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Conserved domains on  [gi|340547913|gb|AEK52124|]
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type II citrate synthase, partial [Aeromonas sp. Ae74(2011)]

Protein Classification

type II citrate synthase( domain architecture ID 1000108)

type II citrate synthase catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA) in the first step of the citric acid cycle (TCA or Krebs cycle)

CATH:  1.10.580.10|2.20.28.60|1.10.230.10
EC:  2.3.3.16
Gene Ontology:  GO:0006099|GO:0004108
PubMed:  3013232
SCOP:  3001050

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gltA super family cl29033
citrate synthase;
1-165 4.71e-142

citrate synthase;


The actual alignment was detected with superfamily member PRK05614:

Pssm-ID: 180164  Cd Length: 419  Bit Score: 400.79  E-value: 4.71e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK05614 200 FLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:PRK05614 280 EIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERK 359


                 ....*
gi 340547913 161 LYPNV 165
Cdd:PRK05614 360 LYPNV 364
 
Name Accession Description Interval E-value
gltA PRK05614
citrate synthase;
1-165 4.71e-142

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 400.79  E-value: 4.71e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK05614 200 FLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:PRK05614 280 EIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERK 359


                 ....*
gi 340547913 161 LYPNV 165
Cdd:PRK05614 360 LYPNV 364
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
 1-165 6.26e-127

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: 361.51  E-value: 6.26e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06114  182 FLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:cd06114  262 EIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPLLEIAMELEEIALKDDYFIERK 341


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06114  342 LYPNV 346
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
 1-165 1.38e-118

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: 340.99  E-value: 1.38e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913    1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:TIGR01798 187 FLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTEL-QIKDPLLDVAMELERIALSDPYFVEK 159
Cdd:TIGR01798 267 EIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELgLHDDPLFKLAMELEKIALNDPYFIER 346


                  ....*.
gi 340547913  160 KLYPNV 165
Cdd:TIGR01798 347 KLYPNV 352
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
 1-165 5.90e-101

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: 295.08  E-value: 5.90e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVpteeyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:COG0372  167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKndPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQiKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:COG0372  242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEYFIEKK 318


                 ....*
gi 340547913 161 LYPNV 165
Cdd:COG0372  319 LYPNV 323
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
 1-165 8.71e-91

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: 268.22  E-value: 8.71e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913    1 FLHMMFGvpteeYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:pfam00285 153 FLYMLFG-----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   81 EIGSVDRIPEYIAKAKDKNDpFRLMGFGHRVYKNHDPRATVMRETCHEVLtELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:pfam00285 228 EIGSPDEVEEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELA-EEGGDDPLLELAEELEEVAPEDLYFVEKN 305


                  ....*
gi 340547913  161 LYPNV 165
Cdd:pfam00285 306 LYPNV 310
Cit_synThplmales NF041157
citrate synthase;
1-165 3.35e-37

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 131.28  E-value: 3.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTEEyKVnpiveRAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:NF041157 155 FLRATFGrKPSEE-EI-----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQF 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIaKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDpLLDVAMELERIALSdpYFVEK 159
Cdd:NF041157 229 LEIGSPDNVEKWF-NENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKK-YLEIAEKLEELGIK--HFGSK 304


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:NF041157 305 GIYPNT 310
 
Name Accession Description Interval E-value
gltA PRK05614
citrate synthase;
1-165 4.71e-142

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 400.79  E-value: 4.71e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK05614 200 FLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:PRK05614 280 EIGSVDNIPEFIARAKDKNDGFRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLEVAMELEEIALNDEYFIERK 359


                 ....*
gi 340547913 161 LYPNV 165
Cdd:PRK05614 360 LYPNV 364
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
 1-165 6.26e-127

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: 361.51  E-value: 6.26e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06114  182 FLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:cd06114  262 EIGSVGNVDKYIAKAKDKNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPLLEIAMELEEIALKDDYFIERK 341


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06114  342 LYPNV 346
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
 1-165 1.38e-118

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: 340.99  E-value: 1.38e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913    1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:TIGR01798 187 FLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTEL-QIKDPLLDVAMELERIALSDPYFVEK 159
Cdd:TIGR01798 267 EIGSVKNIDEFIKKVKDKNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKELgLHDDPLFKLAMELEKIALNDPYFIER 346


                  ....*.
gi 340547913  160 KLYPNV 165
Cdd:TIGR01798 347 KLYPNV 352
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
 1-165 5.90e-101

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: 295.08  E-value: 5.90e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVpteeyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:COG0372  167 FLYMLFGE-----EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLE 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKndPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQiKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:COG0372  242 EIGSPDNVEEYIRKALDK--KERIMGFGHRVYKNYDPRAKILKEAAEELLEELG-DDPLLEIAEELEEVALEDEYFIEKK 318


                 ....*
gi 340547913 161 LYPNV 165
Cdd:COG0372  319 LYPNV 323
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
 1-165 5.28e-96

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: 282.40  E-value: 5.28e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06107  167 FLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLR 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNdpFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQiKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:cd06107  247 EIGTPENVPAFIERVKNGK--RRLMGFGHRVYKNYDPRAKVIREILHEVLTEVE-KDPLLKVAMELERIALEDEYFVSRK 323


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06107  324 LYPNV 328
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
 1-165 8.71e-91

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: 268.22  E-value: 8.71e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913    1 FLHMMFGvpteeYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:pfam00285 153 FLYMLFG-----YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   81 EIGSVDRIPEYIAKAKDKNDpFRLMGFGHRVYKNHDPRATVMRETCHEVLtELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:pfam00285 228 EIGSPDEVEEYIRKVLNKGK-ERIMGFGHRVYKNYDPRAKILKEFAEELA-EEGGDDPLLELAEELEEVAPEDLYFVEKN 305


                  ....*
gi 340547913  161 LYPNV 165
Cdd:pfam00285 306 LYPNV 310
PLN02456 PLN02456
citrate synthase
 1-165 5.79e-87

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 261.88  E-value: 5.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVR-LAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PLN02456 226 FLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVLtELQIKDPLLDVAMELERIALSDPYFVEK 159
Cdd:PLN02456 306 KEIGTVENIPEYVEGVKNSKK--VLPGFGHRVYKNYDPRAKCIREFALEVF-KHVGDDPLFKVASALEEVALLDEYFKVR 382


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:PLN02456 383 KLYPNV 388
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
 1-165 2.84e-76

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: 228.35  E-value: 2.84e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVpteeyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06101   58 FLYMLGGE-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQiKDPLLDVAMELERIALSDPYFveKK 160
Cdd:cd06101  133 EIGTPKNEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKG-LDPMFELAAELEKIAPEVLYE--KK 209


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06101  210 LYPNV 214
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
 1-165 1.07e-75

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: 229.80  E-value: 1.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVpteeyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06118  153 FLYMLFGE-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIakAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQiKDPLLDVAMELERIALSDPYFveKK 160
Cdd:cd06118  228 EIGTPENVEAYI--WKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKG-DDKLFEIAEELEEIALEVLGE--KG 302


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06118  303 IYPNV 307
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
 1-165 7.22e-75

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: 222.98  E-value: 7.22e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVpteeyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06099    6 FLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIkDPLLDVAMELERIALSDPYFveKK 160
Cdd:cd06099   81 EIGTPKNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGD-DPMFELAAELEKIAEEVLYE--KK 157


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06099  158 LYPNV 162
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
 1-165 2.20e-72

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: 222.40  E-value: 2.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06116  160 FLSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQ 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVLtELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:cd06116  240 QIGSPKNIPDFIETVKQGKE--RLMGFGHRVYKNYDPRARIIKKIADEVF-EATGRNPLLDIAVELEKIALEDEYFISRK 316


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06116  317 LYPNV 321
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
 1-165 1.67e-68

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: 213.07  E-value: 1.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06115  187 FLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVLtELQIKDPLLDVAMELERIALSDPYFVEKK 160
Cdd:cd06115  267 EIGTVENIPAFIEGVKNRKR--KLSGFGHRVYKNYDPRAKIIKKLADEVF-EIVGKDPLIEIAVALEKAALSDEYFVKRK 343


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06115  344 LYPNV 348
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
 1-165 3.75e-48

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: 158.98  E-value: 3.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTEEykvnpiVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:cd06110  153 FLYMLTGeKPSEE------AARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKML 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpyfvEK 159
Cdd:cd06110  227 LEIGSVDNVAAYVKDKLANKE--KIMGFGHRVYKTGDPRAKHLREMSRR-LGKETGEPKWYEMSEAIEQAMRD-----EK 298


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:cd06110  299 GLNPNV 304
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
 1-165 1.78e-47

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: 157.91  E-value: 1.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913    1 FLHMMFG-VPTEEYkvnpivERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:TIGR01800 153 FLYMLHGeEPTKEW------EKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAML 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETChEVLTELQIKDPLLDVAMELERIALSdpyfvEK 159
Cdd:TIGR01800 227 DEIGDPDKAEAWIRKALENKE--RIMGFGHRVYKTYDPRAKILKEYA-KKLSAKEGSSKWYEIAERLEDVMEE-----EK 298


                  ....*.
gi 340547913  160 KLYPNV 165
Cdd:TIGR01800 299 GIYPNV 304
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
 1-165 6.98e-47

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: 156.43  E-value: 6.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGvptEEykVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06112  157 FLYMLFG---EE--PDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLE 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSdpYFVEKK 160
Cdd:cd06112  232 EIGSPENVKAYLDKKLANKQ--KIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEE--LLGHKG 307


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06112  308 VYPNV 312
PRK14036 PRK14036
citrate synthase; Provisional
 1-165 5.44e-45

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 151.65  E-value: 5.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMfgvpTEEyKVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK14036 158 FLYML----TER-EPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLE 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIAlsDPYFVEKK 160
Cdd:PRK14036 233 EIGSVENVRPYLDERLANKQ--KIMGFGHREYKVKDPRATILQKLAEE-LFARFGHDEYYEIALELERVA--EERLGPKG 307


                 ....*
gi 340547913 161 LYPNV 165
Cdd:PRK14036 308 IYPNV 312
PRK14035 PRK14035
citrate synthase; Provisional
 1-165 1.36e-37

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 132.19  E-value: 1.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTEeykvnpIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PRK14035 156 FLYMLRGeLPTD------IEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDML 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpyfvEK 159
Cdd:PRK14035 230 SEIRSIGDVDAYLDEKFANKE--KIMGFGHRVYKDGDPRAKYLREMSRK-ITKGTGREELFEMSVKIEKRMKE-----EK 301


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:PRK14035 302 GLIPNV 307
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
 1-165 3.08e-37

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: 130.50  E-value: 3.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVnpiveRAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06109  142 YLRMLTGEPPSEAHV-----RALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLD 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRetchEVLTELQIKDPLLDVAMELERIALS--DPYFVE 158
Cdd:cd06109  217 AIGTPENAEAWLREALARGE--RLMGFGHRVYRVRDPRADVLK----AAAERLGAPDERLEFAEAVEQAALAllREYKPG 290


                 ....*..
gi 340547913 159 KKLYPNV 165
Cdd:cd06109  291 RPLETNV 297
Cit_synThplmales NF041157
citrate synthase;
1-165 3.35e-37

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 131.28  E-value: 3.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTEEyKVnpiveRAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:NF041157 155 FLRATFGrKPSEE-EI-----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQF 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIaKAKDKNDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDpLLDVAMELERIALSdpYFVEK 159
Cdd:NF041157 229 LEIGSPDNVEKWF-NENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKK-YLEIAEKLEELGIK--HFGSK 304


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:NF041157 305 GIYPNT 310
PRK14034 PRK14034
citrate synthase; Provisional
 1-165 2.12e-36

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 129.11  E-value: 2.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGvptEEykVNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK14034 156 FLYMLNG---EE--PDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLT 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpyfvEKK 160
Cdd:PRK14034 231 EIGEEENVESYIHNKLQNKE--KIMGFGHRVYRQGDPRAKHLREMSKR-LTVLLGEEKWYNMSIKIEEIVTK-----EKG 302


                 ....*
gi 340547913 161 LYPNV 165
Cdd:PRK14034 303 LPPNV 307
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
 1-165 3.28e-35

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: 125.50  E-value: 3.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEeykvnPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06108  151 FLHLLHGKKPG-----ELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIE 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETChEVLTELQIKDPLLDVAMELERIALSdpyfvEKK 160
Cdd:cd06108  226 RFKSPEEAEQGLLEKLERKE--LIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPLLYQISERIEEVMWE-----EKK 297


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06108  298 LFPNL 302
PRK12350 PRK12350
citrate synthase 2; Provisional
 21-152 1.16e-33

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 121.22  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  21 RAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLEEIGSVDRIPEYIAKAKDKND 100
Cdd:PRK12350 156 AALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVERTGDARGWVKGALDRGE 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340547913 101 pfRLMGFGHRVYKNHDPRATVMRETCHEvltelqIKDPLLDVAMELERIALS 152
Cdd:PRK12350 236 --RLMGFGHRVYRAEDPRARVLRATAKR------LGAPRYEVAEAVEQAALA 279
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
 1-165 1.83e-32

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: 118.28  E-value: 1.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPteeykvNPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:cd06111  153 FLHMCFGeVP------SPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMM 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVlteLQIKDPLLDVAMeleRIALSDPYFVEK 159
Cdd:cd06111  227 LEIDDPEKAAQWMLDALARKE--KVMGFGHRVYKSGDSRVPTMEKALRRV---AAVHDGQKWLAM---YDALEDAMVAAK 298


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:cd06111  299 GIKPNL 304
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
1-165 2.47e-31

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 115.43  E-value: 2.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTEEykvnpiVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PRK14033 163 FLHMCFGeVPEPE------VVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTM 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAKAKDKNDpfRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDpLLDVAMELERIALSdpyfvEK 159
Cdd:PRK14033 237 LEIGDPARAAEWLRDALARKE--KVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQR-WLDIYEALEKAMAE-----AT 308


                 ....*.
gi 340547913 160 KLYPNV 165
Cdd:PRK14033 309 GIKPNL 314
PRK14037 PRK14037
citrate synthase; Provisional
 1-164 2.48e-30

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 112.92  E-value: 2.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEYKVNpiverAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:PRK14037 156 FLLASFAREPTAEEIK-----AMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFV 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIakaKDK--NDPFRLMGFGHRVYKNHDPRATVMRETCHEVLTELQIKDPLLDVAMELERIALSDpyFVE 158
Cdd:PRK14037 231 EIGDPNNVEMWF---NDKiiNGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQ--FGS 305


                 ....*.
gi 340547913 159 KKLYPN 164
Cdd:PRK14037 306 KGIYPN 311
PRK12349 PRK12349
citrate synthase;
1-164 8.68e-29

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 108.65  E-value: 8.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFG-VPTeeykvnPIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PRK12349 159 FLYMLTGkKPT------ELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYML 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAK---AKDKndpfrLMGFGHRVY-KNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpy 155
Cdd:PRK12349 233 LEAGTVEKFEELLQKklyNKEK-----IMGFGHRVYmKKMDPRALMMKEALKQ-LCDVKGDYTLYEMCEAGEKIMEK--- 303


                 ....*....
gi 340547913 156 fvEKKLYPN 164
Cdd:PRK12349 304 --EKGLYPN 310
PRK12351 PRK12351
methylcitrate synthase; Provisional
 1-164 1.36e-27

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 105.78  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGV-PTEEYkvnpivERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PRK12351 163 FLHLLHGKkPSESW------VKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQ 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  80 EEIGSVDRIPEYIAK---AKDKndpfrLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpyf 156
Cdd:PRK12351 237 QRYDTPDEAEADIRRrveNKEV-----VIGFGHPVYTISDPRNKVIKEVAKK-LSKEAGDTKLYDIAERLETVMWE---- 306


                 ....*...
gi 340547913 157 vEKKLYPN 164
Cdd:PRK12351 307 -EKKMFPN 313
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
 20-146 6.44e-24

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: 94.25  E-value: 6.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  20 ERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLEEIGSVDRIPEYIAKAKDKN 99
Cdd:cd06102   98 ADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRG 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 340547913 100 DPfrLMGFGHRVYKNHDPRATVMRETCHEVL-TELQIKDPLLDVAMEL 146
Cdd:cd06102  178 EA--LPGFGHPLYPDGDPRAAALLAALRPLGpAAPPAARALIEAARAL 223
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
 1-165 3.62e-22

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: 90.67  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMFGVPTEEykvnpIVERAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLE 80
Cdd:cd06117  154 FLHLLHGEKPSE-----SWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQ 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  81 EIGSVDRIPEYIAKAKDKNDPfrLMGFGHRVYKNHDPRATVMRETCHEvLTELQIKDPLLDVAMELERIALSdpyfvEKK 160
Cdd:cd06117  229 RYESADEAEADIRRRVENKEV--VIGFGHPVYTIADPRNQVIKEVAKQ-LSKEGGDMKMFDIAERLETVMWE-----EKK 300


                 ....*
gi 340547913 161 LYPNV 165
Cdd:cd06117  301 MFPNL 305
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
 21-150 3.81e-21

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: 88.48  E-value: 3.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  21 RAMDRIFTLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRMLEEI-------GSVDRIPEYI 92
Cdd:cd06113  196 KLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIkenvkdwTDEDEVRAYL 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340547913  93 AKAKDK--NDPFRLM-GFGHRVYKNHDPRATVMRETCHEVLTELQIKDPlLDVAMELERIA 150
Cdd:cd06113  276 RKILNKeaFDKSGLIyGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEE-FALYERIERLA 335
PRK09569 PRK09569
citrate (Si)-synthase;
1-165 2.73e-20

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 86.34  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMfGVPtEEYKvnpiveRAMDRIFTLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLR-- 77
Cdd:PRK09569 210 FAHMI-GQP-KPYK------DVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGwi 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  78 --MLEEIGSVDRIPEYIAKA-KDKNDPFRLM-GFGHRVYKNHDPRATVMRETCHEVLTElqikDPLLDVAMELERIA--- 150
Cdd:PRK09569 282 qqFQEKLGGEEPTKEQVEQAlWDTLNAGQVIpGYGHAVLRKTDPRYTAQREFCLKHLPD----DPLFKLVAMIFEVApgv 357

                        170       180
                 ....*....|....*....|.
gi 340547913 151 ------LSDPyfvekklYPNV 165
Cdd:PRK09569 358 ltehgkTKNP-------WPNV 371
PRK14032 PRK14032
citrate synthase; Provisional
 1-132 5.78e-20

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 85.34  E-value: 5.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMfgVPTEEYkvNPIVERAMDRIFTLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLRML 79
Cdd:PRK14032 210 ILYML--RPDNKY--TELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMF 285

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340547913  80 EEI-------GSVDRIPEYIAKAKDKnDPF----RLMGFGHRVYKNHDPRATVMRETCHEVLTE 132
Cdd:PRK14032 286 EDIkenvkdwEDEDEIADYLTKILNK-EAFdksgLIYGMGHAVYTISDPRAVILKKFAEKLAKE 348
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
 1-127 2.32e-17

Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99857  Cd Length: 426  Bit Score: 77.72  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913   1 FLHMMfGVPTEEYkvnpivERAMDRIFTLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLR-- 77
Cdd:cd06103  209 FAHML-GYEDEEF------TDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKwl 281

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 340547913  78 --MLEEIG---SVDRIPEYiakAKDKNDPFRLM-GFGHRVYKNHDPRATVMRETCH 127
Cdd:cd06103  282 lkMQKELGkdvSDEELEKY---IWDTLNSGRVVpGYGHAVLRKTDPRFTCQREFAL 334
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
 21-153 1.04e-16

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: 74.14  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  21 RAMDRIFTLHADH-EQNASTSTVRLAGSSGANPF-ACIAAGIASLwGPAHGGANEACLRMLEEI----GSVDRIP-EYIA 93
Cdd:cd06100   32 RLLEALLVALADHgPATPSAHAARLTASAGPEDLqSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgDALDAAAaEFVA 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  94 KAKDKNdpFRLMGFGHRVYKNHDPRATVMretcHEVLTELQIKDPLLDVAMELERIALSD 153
Cdd:cd06100  111 EYRAAK--KRIPGFGHPVHKNPDPRVPRL----LELARELGPAGPHLDYALAVEKALTAA 164
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
 28-165 1.96e-15

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: 72.40  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  28 TLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLR----MLEEIG---SVDRIPEYIAK--AKD 97
Cdd:cd06105  227 TIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVwltkLQKEVGkdvSDEQLREYVWKtlNSG 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340547913  98 KNDPfrlmGFGHRVYKNHDPRATVMRETCHEVLTElqikDPLLDVAMELERIAlsDPYFVE----KKLYPNV 165
Cdd:cd06105  307 RVVP----GYGHAVLRKTDPRYTCQREFALKHLPN----DPLFKLVSQLYKIV--PPVLTEqgkaKNPWPNV 368
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
 27-165 6.06e-15

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: 71.00  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  27 FTLHADHEQ-NASTSTVRLAGSSGANPFACIAAGIASLWGPAHGGANEACLR----MLEEIGSV---DRIPEYIAKAKDK 98
Cdd:cd06106  228 IALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRwileMQKNIGSKatdQDIRDYLWKTLKS 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340547913  99 NdpfRLM-GFGHRVYKNHDPRATVMRETChEVLTELQiKDPLLDVAMELERIAlsDPYFVE----KKLYPNV 165
Cdd:cd06106  308 G---RVVpGYGHAVLRKPDPRFTALMEFA-QTRPELE-NDPVVQLVQKLSEIA--PGVLTEhgktKNPFPNV 372
PRK06224 PRK06224
citryl-CoA lyase;
21-128 2.52e-13

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 65.28  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547913  21 RAMDRIFTLHADHEQNASTSTVRLAGSSGANPFACIAAGIASLwGPAHGGANEACLRMLEEI-------GSVDRIPEYIA 93
Cdd:PRK06224  56 RLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaadagADLDAAARAIV 134

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 340547913  94 ---KAKDKndpfRLMGFGHRVYKNHDPRATVMRETCHE 128
Cdd:PRK06224 135 aeyRAAGK----RVPGFGHPLHKPVDPRAPRLLALARE 168
 
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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