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Conserved domains on  [gi|2643421709|ref|WP_323129338|]
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citrate/2-methylcitrate synthase, partial [Klebsiella variicola]

Protein Classification

citrate synthase family protein( domain architecture ID 475)

citrate synthase family protein similar to citrate synthase that 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

CATH:  1.10.580.10
EC:  2.3.-.-
Gene Ontology:  GO:0016746
PubMed:  3013232
SCOP:  3001050

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CS_ACL-C_CCL super family cl00416
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
1-243 8.12e-155

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.


The actual alignment was detected with superfamily member cd06114:

Pssm-ID: 469765  Cd Length: 400  Bit Score: 436.63  E-value: 8.12e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06114   157 AAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFAS 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:cd06114   237 ISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:cd06114   317 DDPLLEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPeLKIGRPRQ 396

                  ....
gi 2643421709 240 IYVG 243
Cdd:cd06114   397 LYTG 400
 
Name Accession Description Interval E-value
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
1-243 8.12e-155

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: 436.63  E-value: 8.12e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06114   157 AAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFAS 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:cd06114   237 ISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:cd06114   317 DDPLLEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPeLKIGRPRQ 396

                  ....
gi 2643421709 240 IYVG 243
Cdd:cd06114   397 LYTG 400
gltA PRK05614
citrate synthase;
1-244 3.01e-143

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 408.11  E-value: 3.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:PRK05614  175 AAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFAC 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:PRK05614  255 IAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGL 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:PRK05614  335 NDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSDPeQKIGRPRQ 414

                  ....*
gi 2643421709 240 IYVGE 244
Cdd:PRK05614  415 LYTGY 419
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
1-249 5.49e-125

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: 361.41  E-value: 5.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:TIGR01798 162 AAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFAC 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:TIGR01798 242 IAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELGL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 -SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPR 238
Cdd:TIGR01798 322 hDDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPgQKIGRPR 401
                         250
                  ....*....|.
gi 2643421709 239 QIYVGEGYRDY 249
Cdd:TIGR01798 402 QLYTGETQRDY 412
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
1-250 5.42e-119

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: 345.16  E-value: 5.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIpaekyVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:COG0372   142 AAYAYRYRRGLPPVYPDPDLSYAENFLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSA 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPqaFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:COG0372   217 IAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIRKALDKK--ERIMGFGHRVYKNYDPRAKILKEAAEELLEELGD 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 sDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPRQI 240
Cdd:COG0372   295 -DPLLEIAEELEEVALEDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRADN-RIIRPRQI 372
                         250
                  ....*....|
gi 2643421709 241 YVGEGYRDYV 250
Cdd:COG0372   373 YVGPEDRDYV 382
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
1-238 2.31e-98

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: 291.72  E-value: 2.31e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAipaekYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:pfam00285 128 AAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG-----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSA 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRdpQAFRRL-GFGNSRYRHRDPRAGILRETSHRvLAEVG 159
Cdd:pfam00285 203 IAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYIRKVLN--KGKERImGFGHRVYKNYDPRAKILKEFAEE-LAEEG 279
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2643421709 160 MSDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPR 238
Cdd:pfam00285 280 GDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFYSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
Cit_synth_Halo_CitZ NF041301
citrate synthase;
10-251 7.10e-48

citrate synthase;


Pssm-ID: 469198  Cd Length: 379  Bit Score: 162.89  E-value: 7.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  10 EQPAAyPRNDLSYAGNFLQMLfaipaEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLW 89
Cdd:NF041301  148 EDPVE-PREDLSHAANFLYML-----NGEEPDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLS 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  90 GPMHGGANESSMRMLEEIESVDQVPafLRQAKRDPQAFRRL-GFGNSRYRHRDPRAGILRETShRVLAEVGMSDRLLQVA 168
Cdd:NF041301  222 GSLHGGANQDVMRMLKEVDESDKDP--VEWVKDALEEGRRVpGFGHRVYNVKDPRAKILGEKS-EELGEAAGDTKWYEYS 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 169 MALEDvaltdpYFVDN-GLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMhQAPLTIYRPRQIYVGEGYR 247
Cdd:NF041301  299 VAIEE------YMTEEkGLAPNVDFYSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQ-YEDNRLIRPRARYVGPKDR 371

                  ....
gi 2643421709 248 DYVS 251
Cdd:NF041301  372 EFVP 375
 
Name Accession Description Interval E-value
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
1-243 8.12e-155

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: 436.63  E-value: 8.12e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06114   157 AAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFAS 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:cd06114   237 ISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:cd06114   317 DDPLLEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPeLKIGRPRQ 396

                  ....
gi 2643421709 240 IYVG 243
Cdd:cd06114   397 LYTG 400
gltA PRK05614
citrate synthase;
1-244 3.01e-143

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 408.11  E-value: 3.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:PRK05614  175 AAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFAC 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:PRK05614  255 IAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGL 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:PRK05614  335 NDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSDPeQKIGRPRQ 414

                  ....*
gi 2643421709 240 IYVGE 244
Cdd:PRK05614  415 LYTGY 419
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
1-249 5.49e-125

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: 361.41  E-value: 5.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:TIGR01798 162 AAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFAC 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:TIGR01798 242 IAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELGL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 -SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPR 238
Cdd:TIGR01798 322 hDDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPgQKIGRPR 401
                         250
                  ....*....|.
gi 2643421709 239 QIYVGEGYRDY 249
Cdd:TIGR01798 402 QLYTGETQRDY 412
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
1-250 5.42e-119

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: 345.16  E-value: 5.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIpaekyVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:COG0372   142 AAYAYRYRRGLPPVYPDPDLSYAENFLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSA 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPqaFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:COG0372   217 IAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIRKALDKK--ERIMGFGHRVYKNYDPRAKILKEAAEELLEELGD 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 sDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPRQI 240
Cdd:COG0372   295 -DPLLEIAEELEEVALEDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRADN-RIIRPRQI 372
                         250
                  ....*....|
gi 2643421709 241 YVGEGYRDYV 250
Cdd:COG0372   373 YVGPEDRDYV 382
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
1-243 2.23e-103

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: 305.51  E-value: 2.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06107   142 AAAAYCHRIGRPFVYPRANLSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISC 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRdpQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:cd06107   222 MAAAIAALYGPLHGGANEAALKMLREIGTPENVPAFIERVKN--GKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEK 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 sDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLT-IYRPRQ 239
Cdd:cd06107   300 -DPLLKVAMELERIALEDEYFVSRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQrIWRPRQ 378

                  ....
gi 2643421709 240 IYVG 243
Cdd:cd06107   379 VYTG 382
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
1-238 2.31e-98

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: 291.72  E-value: 2.31e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAipaekYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:pfam00285 128 AAYIYRHRRGLPPIYPDPDLSYAENFLYMLFG-----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSA 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRdpQAFRRL-GFGNSRYRHRDPRAGILRETSHRvLAEVG 159
Cdd:pfam00285 203 IAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYIRKVLN--KGKERImGFGHRVYKNYDPRAKILKEFAEE-LAEEG 279
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2643421709 160 MSDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPR 238
Cdd:pfam00285 280 GDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFYSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
1-241 2.20e-86

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: 261.00  E-value: 2.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAekyvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06118   128 AANIYRNREGLEIIAPDPDLSYAENFLYMLFGEEP-----DPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSA 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRqaKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGm 160
Cdd:cd06118   203 IAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYIW--KKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG- 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFvdNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQI 240
Cdd:cd06118   280 DDKLFEIAEELEEIALEVLGE--KGIYPNVDFYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAE 357

                  .
gi 2643421709 241 Y 241
Cdd:cd06118   358 Y 358
PLN02456 PLN02456
citrate synthase
1-250 4.79e-86

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 263.42  E-value: 4.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADH-GQCASTTTVRAAGSSGANLFA 79
Cdd:PLN02456  201 AAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHeGGCSTAAARHLVGSSGVDPYT 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  80 CVAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKrdpQAFRRL-GFGNSRYRHRDPRAGILRETSHRVLAEV 158
Cdd:PLN02456  281 SVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVK---NSKKVLpGFGHRVYKNYDPRAKCIREFALEVFKHV 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 159 GmSDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLT-IYRP 237
Cdd:PLN02456  358 G-DDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALGLPDErIMRP 436
                         250
                  ....*....|...
gi 2643421709 238 RQIYVGEGYRDYV 250
Cdd:PLN02456  437 KQVYTGEWLRHYC 449
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
1-250 9.15e-86

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: 260.53  E-value: 9.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06116   135 AAFAYRHRLGLPYVLPDNDLSYTGNFLSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTA 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGM 160
Cdd:cd06116   215 VAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVFEATGR 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDrLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAP-LTIYRPRQ 239
Cdd:cd06116   293 NP-LLDIAVELEKIALEDEYFISRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPeQKIARPRQ 371
                         250
                  ....*....|.
gi 2643421709 240 IYVGEGYRDYV 250
Cdd:cd06116   372 VYTGPRDRDYV 382
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
1-250 1.50e-80

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: 248.12  E-value: 1.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFAC 80
Cdd:cd06115   162 AAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  81 VAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGm 160
Cdd:cd06115   242 VAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVFEIVG- 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 161 SDRLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLT-IYRPRQ 239
Cdd:cd06115   319 KDPLIEIAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTkIMRPQQ 398
                         250
                  ....*....|.
gi 2643421709 240 IYVGEGYRDYV 250
Cdd:cd06115   399 LYTGVWLRHYV 409
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
21-241 9.36e-79

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: 238.37  E-value: 9.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  21 SYAGNFLQMLFAipaEKYvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGANESS 100
Cdd:cd06101    53 SYAENFLYMLGG---EEP--DPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAV 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 101 MRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGmSDRLLQVAMALEDVALTDPY 180
Cdd:cd06101   128 LKMLEEIGTPKNEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG-LDPMFELAAELEKIAPEVLY 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2643421709 181 FvdNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQIY 241
Cdd:cd06101   207 E--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
21-241 6.84e-77

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: 231.84  E-value: 6.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  21 SYAGNFLQMLFAipaEKYvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGANESS 100
Cdd:cd06099     1 SYAENFLYMLGG---EEP--DPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 101 MRMLEEIESVDQVPAFLRQAKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGmSDRLLQVAMALEDVALTDPY 180
Cdd:cd06099    76 LKMLEEIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDG-DDPMFELAAELEKIAEEVLY 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2643421709 181 FvdNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQIY 241
Cdd:cd06099   155 E--KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
16-252 4.39e-61

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) 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: 196.88  E-value: 4.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLFAipAEKYvlnPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGG 95
Cdd:cd06112   147 PRPDLDYAENFLYMLFG--EEPD---PATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  96 ANESSMRMLEEIESVDQVPAFLRqaKRDPQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGMSDRLLQVAMALEDVA 175
Cdd:cd06112   222 ANEDVLEMLEEIGSPENVKAYLD--KKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLC 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 176 LTdpYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMhqapLT---IYRPRQIYVGEGYRDYVSR 252
Cdd:cd06112   300 EE--LLGHKGVYPNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQ----LGdnrIFRPTQIYIGEIDRKYVPL 373
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
2-250 1.86e-60

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: 194.89  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   2 AMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAIPAekyvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACV 81
Cdd:TIGR01800 129 AYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGEEP-----TKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAI 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  82 AAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLR---QAKRdpqafRRLGFGNSRYRHRDPRAGILRETSHRVLAEV 158
Cdd:TIGR01800 204 TAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRkalENKE-----RIMGFGHRVYKTYDPRAKILKEYAKKLSAKE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 159 GMSdRLLQVAMALEDVALTdpyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPR 238
Cdd:TIGR01800 279 GSS-KWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYYMMGIPTDLFTPIFAMSRVTGWTAHIIEQVENNRLI-RPR 351
                         250
                  ....*....|..
gi 2643421709 239 QIYVGEGYRDYV 250
Cdd:TIGR01800 352 ADYVGPEERKYV 363
PRK14036 PRK14036
citrate synthase; Provisional
16-250 2.53e-57

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 187.09  E-value: 2.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLFaipaEKYVlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGG 95
Cdd:PRK14036  148 PRDDLDYAANFLYMLT----EREP-DPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGG 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  96 ANESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGmSDRLLQVAMALEDVA 175
Cdd:PRK14036  223 ANEDVLAMLEEIGSVENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEELFARFG-HDEYYEIALELERVA 299
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2643421709 176 ltDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPRQIYVGEGYRDYV 250
Cdd:PRK14036  300 --EERLGPKGIYPNVDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGAN-RIFRPTQIYTGSHNRRYI 371
PRK14035 PRK14035
citrate synthase; Provisional
16-250 1.58e-56

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 184.96  E-value: 1.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLF-AIPAEkyvlnpVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHG 94
Cdd:PRK14035  146 PRPDLSYAANFLYMLRgELPTD------IEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHG 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  95 GANESSMRMLEEIESVDQVPAFLrQAKRDPQAfRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGMSDrLLQVAMALEDV 174
Cdd:PRK14035  220 GANERVMDMLSEIRSIGDVDAYL-DEKFANKE-KIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREE-LFEMSVKIEKR 296
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2643421709 175 ALTdpyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEmHQAPLTIYRPRQIYVGEGYRDYV 250
Cdd:PRK14035  297 MKE-----EKGLIPNVDFYSATVYHVMGIPHDLFTPIFAVSRVAGWIAHILE-QYKDNRIMRPRAKYIGETNRKYI 366
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
16-243 4.86e-56

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: 183.24  E-value: 4.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLF-AIPaekyvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHG 94
Cdd:cd06110   143 PDPDLSHAANFLYMLTgEKP------SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  95 GANESSMRMLEEIESVDQVPAFLRQAKRDPQAFrrLGFGNSRYRHRDPRAGILRETSHRVLAEVG------MSDRLLQvA 168
Cdd:cd06110   217 GANERVMKMLLEIGSVDNVAAYVKDKLANKEKI--MGFGHRVYKTGDPRAKHLREMSRRLGKETGepkwyeMSEAIEQ-A 293
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2643421709 169 MALEDvaltdpyfvdnGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPRQIYVG 243
Cdd:cd06110   294 MRDEK-----------GLNPNVDFYSASVYYMLGIPVDLFTPIFAISRVSGWCAHILEQYFNN-RLIRPRAEYVG 356
PRK14034 PRK14034
citrate synthase; Provisional
16-251 1.67e-48

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 164.17  E-value: 1.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLFAIPAekyvlNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGG 95
Cdd:PRK14034  146 PRKDLSLAANFLYMLNGEEP-----DEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGG 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  96 ANESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGMSdRLLQVAMALEDVA 175
Cdd:PRK14034  221 ANENVMKMLTEIGEEENVESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEE-KWYNMSIKIEEIV 297
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2643421709 176 LTdpyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPRQIYVGEGYRDYVS 251
Cdd:PRK14034  298 TK-----EKGLPPNVDFYSASVYHCLGIDHDLFTPIFAISRMSGWLAHILEQYENNRLI-RPRADYVGPTHQVYVP 367
Cit_synth_Halo_CitZ NF041301
citrate synthase;
10-251 7.10e-48

citrate synthase;


Pssm-ID: 469198  Cd Length: 379  Bit Score: 162.89  E-value: 7.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  10 EQPAAyPRNDLSYAGNFLQMLfaipaEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLW 89
Cdd:NF041301  148 EDPVE-PREDLSHAANFLYML-----NGEEPDEVLAETFDMALVLHADHGLNASTFSAMVTASTLADLHSAVTSAIGTLS 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  90 GPMHGGANESSMRMLEEIESVDQVPafLRQAKRDPQAFRRL-GFGNSRYRHRDPRAGILRETShRVLAEVGMSDRLLQVA 168
Cdd:NF041301  222 GSLHGGANQDVMRMLKEVDESDKDP--VEWVKDALEEGRRVpGFGHRVYNVKDPRAKILGEKS-EELGEAAGDTKWYEYS 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 169 MALEDvaltdpYFVDN-GLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMhQAPLTIYRPRQIYVGEGYR 247
Cdd:NF041301  299 VAIEE------YMTEEkGLAPNVDFYSASTYYQMGIPIDLYTPIFAMSRVGGWIAHVLEQ-YEDNRLIRPRARYVGPKDR 371

                  ....
gi 2643421709 248 DYVS 251
Cdd:NF041301  372 EFVP 375
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
1-243 2.44e-47

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: 160.55  E-value: 2.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   1 AAMSYKYTIEQPAAyPRNDLSYAGNFLQMLFA-IPAEKYVlnpvieQAMNQILVLHADHGQCASTTTVRAAGSSGANLFA 79
Cdd:cd06109   118 AALLRLSRGKQPIA-PDPSLSHAADYLRMLTGePPSEAHV------RALDAYLVTVADHGMNASTFTARVIASTEADLTS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  80 CVAAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILREtshrVLAEVG 159
Cdd:cd06109   191 AVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREALARGE--RLMGFGHRVYRVRDPRADVLKA----AAERLG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 160 MSDRLLQVAMALEDVALT--DPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEmHQAPLTIYRP 237
Cdd:cd06109   265 APDERLEFAEAVEQAALAllREYKPGRPLETNVEFYTALLLEALGLPREAFTPTFAAGRTAGWTAHVLE-QARTGRLIRP 343

                  ....*.
gi 2643421709 238 RQIYVG 243
Cdd:cd06109   344 QSRYVG 349
PRK14037 PRK14037
citrate synthase; Provisional
5-251 1.38e-41

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 146.43  E-value: 1.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   5 YKYTIEQPAAYPRNDLSYAGNFLQMLFA-IPAEKYVlnpvieQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAA 83
Cdd:PRK14037  135 YRRKEGNKPRIPEPSDSFAESFLLASFArEPTAEEI------KAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITA 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  84 GLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRDpQAFRRLGFGNSRYRHRDPRAGILRETSHRVLAEVGMSDR 163
Cdd:PRK14037  209 ALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIIN-GKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKK 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 164 LLQVAMALEDVALTDpyFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQIYVG 243
Cdd:PRK14037  288 YFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVG 365

                  ....*...
gi 2643421709 244 EGYRDYVS 251
Cdd:PRK14037  366 PEHREYVP 373
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
18-251 3.00e-41

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: 145.14  E-value: 3.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  18 NDLSYAGNFLQMLFAIPAEkyvlnPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGAN 97
Cdd:cd06108   143 DEDSIAGHFLHLLHGKKPG-----ELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGAN 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  98 ESSMRMLEEIESVDQVPAFLRQAKRDPQafRRLGFGNSRYRHRDPRAGILRETSHRvLAEVGMSDRLLQVAMALEDVALT 177
Cdd:cd06108   218 EAAMELIERFKSPEEAEQGLLEKLERKE--LIMGFGHRVYKEGDPRSDIIKKWSKK-LSEEGGDPLLYQISERIEEVMWE 294
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2643421709 178 DPyfvdnGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEmHQAPLTIYRPRQIYVGEGYRDYVS 251
Cdd:cd06108   295 EK-----KLFPNLDFYSASAYHFCGIPTELFTPIFVMSRVTGWAAHIME-QRANNRLIRPSADYIGPEPRPFVP 362
PRK12350 PRK12350
citrate synthase 2; Provisional
9-247 1.16e-39

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 140.48  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   9 IEQPAAyPRNDLSYAGNFLQMLFAipAEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASL 88
Cdd:PRK12350  122 IGQPAV-PQREIDHAATILERFMG--RWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGAL 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  89 WGPMHGGANESSMRMLEEIESVDQVPAFLRQA-KRDPqafRRLGFGNSRYRHRDPRAGILRETSHRVLAevgmsdRLLQV 167
Cdd:PRK12350  199 SGPLHGGAPARVLPMLDAVERTGDARGWVKGAlDRGE---RLMGFGHRVYRAEDPRARVLRATAKRLGA------PRYEV 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 168 AMALEDVALTD-----PyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPRQIYV 242
Cdd:PRK12350  270 AEAVEQAALAElrerrP---DRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLV-RPSARYV 345

                  ....*
gi 2643421709 243 GEGYR 247
Cdd:PRK12350  346 GPAPR 350
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
15-243 1.99e-36

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: 133.16  E-value: 1.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  15 YPRNDLSYAGNFLQMLFaiPAEKYvlNPVIEQAMNQILVLHADHGQCA-STTTVRAAGSSGANLFACVAAGLASLWGPMH 93
Cdd:cd06113   169 HPQPELSTAENILSMLR--PDKKY--TELEAKLLDLCLVLHAEHGGGNnSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRH 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  94 GGANESSMRMLEEI-------ESVDQVPAFLRQAkRDPQAFRR----LGFGNSRYRHRDPRAGILRETSHRVLAEVGMSD 162
Cdd:cd06113   245 GGANIKVMEMLEDIkenvkdwTDEDEVRAYLRKI-LNKEAFDKsgliYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 163 --RLLQVAMALEDVALTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQI 240
Cdd:cd06113   324 efALYERIERLAPEVIAEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRPAYK 403

                  ...
gi 2643421709 241 YVG 243
Cdd:cd06113   404 YVG 406
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
2-248 1.19e-34

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: 127.53  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   2 AMSYKYTIEQPAAYPRNDLSYAGNFLQMLFAipaekYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACV 81
Cdd:cd06111   129 AADIRRRKGLDPIPPDSDLGIAENFLHMCFG-----EVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAI 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  82 AAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQAKRdpQAFRRLGFGNSRYRHRDPRAGILREtSHRVLAEVGMS 161
Cdd:cd06111   204 TGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDALA--RKEKVMGFGHRVYKSGDSRVPTMEK-ALRRVAAVHDG 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 162 DRLLQVAMALEDVAltdpyFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPRQIY 241
Cdd:cd06111   281 QKWLAMYDALEDAM-----VAAKGIKPNLDFPAGPAYYLMGFDIDFFTPIFVMARITGWTAHIMEQRADNALI-RPLSEY 354

                  ....*..
gi 2643421709 242 VGEGYRD 248
Cdd:cd06111   355 NGPEQRP 361
PRK12351 PRK12351
methylcitrate synthase; Provisional
18-250 2.35e-34

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 126.96  E-value: 2.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  18 NDLSYAGNFLQMLFAI-PAEKYVlnpvieQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGA 96
Cdd:PRK12351  155 DDDSIGGHFLHLLHGKkPSESWV------KAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  97 NESSMRMLEEIESVDQVPAFLRqakrdpqafRRL-------GFGNSRYRHRDPRAGILRETSHRVLAEVGmSDRLLQVAM 169
Cdd:PRK12351  229 NEVAFEIQQRYDTPDEAEADIR---------RRVenkevviGFGHPVYTISDPRNKVIKEVAKKLSKEAG-DTKLYDIAE 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 170 ALEDVALTdpyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEmHQAPLTIYRPRQIYVGEGYRDY 249
Cdd:PRK12351  299 RLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTAMFTPLFVISRTTGWAAHVIE-QRQDNKIIRPSANYTGPEDRKF 372

                  .
gi 2643421709 250 V 250
Cdd:PRK12351  373 V 373
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
35-243 2.23e-33

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: 122.37  E-value: 2.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  35 AEKYVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGANESSMRMLEEIESVDQVP 114
Cdd:cd06102    88 ARAWGLDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 115 AFLRQAKRDPQAFRrlGFGNSRYRHRDPRAGILRETSHRVLAE-VGMSDRLLQVAMALedvaltdpyfvdNGLSPSVDFY 193
Cdd:cd06102   168 AAVRERLRRGEALP--GFGHPLYPDGDPRAAALLAALRPLGPAaPPAARALIEAARAL------------TGARPNIDFA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2643421709 194 TAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPRQIYVG 243
Cdd:cd06102   234 LAALTRALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLI-RPRARYVG 282
PRK12349 PRK12349
citrate synthase;
2-246 9.02e-33

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 122.91  E-value: 9.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   2 AMSYKYTIEQPAAYPRNDLSYAGNFLQMLfaipAEKyVLNPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACV 81
Cdd:PRK12349  135 ANSYHILNNEEPIEPLKELSYSANFLYML----TGK-KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGAL 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  82 AAGLASLWGPMHGGANESSMRMLEEIESVDQVPAFLRQ--AKRDpqafRRLGFGNSRY-RHRDPRAGILREtSHRVLAEV 158
Cdd:PRK12349  210 TGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEELLQKklYNKE----KIMGFGHRVYmKKMDPRALMMKE-ALKQLCDV 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 159 GMSDRLLQVAMALEDVALTdpyfvDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPR 238
Cdd:PRK12349  285 KGDYTLYEMCEAGEKIMEK-----EKGLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHANN-RLFRPR 358

                  ....*...
gi 2643421709 239 QIYVGEGY 246
Cdd:PRK12349  359 VNYIGERH 366
PRK14032 PRK14032
citrate synthase; Provisional
15-253 1.22e-32

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 123.86  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  15 YPRNDLSYAGNFLQMLFaiPAEKYvlNPVIEQAMNQILVLHADHGQCA-STTTVRAAGSSGANLFACVAAGLASLWGPMH 93
Cdd:PRK14032  199 PPKPELSTAENILYMLR--PDNKY--TELEARLLDLALVLHAEHGGGNnSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKH 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  94 GGANESSMRMLEEI-------ESVDQVPAFLRQAkRDPQAFRR----LGFGNSRYRHRDPRAGILRETSHRVLAEVGMSD 162
Cdd:PRK14032  275 GGANIKVMEMFEDIkenvkdwEDEDEIADYLTKI-LNKEAFDKsgliYGMGHAVYTISDPRAVILKKFAEKLAKEKGREE 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 163 RLLQVAMaLEDVA---LTDPYFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIYRPRQ 239
Cdd:PRK14032  354 EFNLYEK-IEKLApelIAEERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGGKIIRPAY 432
                         250
                  ....*....|....
gi 2643421709 240 IYVGEGyRDYVSRR 253
Cdd:PRK14032  433 KSVLER-REYVPLE 445
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
16-247 7.93e-31

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 117.74  E-value: 7.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  16 PRNDLSYAGNFLQMLF-AIPAekyvlnPVIEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHG 94
Cdd:PRK14033  153 PRSDLGYAENFLHMCFgEVPE------PEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHG 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  95 GANESSMRMLEEIESVDQVPAFLRQA---KRdpqafRRLGFGNSRYRHRDPRAGILREtSHRVLAEVGMSDRLLQVAMAL 171
Cdd:PRK14033  227 GANEAVMHTMLEIGDPARAAEWLRDAlarKE-----KVMGFGHRVYKHGDSRVPTMKA-ALRRVAAVRDGQRWLDIYEAL 300
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2643421709 172 EDValtdpyFVD-NGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPLTIyRPRQIYVGEGYR 247
Cdd:PRK14033  301 EKA------MAEaTGIKPNLDFPAGPAYYLMGFDIDFFTPIFVMSRITGWTAHIMEQRASNALI-RPLSEYNGPEQR 370
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
18-250 2.51e-30

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: 116.10  E-value: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  18 NDLSYAGNFLQMLFA-IPAEKYvlnpviEQAMNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGA 96
Cdd:cd06117   146 DDDSIGGHFLHLLHGeKPSESW------EKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGA 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  97 NESSMRMLEEIESVDQVPAFLRQAKRDPQAFrrLGFGNSRYRHRDPRAGILRETSHRVLAEVGmSDRLLQVAMALEDVAl 176
Cdd:cd06117   220 NEVAFEIQQRYESADEAEADIRRRVENKEVV--IGFGHPVYTIADPRNQVIKEVAKQLSKEGG-DMKMFDIAERLETVM- 295
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2643421709 177 tdpyFVDNGLSPSVDFYTAVILKAMNLPSSMFAVVTAVGRTVGWVAHWNEMHQAPlTIYRPRQIYVGEGYRDYV 250
Cdd:cd06117   296 ----WEEKKMFPNLDWFSAVSYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQDG-KIIRPSANYTGPEDLKFV 364
PRK06224 PRK06224
citryl-CoA lyase;
48-231 6.61e-17

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 77.99  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  48 MNQILVLHADHGQCASTTTVRAAGSSGANLFACVAAGLASLwGPMHGGANESSMRMLEEI-ESVDQVPAFLRQAKRDPQA 126
Cdd:PRK06224   58 LDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaAAADAGADLDAAARAIVAE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 127 FRRL-----GFGNSRYRHRDPRAGILRETSHrvlaEVGMSDRLLQVAMALEDVALTDpyfVDNGLSPSVDFYTAVILKAM 201
Cdd:PRK06224  137 YRAAgkrvpGFGHPLHKPVDPRAPRLLALAR----EAGVAGRHCRLAEALEAALAAA---KGKPLPLNVDGAIAAILADL 209
                         170       180       190
                  ....*....|....*....|....*....|
gi 2643421709 202 NLPSSMFAVVTAVGRTVGWVAHWNEMHQAP 231
Cdd:PRK06224  210 GFPPALARGLFVISRAAGLVAHVWEELQQP 239
PRK09569 PRK09569
citrate (Si)-synthase;
19-243 2.27e-15

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 75.17  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  19 DLSYAGNFLQMLfAIPAEkyvlnpvIEQAMNQILVLHADHGQC-ASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGAN 97
Cdd:PRK09569  203 ELDYGANFAHMI-GQPKP-------YKDVARMYFILHSDHESGnVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLAN 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  98 ES----SMRMLEEIESVDQVPAFLRQAKRDPQAFRRL--GFGNSRYRHRDPRAGILRETSHRVLAEvgmsDRLLQVAMAL 171
Cdd:PRK09569  275 QEvlgwIQQFQEKLGGEEPTKEQVEQALWDTLNAGQVipGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLFKLVAMI 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 172 EDVA---LT------DPYfvdnglsPSVDFYTAVILKAMNLPSSMF-AVVTAVGRTVGWVAH--WNEMHQAPltIYRPRQ 239
Cdd:PRK09569  351 FEVApgvLTehgktkNPW-------PNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANitWDRGLGYA--IERPKS 421

                  ....
gi 2643421709 240 IYVG 243
Cdd:PRK09569  422 VTTE 425
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
48-226 8.17e-15

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: 71.44  E-value: 8.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  48 MNQILVLHADHGQCA-STTTVRAAGSSGAN-LFACVAAGLASLwGPMHGGANESSMRMLEEIE-SVDQVPAFLRQAKRDP 124
Cdd:cd06100    34 LEALLVALADHGPATpSAHAARLTASAGPEdLQSAVAAGLLGI-GDRFGGAGEGAARLFKEAVdSGDALDAAAAEFVAEY 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 125 QAFRRL--GFGNSRYRHRDPRAGILREtshrVLAEVGMSDRLLQVAMALEDVALTDpyfVDNGLSPSVDFYTAVILKAMN 202
Cdd:cd06100   113 RAAKKRipGFGHPVHKNPDPRVPRLLE----LARELGPAGPHLDYALAVEKALTAA---KGKPLPLNVDGAIAAILLDLG 185
                         170       180
                  ....*....|....*....|....
gi 2643421709 203 LPSSMFAVVTAVGRTVGWVAHWNE 226
Cdd:cd06100   186 FPPGALRGLFVLGRSPGLIAHALE 209
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
19-215 3.10e-08

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: 53.91  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  19 DLSYAGNFLQML-FAipaekyvlNPVIEQAMNQILVLHADH-GQCASTTTVRAAGSSGANLFACVAAGLASLWGPMHGGA 96
Cdd:cd06105   200 NLDWSANFANMLgYT--------DPQFTELMRLYLTIHSDHeGGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLA 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  97 NESSMRMLEEIE-------SVDQVPAF----LRQAKRDPqafrrlGFGNSRYRHRDPRAGILRETSHRVLAEvgmsDRLL 165
Cdd:cd06105   272 NQEVLVWLTKLQkevgkdvSDEQLREYvwktLNSGRVVP------GYGHAVLRKTDPRYTCQREFALKHLPN----DPLF 341
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2643421709 166 QVAMALEDVA---LTDPYFVDNGLsPSVDFYTAVIL-----KAMNLPSSMFAVVTAVG 215
Cdd:cd06105   342 KLVSQLYKIVppvLTEQGKAKNPW-PNVDAHSGVLLqyyglTEMNYYTVLFGVSRALG 398
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
48-236 2.88e-06

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 47.89  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  48 MNQILVLHADHGQCAS-----TTTVRAagssGANLFACVAAGLASLwGPMHGGANESSMRMLEEIESVDQVP-AFLRQAK 121
Cdd:PLN02522  403 IEMCIMLCADHGPCVSgahntIVTARA----GKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMK 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 122 RdpQAFRRLGFGN--SRYRHRDPRAGILRETSHRVLAEVgmsdRLLQVAMALEDVALTDPyfvdNGLSPSVDFYTAVILK 199
Cdd:PLN02522  478 K--KGIRVPGIGHriKSRDNRDKRVELLQKYARTHFPSV----KYMEYAVQVETYTLSKA----NNLVLNVDGAIGSLFL 547
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2643421709 200 AMNLPSSMFAVVTA--------------VGRTVGWVAHWNEMHQAPLTIYR 236
Cdd:PLN02522  548 DLLAGSGMFTKQEIdeiveigylnglfvLARSIGLIGHTFDQKRLKQPLYR 598
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
4-240 8.44e-06

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: 46.34  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709   4 SYKYTIEQPAAYPRNDLSYagNFLQMLFAIPAEKYVlnpvieQAMNQILVLHADH-GQCASTTTVRAAGSSGANLFACVA 82
Cdd:cd06106   188 VYGEGHGLGKIDPEVDWSY--NFTSMLGYGDNLDFV------DLLRLYIALHGDHeGGNVSAHTTHLVGSALSDPYLSYS 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709  83 AGLASLWGPMHGGANESSMRMLEEIE-------SVDQVPAFLRQAKRDPQAFRrlGFGNSRYRHRDPRAGILRE---TSH 152
Cdd:cd06106   260 AGLMGLAGPLHGLAAQEVLRWILEMQknigskaTDQDIRDYLWKTLKSGRVVP--GYGHAVLRKPDPRFTALMEfaqTRP 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2643421709 153 RVLAE--VGMSDRLLQVA--MALEDVALTDPYfvdnglsPSVDFYTAVILKAMNLPSSMFAVVT-AVGRTVGWVAH--WN 225
Cdd:cd06106   338 ELENDpvVQLVQKLSEIApgVLTEHGKTKNPF-------PNVDAASGVLFYHYGIREFLYYTVIfGVSRALGPLTQlvWD 410
                         250
                  ....*....|....*
gi 2643421709 226 EMHQAPltIYRPRQI 240
Cdd:cd06106   411 RILGLP--IERPKSL 423
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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