KMLEEISSVKHIPEFVRRAKDKNDSFRLM-G 303
Cdd:cd06103 234 HEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLkwllKMQKELGKDVSDEELEKYIWDTLNSGRVVpG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 304 FGHRVYKNYDPRATVMRETCHEVLKElgtkDDLLE-VAMELENIalndPYFIE-----KKLYPNVDFYSGIILKAMGIPS 377
Cdd:cd06103 314 YGHAVLRKTDPRFTCQREFALKHLPD----DPLFKlVAQCYKII----PGVLKehgkvKNPYPNVDAHSGVLLQHYGMTE 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 16128695 378 -SMFTVIFAMARTVGWIAH--WSEMHsdGMKIARPRQL 412
Cdd:cd06103 386 pQYYTVLFGVSRALGVLAQlvWSRAL--GLPIERPKSM 421
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
88-415 |
1.66e-29 |
|
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99858 Cd Length: 427 Bit Score: 119.01 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 88 YILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAvmcGITGALAAFYHDSL-------DVNNPRHREI 160
Cdd:cd06105 89 WLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMS---QLSAAITALNSESKfakayaeGIHKSKYWEY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 161 A---AFRLLSKMPTMAAMCYK--YSIGQpFVYPRNDLSYAGNFLNMMfstpcePYEvNPILERAMDRILILHADHEQ-NA 234
Cdd:cd06105 166 VyedSMDLIAKLPCVAAKIYRnlYRGGK-IIAIDSNLDWSANFANML------GYT-DPQFTELMRLYLTIHSDHEGgNV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 235 STSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL----KMLEEIS---SVKHIPEFVRrakDKNDSFRLM-GFGH 306
Cdd:cd06105 238 SAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltKLQKEVGkdvSDEQLREYVW---KTLNSGRVVpGYGH 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 307 RVYKNYDPRATVMRETChevLKELgTKDDLLEVAMELENIAlnDPYFIE----KKLYPNVDFYSGIILKAMGIPS-SMFT 381
Cdd:cd06105 315 AVLRKTDPRYTCQREFA---LKHL-PNDPLFKLVSQLYKIV--PPVLTEqgkaKNPWPNVDAHSGVLLQYYGLTEmNYYT 388
|
330 340 350
....*....|....*....|....*....|....*.
gi 16128695 382 VIFAMARTVGWIAH--WSEmhSDGMKIARPRQLYTG 415
Cdd:cd06105 389 VLFGVSRALGVLSQliWDR--ALGLPLERPKSVSTD 422
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
58-412 |
7.52e-28 |
|
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: 114.14 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 58 TFIDGDEGILLHrGFPIDQL-------ATDSNYL--EVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRD 128
Cdd:cd06106 51 SVLDAEEGIRFH-GKTIPECqkelpkaPIGGEMLpeSMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 129 SHPMAvmcGITGALAAFYHDSL-------DVNNPRHREIA---AFRLLSKMPTMAAMCYKYS----IGQPFVYPRNDLSY 194
Cdd:cd06106 130 LHPMT---QLSIGVAALNHDSKfaaayekGIKKTEYWEPTledSLNLIARLPALAARIYRNVygegHGLGKIDPEVDWSY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 195 agNFLNMMfstpcePYEVNPILERAMDRILILHADHEQ-NASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAAL 273
Cdd:cd06106 207 --NFTSML------GYGDNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 274 K----MLEEISSVKHIPEFVRRAKDKNDSFRLM-GFGHRVYKNYDPRATVMRETChEVLKELgTKDDLLEVAMELENIAl 348
Cdd:cd06106 279 RwileMQKNIGSKATDQDIRDYLWKTLKSGRVVpGYGHAVLRKPDPRFTALMEFA-QTRPEL-ENDPVVQLVQKLSEIA- 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128695 349 nDPYFIE----KKLYPNVDFYSGIILKAMGIPSSMF-TVIFAMARTVGWIAH--WSEMHsdGMKIARPRQL 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 |
4.81e-26 |
|
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: 104.96 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 218 RAMDRILILHADH-EQNASTSTVRTAGSSGANPF-ACIAAGIASLwGPAHGGANEAALKMLEEI-----SSVKHIPEFVR 290
Cdd:cd06100 32 RLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgdALDAAAAEFVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 291 RAKDKNdsFRLMGFGHRVYKNYDPRATVMretcHEVLKELGTKDDLLEVAMELENIALNDPyfiEKKLYPNVDFYSGIIL 370
Cdd:cd06100 111 EYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGPAGPHLDYALAVEKALTAAK---GKPLPLNVDGAIAAIL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128695 371 KAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIAR 408
Cdd:cd06100 182 LDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYR 219
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
218-421 |
1.27e-21 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 93.78 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 218 RAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEI----SSVKHIPEFVR--- 290
Cdd:PRK06224 56 RLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaaDAGADLDAAARaiv 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 291 ---RAKDKndsfRLMGFGHRVYKNYDPRATVMRetchEVLKELGTKDDLLEVAMELENIalndpyFIE---KKLYPNVDF 364
Cdd:PRK06224 135 aeyRAAGK----RVPGFGHPLHKPVDPRAPRLL----ALAREAGVAGRHCRLAEALEAA------LAAakgKPLPLNVDG 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128695 365 YSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQL-----YTGYEKRDF 421
Cdd:PRK06224 201 AIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQPIGFRIWDPAeeaveYTGPPPREL 262
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
220-398 |
7.06e-07 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 51.36 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 220 MDRILILHADHEQNASTS--TVRTAgSSGANPFACIAAGIASLwGPAHGGANEAALKMLEEISSVKHIP-EFVRRAKDKN 296
Cdd:PLN02522 403 IEMCIMLCADHGPCVSGAhnTIVTA-RAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMKKKG 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128695 297 dsFRLMGFGHRVYK--NYDPRATVMRETCHEVLKELgtkdDLLEVAMELENIALNDpyfiEKKLYPNVDFYSGIILKAMG 374
Cdd:PLN02522 481 --IRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSV----KYMEYAVQVETYTLSK----ANNLVLNVDGAIGSLFLDLL 550
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128695 375 IPSSMFTV--------------IFAMARTVGWIAHWSE 398
Cdd:PLN02522 551 AGSGMFTKqeideiveigylngLFVLARSIGLIGHTFD 588
|
|
| |
