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Conserved domains on  [gi|498124376|ref|WP_010438532|]
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2-methylcitrate synthase [Vibrio cyclitrophicus]

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 ...
30-404 0e+00

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 PRK12351:

Pssm-ID: 469765 [Multi-domain]  Cd Length: 378  Bit Score: 744.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  30 ASAPAIGGAGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQ 109
Cdd:PRK12351   2 AAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 110 PLKAALELIPADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEdQSEVCLG 186
Cdd:PRK12351  82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVE-TDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 187 GYFLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWK 266
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 267 TADEAETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHAS 346
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498124376 347 AYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
 
Name Accession Description Interval E-value
PRK12351 PRK12351
methylcitrate synthase; Provisional
30-404 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 744.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  30 ASAPAIGGAGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQ 109
Cdd:PRK12351   2 AAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 110 PLKAALELIPADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEdQSEVCLG 186
Cdd:PRK12351  82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVE-TDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 187 GYFLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWK 266
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 267 TADEAETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHAS 346
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498124376 347 AYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
38-401 0e+00

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: 656.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  38 AGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:cd06108    1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESDFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDQSEvCLGGYFLKMLTDKA 197
Cdd:cd06108   81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDED-SIAGHFLHLLHGKK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 198 PSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQ 277
Cdd:cd06108  160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 278 MLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIPTKL 357
Cdd:cd06108  240 KLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTEL 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 498124376 358 FTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPI 401
Cdd:cd06108  320 FTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
38-404 0e+00

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: 577.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376   38 AGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:TIGR01800   1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  118 IPADAHPMDVMRTGCSMLGNLEQE---SDFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDQSEVclGGYFLKMLT 194
Cdd:TIGR01800  81 LPAESHPMDVLRTAVSYLGALDPEkfgHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSI--AGNFLYMLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:TIGR01800 159 GEEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  275 IMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIP 354
Cdd:TIGR01800 239 IRKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIP 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 498124376  355 TKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:TIGR01800 319 TDLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
39-404 0e+00

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 536.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PADAHPMDVMRTGCSMLGNLEQES---DFSEQLFATERMLALFPAIICYWYRFSHdGVRIDTEDQSevcLG--GYFLKML 193
Cdd:COG0372   96 PRDAHPMDVLRTAVSALGAFDPDAddiDPEARLEKAIRLIAKLPTIAAYAYRYRR-GLPPVYPDPD---LSyaENFLYML 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 194 TDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAET 273
Cdd:COG0372  172 FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEE 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 274 NIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKR-----EKGLFCNADFFHASAY 348
Cdd:COG0372  252 YIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSGIVY 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:COG0372  332 HALGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
39-387 2.05e-155

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: 442.33  E-value: 2.05e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376   39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  119 PADAHPMDVMRTGCSMLGNLEQES----DFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDqsEVCLGGYFLKMLT 194
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAisdkADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDP--DLSYAENFLYMLF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:pfam00285 159 GYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  275 IMQMLA-NKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM-----KREKGLFCNADFFHASAY 348
Cdd:pfam00285 239 IRKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVApedlyFVEKNLYPNVDFYSGVLY 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 498124376  349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPS 387
Cdd:pfam00285 319 HALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
 
Name Accession Description Interval E-value
PRK12351 PRK12351
methylcitrate synthase; Provisional
30-404 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 744.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  30 ASAPAIGGAGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQ 109
Cdd:PRK12351   2 AAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 110 PLKAALELIPADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEdQSEVCLG 186
Cdd:PRK12351  82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVE-TDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 187 GYFLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWK 266
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 267 TADEAETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHAS 346
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498124376 347 AYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
38-401 0e+00

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: 656.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  38 AGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:cd06108    1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESDFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDQSEvCLGGYFLKMLTDKA 197
Cdd:cd06108   81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDED-SIAGHFLHLLHGKK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 198 PSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQ 277
Cdd:cd06108  160 PGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 278 MLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIPTKL 357
Cdd:cd06108  240 KLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTEL 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 498124376 358 FTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPI 401
Cdd:cd06108  320 FTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
38-404 0e+00

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: 577.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376   38 AGLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:TIGR01800   1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  118 IPADAHPMDVMRTGCSMLGNLEQE---SDFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDQSEVclGGYFLKMLT 194
Cdd:TIGR01800  81 LPAESHPMDVLRTAVSYLGALDPEkfgHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSI--AGNFLYMLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:TIGR01800 159 GEEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  275 IMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIP 354
Cdd:TIGR01800 239 IRKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIP 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 498124376  355 TKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:TIGR01800 319 TDLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
39-404 0e+00

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 536.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PADAHPMDVMRTGCSMLGNLEQES---DFSEQLFATERMLALFPAIICYWYRFSHdGVRIDTEDQSevcLG--GYFLKML 193
Cdd:COG0372   96 PRDAHPMDVLRTAVSALGAFDPDAddiDPEARLEKAIRLIAKLPTIAAYAYRYRR-GLPPVYPDPD---LSyaENFLYML 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 194 TDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAET 273
Cdd:COG0372  172 FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEE 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 274 NIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKR-----EKGLFCNADFFHASAY 348
Cdd:COG0372  252 YIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSGIVY 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:COG0372  332 HALGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
40-401 8.13e-171

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: 482.04  E-value: 8.13e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  40 LRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIP 119
Cdd:cd06117    3 LSGVAAGNTALCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 120 ADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSHDGVRID--TEDQSevcLGGYFLKMLT 194
Cdd:cd06117   83 AAAHPMDVMRTGVSVLGCVLPEKEdhpVSGARDIADRLMASLGSILLYWYHYSHNGKRIEveTDDDS---IGGHFLHLLH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:cd06117  160 GEKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 275 IMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIP 354
Cdd:cd06117  240 IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 498124376 355 TKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPI 401
Cdd:cd06117  320 TAMFTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
39-387 2.05e-155

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: 442.33  E-value: 2.05e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376   39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  119 PADAHPMDVMRTGCSMLGNLEQES----DFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDqsEVCLGGYFLKMLT 194
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAisdkADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDP--DLSYAENFLYMLF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:pfam00285 159 GYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  275 IMQMLA-NKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM-----KREKGLFCNADFFHASAY 348
Cdd:pfam00285 239 IRKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVApedlyFVEKNLYPNVDFYSGVLY 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 498124376  349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPS 387
Cdd:pfam00285 319 HALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
39-392 3.88e-144

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: 413.98  E-value: 3.88e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTV-GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:cd06110    2 GLEGVIAADSKISYIdGDAGI-LIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDqsEVCLGGYFLKMLT 194
Cdd:cd06110   81 LPKDAHPMDVLRTAVSALALYDPEADdmsREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDP--DLSHAANFLYMLT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:cd06110  159 GEKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 275 IMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIP 354
Cdd:cd06110  239 VKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIP 318
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 498124376 355 TKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTG 392
Cdd:cd06110  319 VDLFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
39-390 1.34e-135

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: 392.35  E-value: 1.34e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTV-GKSGtGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:cd06118    2 GLEGVKAKETSISYIdGDEG-ILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWYRFSH--DGVRID-TEDQSEvclggYFLK 191
Cdd:cd06118   81 LPKNAHPMDVLRTAVSALGSFDPFARdksPEARYEKAIRLIAKLPTIAANIYRNREglEIIAPDpDLSYAE-----NFLY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 192 MLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEA 271
Cdd:cd06118  156 MLFGEEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 272 ETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM---KREKGLFCNADFFHASAY 348
Cdd:cd06118  236 EAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIAlevLGEKGIYPNVDFYSGVVY 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENN-RIIRPSADY 390
Cdd:cd06118  316 KALGFPTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
39-401 1.40e-123

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 362.35  E-value: 1.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:PRK14033  12 GLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PADAHPMDVMRTGCSMLGN---LEQESDFSEQLFATERMLALFPAIICYWYRFSHDGVRIdtEDQSEVCLGGYFLKMLTD 195
Cdd:PRK14033  92 PTTCHPMDVVRTAVSYLGAedpEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPI--APRSDLGYAENFLHMCFG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 196 KAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNI 275
Cdd:PRK14033 170 EVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 276 MQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIPT 355
Cdd:PRK14033 250 RDALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMGFDI 329
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 498124376 356 KLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPI 401
Cdd:PRK14033 330 DFFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVPPI 375
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
39-397 1.09e-119

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: 351.71  E-value: 1.09e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:cd06111    2 GLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PADAHPMDVMRTGCSMLG--NLEQESDFSEQLFATE-RMLALFPAIICYWYRFSHDGVRIDTEDQSEVclGGYFLKMLTD 195
Cdd:cd06111   82 PKNCHPMDVLRTAVSVLGaeDSETDDSSPDANLAKAiRLLAQLPTVVAADIRRRKGLDPIPPDSDLGI--AENFLHMCFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 196 KAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNI 275
Cdd:cd06111  160 EVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 276 MQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIPT 355
Cdd:cd06111  240 LDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDI 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 498124376 356 KLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQE 397
Cdd:cd06111  320 DFFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPEQRP 361
PRK14035 PRK14035
citrate synthase; Provisional
34-404 2.05e-118

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 349.06  E-value: 2.05e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  34 AIGGAGLRGQSAGTTALCTVgkSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGL-PQPLK 112
Cdd:PRK14035   1 AELQRGLEGVIAAETKISSI--IDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLnDRVYQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 113 AALELIPADAHPMDVMRTGCSMLG----NLEQESDfSEQLFATERMLALFPAIICYWYRFSHDGVRIdtEDQSEVCLGGY 188
Cdd:PRK14035  79 HFEEYSTDHVHPMTALRTSVSYLAhfdpDAEEESD-EARYERAIRIQAKVASLVTAFARVRQGKEPL--KPRPDLSYAAN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 189 FLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTA 268
Cdd:PRK14035 156 FLYMLRGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 269 DEAETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAY 348
Cdd:PRK14035 236 GDVDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVY 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK14035 316 HVMGIPHDLFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
PRK14034 PRK14034
citrate synthase; Provisional
39-404 7.70e-114

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 337.51  E-value: 7.70e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGtgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:PRK14034   6 GLEGVVATTSSVSSIIDDT--LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PAD-AHPMDVMRTGCSMLGNLEQESDFSEQ---LFATERMLALFPAIICYWYRFsHDGVRIdTEDQSEVCLGGYFLKMLT 194
Cdd:PRK14034  84 DLKkVHPMSVLRTAISMLGLYDEEAEIMDEeanYRKAVRLQAKVPTIVAAFSRI-RKGLDP-VEPRKDLSLAANFLYMLN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:PRK14034 162 GEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVESY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 275 IMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDIP 354
Cdd:PRK14034 242 IHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGID 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 498124376 355 TKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK14034 322 HDLFTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
PRK12349 PRK12349
citrate synthase;
39-396 2.16e-108

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 323.21  E-value: 2.16e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:PRK12349   8 GLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 PADAHPMDVMRTGCSMLG----NLEQESDFSEQLFATeRMLALFPAIICYWYRFSHDGVRIDTEDQseVCLGGYFLKMLT 194
Cdd:PRK12349  88 PKETHPMDGLRTGVSALAgydnDIEDRSLEVNKSRAY-KLLSKVPNIVANSYHILNNEEPIEPLKE--LSYSANFLYMLT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 195 DKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETN 274
Cdd:PRK12349 165 GKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEEL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 275 IMQMLANKDKIMGFGHAIY-RESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKREKGLFCNADFFHASAYHFMDI 353
Cdd:PRK12349 245 LQKKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEKIMEKEKGLYPNLDYYAAPVYWMLGI 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 498124376 354 PTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQ 396
Cdd:PRK12349 325 PIQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIGERHV 367
PRK14036 PRK14036
citrate synthase; Provisional
39-404 3.97e-100

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 302.65  E-value: 3.97e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTV-GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:PRK14036   7 GLEGVPATQSSISYVdGQKGI-LEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESDFSEQLF---ATERMLALFPAIICYWY--RFSHDGVRIDTE-DQSEvclggYFLK 191
Cdd:PRK14036  86 FPETGHPMDALQASAAALGLFYSRRALDDPEYirdAVVRLIAKIPTMVAAFQliRKGNDPIQPRDDlDYAA-----NFLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 192 MLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEA 271
Cdd:PRK14036 161 MLTEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSVENV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 272 ETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKR---EKGLFCNADFFHASAY 348
Cdd:PRK14036 241 RPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVAEErlgPKGIYPNVDFYSGLVY 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK14036 321 RKLGIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
39-401 1.97e-98

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: 298.18  E-value: 1.97e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTV-GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:cd06112    4 GLAGVPAAESSISYIdGKNGI-LEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNL--EQESDFSEQLF---ATERMLALFPAIICYWYRFSHDGVRIDTEDqsEVCLGGYFLKM 192
Cdd:cd06112   83 FPETGHPMDMLQATVAALGMFypKPEVLKPNPDYidaATVKLIAKMPTLVAMWARIRNGDDPIEPRP--DLDYAENFLYM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 193 LTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAE 272
Cdd:cd06112  161 LFGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 273 TNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGD-KQLYAVSERVEAVMKR---EKGLFCNADFFHASAY 348
Cdd:cd06112  241 AYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCEEllgHKGVYPNVDFYSGIVY 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPEHQEWLPI 401
Cdd:cd06112  321 KELGIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYVPL 373
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
39-392 2.67e-91

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: 278.80  E-value: 2.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELI 118
Cdd:cd06109    2 GLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 pADAHPMDVMRTGCSMLGNleqesdfSEQLFATERMLALFPAIICYWYRFSHDGVRIdtEDQSEVCLGGYFLKMLTDKAP 198
Cdd:cd06109   82 -AGLDPMDALRALLALLPD-------SPDLATALRLLAAAPVITAALLRLSRGKQPI--APDPSLSHAADYLRMLTGEPP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 199 SELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQM 278
Cdd:cd06109  152 SEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 279 LANKDKIMGFGHAIYRESDPRNALIKRWSKELAqevGDKQLYAVSERVE----AVMKREK---GLFCNADFFHASAYHFM 351
Cdd:cd06109  232 LARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEqaalALLREYKpgrPLETNVEFYTALLLEAL 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 498124376 352 DIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTG 392
Cdd:cd06109  309 GLPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
39-390 5.76e-87

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: 264.95  E-value: 5.76e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPnakelddyktllvglrglpqplkaaleli 118
Cdd:cd06101    2 GLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP----------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 119 padahpmdvmrtgcsmlgnleqesDFSEQlfatermlalfpaiicywyrfshdgvridtedqsevclggyFLKMLTDKAP 198
Cdd:cd06101   53 ------------------------SYAEN-----------------------------------------FLYMLGGEEP 67
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 199 SELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKT--ADEAETNIM 276
Cdd:cd06101   68 DPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTpkNEPAEAYIR 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 277 QMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM---KREKGLFCNADFFHASAYHFMDI 353
Cdd:cd06101  148 KKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIApevLYEKKLYPNVDFYSGVLYKAMGF 227
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 498124376 354 PTKLFTPIFVMSRLTGWTAHVFEQRENN-RIIRPSADY 390
Cdd:cd06101  228 PTELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
189-390 6.54e-80

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: 244.94  E-value: 6.54e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 189 FLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKT- 267
Cdd:cd06099    6 FLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLEEIGTp 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 268 -ADEAETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM---KREKGLFCNADFF 343
Cdd:cd06099   86 kNEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAeevLYEKKLYPNVDFY 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 498124376 344 HASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENN-RIIRPSADY 390
Cdd:cd06099  166 SGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
PRK14037 PRK14037
citrate synthase; Provisional
39-404 1.07e-75

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 239.65  E-value: 1.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTV-GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALEL 117
Cdd:PRK14037   7 GLENVIIKVTNLTFIdGEKGI-LRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 118 IPADAHPMDVMRTGCSMLGNLEQESDFSEqlfaTER-----MLALFPAIICYWYRfSHDGVRIDTEDQSEvCLGGYFLKM 192
Cdd:PRK14037  86 MPRDSDAIGLMEAAFAALASIDKNFKWKE----NDKekaisIIAKMATIVANVYR-RKEGNKPRIPEPSD-SFAESFLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 193 LTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAE 272
Cdd:PRK14037 160 SFAREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 273 ----TNImqmLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGD-KQLYAVSERVEAVMKRE---KGLFCNADFFH 344
Cdd:PRK14037 240 mwfnDKI---INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEaKKYFEIAQKLEELGIKQfgsKGIYPNTDFYS 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498124376 345 ASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQREN-NRIIRPSADYTGPEHQEWLPIHLR 404
Cdd:PRK14037 317 GIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEHREYVPIDKR 377
PRK14032 PRK14032
citrate synthase; Provisional
60-404 2.06e-73

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 235.95  E-value: 2.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQ------FEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQ------PLKA------------AL 115
Cdd:PRK14032  68 LYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDgftrdmILKApskdimnslarsVL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 116 ELIPADAHPMDVmrtgcSMLGNLEQesdfSEQLfatermLALFPAIICYWY---RFSHDGVR-IDTEDQSEVCLGGYFLK 191
Cdd:PRK14032 148 ALYSYDDNPDDT-----SIDNVLRQ----SISL------IARFPTLAVYAYqayRHYHDGKSlYIHPPKPELSTAENILY 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 192 ML-TDKAPSELHKQVMHCSLTLYAEHEF-NASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQ------ 263
Cdd:PRK14032 213 MLrPDNKYTELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEdikenv 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 264 -DWKTADEAETNIMQMLaNK---DK---IMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVE----AVMKR 332
Cdd:PRK14032 293 kDWEDEDEIADYLTKIL-NKeafDKsglIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEklapELIAE 371
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498124376 333 EKGLF---C-NADFFHASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQR-ENNRIIRPSADYTGpEHQEWLPIHLR 404
Cdd:PRK14032 372 ERGIYkgvSaNVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELvNGGKIIRPAYKSVL-ERREYVPLEER 447
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
60-392 2.51e-73

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: 234.47  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQ------FEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQ------PLKAALELIpadahpMDV 127
Cdd:cd06113   38 LYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDnfvedvILKAPSKDI------MNK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 128 MRTGCSMLGNLEQESD---FSEQLFATERMLALFPAIICYWY---RFSHDG----VRIDTEDQSevcLGGYFLKML-TDK 196
Cdd:cd06113  112 LQRSVLALYSYDDKPDdisLENVLRQSIQLIARLPTIAVYAYqakRHYYDGeslyIHHPQPELS---TAENILSMLrPDK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 197 APSELHKQVMHCSLTLYAEHEF-NASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEM-------IQDWKTA 268
Cdd:cd06113  189 KYTELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMledikenVKDWTDE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 269 DEAETNIMQMLaNK---DK---IMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVE----AVMKREKGLF- 337
Cdd:cd06113  269 DEVRAYLRKIL-NKeafDKsglIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERIErlapEVIAEERGIGk 347
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498124376 338 --C-NADFFHASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQREN-NRIIRPSADYTG 392
Cdd:cd06113  348 tvCaNVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNsGRIIRPAYKYVG 406
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
54-392 1.94e-72

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: 232.09  E-value: 1.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  54 GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCS 133
Cdd:cd06114   46 GEKGI-LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVN 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 134 MLGNLEQES----DFSEQLFATERMLALFPAIICYWYRFSHDGVRIDTEDQSEVClgGYFLKML-----TDKAPSELHKQ 204
Cdd:cd06114  125 ALSAFYPDSldvnDPEQRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYV--ENFLHMMfavpyEPYEVDPVVVK 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 205 VMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETnIMQMLANKD- 283
Cdd:cd06114  203 ALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDK-YIAKAKDKNd 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 284 --KIMGFGHAIYRESDPRNALIKRWSKELAQEVG-DKQLYAVSERVEAVMKR-----EKGLFCNADFFHASAYHFMDIPT 355
Cdd:cd06114  282 pfRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGkDDPLLEIAMELEEIALKddyfiERKLYPNVDFYSGIILRALGIPT 361
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 498124376 356 KLFTPIFVMSRLTGWTAHVFEQREN--NRIIRPSADYTG 392
Cdd:cd06114  362 EMFTVLFALGRTPGWIAQWREMHEDpeLKIGRPRQLYTG 400
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
54-392 3.26e-66

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: 215.38  E-value: 3.26e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  54 GKSGTgLTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCS 133
Cdd:cd06107   24 GDKGI-LLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRDAHPMGILCAGLS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 134 MLGNLEQESD--FSEQLF---------ATERMLALFPAI--ICYWYRFSHDGVRIDtedqSEVCLGGYFLKML--TDKAP 198
Cdd:cd06107  103 ALSAFYPEAIpaHTGDLYqnnpevrdkQIIRTLAKMPTIaaAAYCHRIGRPFVYPR----ANLSYIENFLYMMgyVDQEP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 199 SELHK---QVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNI 275
Cdd:cd06107  179 YEPNPrlaRALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREIGTPENVPAFI 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 276 MQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMK-----REKGLFCNADFFHASAYHF 350
Cdd:cd06107  259 ERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALedeyfVSRKLYPNVDFYSGFIYKA 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 498124376 351 MDIPTKLFTPIFVMSRLTGWTAHVFEQREN--NRIIRPSADYTG 392
Cdd:cd06107  339 LGFPPEFFTVLFAVARTSGWMAHWREMMEDplQRIWRPRQVYTG 382
PLN02456 PLN02456
citrate synthase
60-399 3.08e-63

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 209.88  E-value: 3.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCSMLgnle 139
Cdd:PLN02456  88 LRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMAL---- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 140 qeSDFSEQLFATE-----------------RMLALFPAIICYWYRFSH-DGVRIDTEDQSevcLGGYFLKML-----TDK 196
Cdd:PLN02456 164 --STFSPDANAYLrgqhkykswevrdedivRLIGKLPTLAAAIYRRMYgRGPVIPDNSLD---YAENFLYMLgslgdRSY 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 197 APSELHKQVMHCSLTLYAEHEFNASTFAAR-VCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNI 275
Cdd:PLN02456 239 KPDPRLARLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYV 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 276 MQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVM-------KREkgLFCNADFFHASAY 348
Cdd:PLN02456 319 EGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVAlldeyfkVRK--LYPNVDFYSGVLL 396
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498124376 349 HFMDIPTKLFTPIFVMSRLTGWTAHVFEQR--ENNRIIRPSADYTGpehqEWL 399
Cdd:PLN02456 397 RALGFPEEFFTVLFAVSRAAGYLSQWDEALglPDERIMRPKQVYTG----EWL 445
gltA PRK05614
citrate synthase;
60-392 9.62e-61

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 202.03  E-value: 9.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMrtgCSMLGNLE 139
Cdd:PRK05614  69 LLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVL---CGVVGALS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 140 ---QES----DFSEQLFATERMLALFPAIICYWYRFSHdGVRIDTEDQSevcLG--GYFLKMLTdKAPSELHK------Q 204
Cdd:PRK05614 146 afyHDSldinDPEHREIAAIRLIAKMPTLAAMAYKYSI-GQPFVYPRND---LSyaENFLRMMF-ATPCEEYEvnpvlvR 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 205 VMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQMlanKDK 284
Cdd:PRK05614 221 ALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARA---KDK 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 285 -----IMGFGHAIYRESDPRNALIKRWSKELAQEVG-DKQLYAVSERVEAVMKR-----EKGLFCNADFFHASAYHFMDI 353
Cdd:PRK05614 298 ndgfrLMGFGHRVYKNYDPRAKIMRETCHEVLKELGlNDPLLEVAMELEEIALNdeyfiERKLYPNVDFYSGIILKALGI 377
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 498124376 354 PTKLFTPIFVMSRLTGWTAHVFEQREN--NRIIRPSADYTG 392
Cdd:PRK05614 378 PTSMFTVIFALARTVGWIAHWNEMHSDpeQKIGRPRQLYTG 418
PRK12350 PRK12350
citrate synthase 2; Provisional
39-394 1.89e-59

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 196.72  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  39 GLRGQSAGTTALCTVGKSGTGLTYRGYDITDLANHAQFEEVAHLLLRG----HLPNAKelddyktllvglrglPQPLKAA 114
Cdd:PRK12350   4 GLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGrfgpGLPPAE---------------PFPLPVH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 115 LELIPADAHPMDVMRTGCSMLGNLEQESDFSeqlfATERMLALFPAIICYWYRfSHDGVRIDTEDQSEVCLGGYFLKMLT 194
Cdd:PRK12350  69 LGDARVDVQAALAMLAPVWGFRPLLDIDDLT----ARLDLARASVMALSAVAQ-SARGIGQPAVPQREIDHAATILERFM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 195 DK---APSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEA 271
Cdd:PRK12350 144 GRwrgEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVERTGDA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 272 ETNIMQMLANKDKIMGFGHAIYRESDPRNALIKRWSKELAQEvgdkqLYAVSERVEAVM-------KREKGLFCNADFFH 344
Cdd:PRK12350 224 RGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGAP-----RYEVAEAVEQAAlaelrerRPDRPLETNVEFWA 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 498124376 345 ASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTGPE 394
Cdd:PRK12350 299 AVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPA 348
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
60-400 9.21e-54

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: 183.80  E-value: 9.21e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCSMLGNLE 139
Cdd:cd06115   49 LRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 140 QESDFS--------------EQLFateRMLALFPAIICYWYRfsHDGVRIDTEDQSEVCLGGYFLKML-----TDKAPSE 200
Cdd:cd06115  129 PEANPAlagqdiyknkqvrdKQIV---RILGKAPTIAAAAYR--RRAGRPPNLPSQDLSYTENFLYMLdslgeRKYKPNP 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 201 LHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQMLA 280
Cdd:cd06115  204 RLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKN 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 281 NKDKIMGFGHAIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVE-AVMK----REKGLFCNADFFHASAYHFMDIPT 355
Cdd:cd06115  284 RKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKDPLIEIAVALEkAALSdeyfVKRKLYPNVDFYSGLIYRAMGFPT 363
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 498124376 356 KLFTPIFVMSRLTGWTAHVFEQREN--NRIIRPSADYTGPEHQEWLP 400
Cdd:cd06115  364 DFFPVLFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYVP 410
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
60-398 1.63e-49

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: 172.66  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376   60 LTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMrtgCSMLGNLE 139
Cdd:TIGR01798  56 LLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVM---VGVVGALS 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  140 -------QESDFSEQLFATERMLALFPAIICYWYRFSHDGVRIdtEDQSEVCLGGYFLKML-----TDKAPSELHKQVMH 207
Cdd:TIGR01798 133 afyhdalDINDPRHREISAIRLIAKIPTLAAMSYKYSIGQPFV--YPRNNLSYAENFLHMMfatpcEDYKVNPVLARAMD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  208 CSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQMLANKD--KI 285
Cdd:TIGR01798 211 RIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDpfRL 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  286 MGFGHAIYRESDPRNALIKRWSKELAQEVG--DKQLYAVSERVEAVMKR-----EKGLFCNADFFHASAYHFMDIPTKLF 358
Cdd:TIGR01798 291 MGFGHRVYKNYDPRAKVMRETCHEVLKELGlhDDPLFKLAMELEKIALNdpyfiERKLYPNVDFYSGIILKAMGIPTSMF 370
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 498124376  359 TPIFVMSRLTGWTAHVFEQRENN--RIIRPSADYTGPEHQEW 398
Cdd:TIGR01798 371 TVIFALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
60-401 3.56e-49

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: 170.78  E-value: 3.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  60 LTYRGYDITDLANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCSMLGNLE 139
Cdd:cd06116   29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 140 QES----DFSEQLFATERMLALFPAIICYWYRFSHdGVRIDTEDqSEVCLGGYFLKML---TDK--APSELHKQVMHCSL 210
Cdd:cd06116  109 PEAknigDEEQRNKQIIRLIGKMPTIAAFAYRHRL-GLPYVLPD-NDLSYTGNFLSMLfkmTEPkyEPNPVLAKALDVLF 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 211 TLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKTADEAETNIMQMLANKDKIMGFGH 290
Cdd:cd06116  187 ILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGH 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 291 AIYRESDPRNALIKRWSKELAQEVGDKQLYAVSERVEAVMKRE-----KGLFCNADFFHASAYHFMDIPTKLFTPIFVMS 365
Cdd:cd06116  267 RVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDeyfisRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIP 346
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 498124376 366 RLTGWTAHVFEQREN--NRIIRPSADYTGPEHQEWLPI 401
Cdd:cd06116  347 RTSGWLAQWIEMLRDpeQKIARPRQVYTGPRDRDYVPI 384
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
24-392 8.42e-40

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: 143.17  E-value: 8.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  24 KPESKPASApAIGGAGLRGQSAGTTAlctvgkSGTGLTYRGYDITDLANHAQFEEVAHLLLRGHLPnakelddyktllvg 103
Cdd:cd06102    4 RPRAAVAAA-ALDWGEPVLESAITLI------TEGRLFYRGRDAVELAETATLEEVAALLWDGDEA-------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 104 lRGLPQPLKAALELIPADAHPMdvmrtgcsmlgnleqesdfSEQLFATermlalfpaiicyWyrfshdGVRIDTEDqsev 183
Cdd:cd06102   63 -ARLLRLLAAALLGAAPSDAPV-------------------HRRLARA-------------W------GLDPAAAD---- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 184 clggyflkmLTDKApselhkqvmhcsLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQ 263
Cdd:cd06102  100 ---------LLRRA------------LVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLD 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 264 DWKTADEAETNIMQMLANKDKIMGFGHAIYRESDPR-NALIKRWSKELAQEVGDKQlyavseRVEAVMKREKGLFCNADF 342
Cdd:cd06102  159 EALRAGDAEAAVRERLRRGEALPGFGHPLYPDGDPRaAALLAALRPLGPAAPPAAR------ALIEAARALTGARPNIDF 232
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 498124376 343 FHASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRPSADYTG 392
Cdd:cd06102  233 ALAALTRALGLPAGAAFALFALGRSAGWIAHALEQRAQGKLIRPRARYVG 282
PRK09569 PRK09569
citrate (Si)-synthase;
34-299 9.73e-24

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 102.14  E-value: 9.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  34 AIGGAglRGQSAGTTALCTVGKSgTGLTYRGYDITDL---------ANHAQFEEVAHLLLRGHLPNAKELDDYKTLLVGL 104
Cdd:PRK09569  38 CIGGA--RDIRSLVTDISYLDPQ-EGIRFRGKTIPETfealpkapgSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKR 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 105 RGLPQPLKAALELIPADAHPMDVMRTGCSMLgnlEQESDFS--------EQLFATERM-------LALFPAIICYWYRFS 169
Cdd:PRK09569 115 QNVPQYVIDAIRALPRDSHPMVMLSVGILAM---QRESKFAkfynegkfNKMDAWEYMyedasdlVARIPVIAAYIYNLK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 170 HDGvriDTEDQS--EVCLGGYFLKMLTDKAPselHKQVMHCSLTLYAEHEF-NASTFAARVCASTLSDIHSCVTAAIGTL 246
Cdd:PRK09569 192 YKG---DKQIPSdpELDYGANFAHMIGQPKP---YKDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGL 265
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498124376 247 RGSLHGGANEAAMEMIQDWK--------TADEAETNIMQMLANKDKIMGFGHAIYRESDPR 299
Cdd:PRK09569 266 AGPLHGLANQEVLGWIQQFQeklggeepTKEQVEQALWDTLNAGQVIPGYGHAVLRKTDPR 326
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
179-386 1.52e-23

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: 97.64  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 179 DQSEVC----LGGYFLKMLTDKAPSELHKQVMHCSLTLYAEH-EFNASTFAARVCAST-LSDIHSCVTAAIGTLrGSLHG 252
Cdd:cd06100    3 DLSDLIgkisFGDVLYLLLKGRLPTPYEARLLEALLVALADHgPATPSAHAARLTASAgPEDLQSAVAAGLLGI-GDRFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 253 GANEAAMEMIQdwKTADEAETNIM-------QMLANKDKIMGFGHAIYRESDPRnaliKRWSKELAQEVGDKQLY-AVSE 324
Cdd:cd06100   82 GAGEGAARLFK--EAVDSGDALDAaaaefvaEYRAAKKRIPGFGHPVHKNPDPR----VPRLLELARELGPAGPHlDYAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498124376 325 RVEAVM--KREKGLFCNADFFHASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQRENNRIIRP 386
Cdd:cd06100  156 AVEKALtaAKGKPLPLNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYR 219
PRK06224 PRK06224
citryl-CoA lyase;
186-397 4.04e-22

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 94.55  E-value: 4.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 186 GGYFLKMLTDKAPSELHKQVMHCSLTLYAEHEFNASTFAARVCASTLSDIHSCVTAAIGTLrGSLHGGANEAAMEMIQD- 264
Cdd:PRK06224  38 TDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEi 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 265 --WKTAD-----EAETNIMQMLANKDKIMGFGHAIYRESDPR-NALikrwsKELAQEVGDKQLY-AVSERVEAVMKREKG 335
Cdd:PRK06224 117 aaAADAGadldaAARAIVAEYRAAGKRVPGFGHPLHKPVDPRaPRL-----LALAREAGVAGRHcRLAEALEAALAAAKG 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 336 --LFCNADFFHASAYHFMDIPTKLFTPIFVMSRLTGWTAHVFEQREN---NRIIRPSAD---YTGPEHQE 397
Cdd:PRK06224 192 kpLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQpigFRIWDPAEEaveYTGPPPRE 261
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
58-299 1.18e-15

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: 78.11  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  58 TGLTYRGYDITDLANHAQ---------FEEVAHLLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVM 128
Cdd:cd06103   57 EGIRFRGKTIPECQELLPkadgggeplPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 129 RTGCSMLgnlEQESDFSEQLFATE---------------RMLALFPAIICYWYRFSHDGVRIDTEDQSEVCLGGYFLKML 193
Cdd:cd06103  137 SAAILAL---QSESKFAKAYAEGKinkttyweyvyedamDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHML 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 194 TDKapSELHKQVMHCSLTLYAEHEF-NASTFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAM-------EMIQDW 265
Cdd:cd06103  214 GYE--DEEFTDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLkwllkmqKELGKD 291
                        250       260       270
                 ....*....|....*....|....*....|....
gi 498124376 266 KTADEAETNIMQMLANKDKIMGFGHAIYRESDPR 299
Cdd:cd06103  292 VSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPR 325
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
82-299 2.05e-12

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: 68.16  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  82 LLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCSMLgnlEQESDFSEqlfATER-------- 153
Cdd:cd06105   90 LLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITAL---NSESKFAK---AYAEgihkskyw 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 154 ---------MLALFPAIICYWYRFSHDGVRIDTEDqSEVCLGGYFLKML--TDKAPSELhkqvMHCSLTLYAEHEF-NAS 221
Cdd:cd06105  164 eyvyedsmdLIAKLPCVAAKIYRNLYRGGKIIAID-SNLDWSANFANMLgyTDPQFTEL----MRLYLTIHSDHEGgNVS 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 222 TFAARVCASTLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWKT------ADEAETN-IMQMLANKDKIMGFGHAIYR 294
Cdd:cd06105  239 AHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKevgkdvSDEQLREyVWKTLNSGRVVPGYGHAVLR 318

                 ....*
gi 498124376 295 ESDPR 299
Cdd:cd06105  319 KTDPR 323
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
82-369 1.86e-11

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: 65.22  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376  82 LLLRGHLPNAKELDDYKTLLVGLRGLPQPLKAALELIPADAHPMDVMRTGCSMLG-------NLEQ---ESDFSEQLFAT 151
Cdd:cd06106   90 LLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNhdskfaaAYEKgikKTEYWEPTLED 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 152 E-RMLALFPAIICYWYRFSHDGVRIDTEDQSEVCLGGYFLKMLTDKAPSELHkQVMHCSLTLYAEHEF-NASTFAARVCA 229
Cdd:cd06106  170 SlNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLDFV-DLLRLYIALHGDHEGgNVSAHTTHLVG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124376 230 STLSDIHSCVTAAIGTLRGSLHGGANEAAMEMIQDWK-------TADEAETNIMQMLANKDKIMGFGHAIYRESDPRNAL 302
Cdd:cd06106  249 SALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQknigskaTDQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTA 328
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498124376 303 IKRWSKELAQEVGDKQLYAV---SERVEAVMK---REKGLFCNADffHASA---YHFMDIPTKLFTPIFVMSRLTG 369
Cdd:cd06106  329 LMEFAQTRPELENDPVVQLVqklSEIAPGVLTehgKTKNPFPNVD--AASGvlfYHYGIREFLYYTVIFGVSRALG 402
 
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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