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Conserved domains on  [gi|516389467|ref|WP_017779027|]
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MULTISPECIES: 2-methylcitrate synthase [Aeromonas]

Protein Classification

citrate synthase family protein( domain architecture ID 475)

citrate synthase family protein similar to citrate synthase that catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CS_ACL-C_CCL super family cl00416
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
1-375 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: 697.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   1 MGQQKPLGGAGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLP 80
Cdd:PRK12351   1 MAAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  81 AALLEVLERIPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIG 157
Cdd:PRK12351  81 AAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 158 GHFLALLHQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQ 237
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 238 DEAQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHAS 317
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516389467 318 AYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
 
Name Accession Description Interval E-value
PRK12351 PRK12351
methylcitrate synthase; Provisional
1-375 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 697.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   1 MGQQKPLGGAGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLP 80
Cdd:PRK12351   1 MAAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  81 AALLEVLERIPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIG 157
Cdd:PRK12351  81 AAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 158 GHFLALLHQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQ 237
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 238 DEAQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHAS 317
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516389467 318 AYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
10-372 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: 670.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  10 AGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06108    1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPEDGFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIGGHFLALLHQKAP 169
Cdd:cd06108   81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 170 SELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAK 249
Cdd:cd06108  161 GELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLEK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 250 LAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPTKLF 329
Cdd:cd06108  241 LERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTELF 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 516389467 330 TPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSL 372
Cdd:cd06108  321 TPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
11-375 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: 560.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PADAHPMDVLRTGCSMLGDLEPE---DGFEHEHEVADRLLAAFPGILLYWYKFSHdGVRIALDTDEECIGGHFLALLHQK 167
Cdd:COG0372   96 PRDAHPMDVLRTAVSALGAFDPDaddIDPEARLEKAIRLIAKLPTIAAYAYRYRR-GLPPVYPDPDLSYAENFLYMLFGE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 168 APSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQ 247
Cdd:COG0372  175 EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIR 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 248 AKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYHYM 322
Cdd:COG0372  255 KALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSGIVYHAL 334
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516389467 323 GIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:COG0372  335 GIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
10-375 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: 549.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   10 AGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:TIGR01800   1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   90 IPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:TIGR01800  81 LPAESHPMDVLRTAVSYLGALDPEKFghtPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDS-IAGNFLYMLHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  247 QAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPT 326
Cdd:TIGR01800 240 RKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPT 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 516389467  327 KLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:TIGR01800 320 DLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
11-358 2.59e-167

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: 471.61  E-value: 2.59e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   91 PADAHPMDVLRTGCSMLGDLEPEDGFE----HEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAISDkadyWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLS-YAENFLYMLFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  247 QAKLA-AKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYH 320
Cdd:pfam00285 240 RKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEdlyfvEKNLYPNVDFYSGVLYH 319
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 516389467  321 YMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPS 358
Cdd:pfam00285 320 ALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
 
Name Accession Description Interval E-value
PRK12351 PRK12351
methylcitrate synthase; Provisional
1-375 0e+00

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 697.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   1 MGQQKPLGGAGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLP 80
Cdd:PRK12351   1 MAAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  81 AALLEVLERIPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIG 157
Cdd:PRK12351  81 AAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 158 GHFLALLHQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQ 237
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 238 DEAQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHAS 317
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516389467 318 AYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK12351 321 SYHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
10-372 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: 670.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  10 AGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06108    1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPEDGFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIGGHFLALLHQKAP 169
Cdd:cd06108   81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 170 SELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAK 249
Cdd:cd06108  161 GELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLEK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 250 LAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPTKLF 329
Cdd:cd06108  241 LERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTELF 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 516389467 330 TPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSL 372
Cdd:cd06108  321 TPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
11-375 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: 560.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:COG0372   16 GLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PADAHPMDVLRTGCSMLGDLEPE---DGFEHEHEVADRLLAAFPGILLYWYKFSHdGVRIALDTDEECIGGHFLALLHQK 167
Cdd:COG0372   96 PRDAHPMDVLRTAVSALGAFDPDaddIDPEARLEKAIRLIAKLPTIAAYAYRYRR-GLPPVYPDPDLSYAENFLYMLFGE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 168 APSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQ 247
Cdd:COG0372  175 EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIR 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 248 AKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYHYM 322
Cdd:COG0372  255 KALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSGIVYHAL 334
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516389467 323 GIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:COG0372  335 GIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
10-375 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: 549.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   10 AGLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:TIGR01800   1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   90 IPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:TIGR01800  81 LPAESHPMDVLRTAVSYLGALDPEKFghtPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDS-IAGNFLYMLHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  247 QAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPT 326
Cdd:TIGR01800 240 RKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPT 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 516389467  327 KLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:TIGR01800 320 DLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
12-372 9.32e-177

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: 495.90  E-value: 9.32e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  12 LRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIP 91
Cdd:cd06117    3 LSGVAAGNTALCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  92 ADAHPMDVLRTGCSMLGDLEPEdgfEHEH------EVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIGGHFLALLH 165
Cdd:cd06117   83 AAAHPMDVMRTGVSVLGCVLPE---KEDHpvsgarDIADRLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 166 QKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRE 245
Cdd:cd06117  160 GEKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 246 LQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIP 325
Cdd:cd06117  240 IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 516389467 326 TKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSL 372
Cdd:cd06117  320 TAMFTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
11-358 2.59e-167

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: 471.61  E-value: 2.59e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   91 PADAHPMDVLRTGCSMLGDLEPEDGFE----HEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEAISDkadyWENALRDDLIAKLPTIAAYIYRHRRGLPPIYPDPDLS-YAENFLYMLFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  247 QAKLA-AKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYH 320
Cdd:pfam00285 240 RKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEdlyfvEKNLYPNVDFYSGVLYH 319
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 516389467  321 YMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPS 358
Cdd:pfam00285 320 ALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-361 3.68e-155

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: 440.50  E-value: 3.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTV-GKSGtGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06118    2 GLEGVKAKETSISYIdGDEG-ILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPEDG---FEHEHEVADRLLAAFPGILLYWYKFSHdGVRIALDTDEECIGGHFLALLHQ 166
Cdd:cd06118   81 LPKNAHPMDVLRTAVSALGSFDPFARdksPEARYEKAIRLIAKLPTIAANIYRNRE-GLEIIAPDPDLSYAENFLYMLFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:cd06118  160 EEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 247 QAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE---EKELFPNADFFHASAYHYMG 323
Cdd:cd06118  240 WKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEvlgEKGIYPNVDFYSGVVYKALG 319
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 516389467 324 IPTKLFTPIFVCSRVTGWCAHVMEQREHN-RIIRPSADY 361
Cdd:cd06118  320 FPTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
11-363 8.20e-149

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: 424.38  E-value: 8.20e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTV-GKSGTgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06110    2 GLEGVIAADSKISYIdGDAGI-LIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPE---DGFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDtDEECIGGHFLALLHQ 166
Cdd:cd06110   81 LPKDAHPMDVLRTAVSALALYDPEaddMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPD-PDLSHAANFLYMLTG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:cd06110  160 EKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 247 QAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPT 326
Cdd:cd06110  240 KDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIPV 319
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 516389467 327 KLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVG 363
Cdd:cd06110  320 DLFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
11-370 3.27e-134

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 388.15  E-value: 3.27e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:PRK14033  12 GLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PADAHPMDVLRTGCSMLG--DLEPED-GFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQK 167
Cdd:PRK14033  92 PTTCHPMDVVRTAVSYLGaeDPEADDsSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLG-YAENFLHMCFGE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 168 APSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQ 247
Cdd:PRK14033 171 VPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLR 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 248 AKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPTK 327
Cdd:PRK14033 251 DALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMGFDID 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 516389467 328 LFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFV 370
Cdd:PRK14033 331 FFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVP 373
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
11-367 7.71e-127

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: 369.05  E-value: 7.71e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:cd06111    2 GLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PADAHPMDVLRTGCSMLG--DLEPED-GFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQK 167
Cdd:cd06111   82 PKNCHPMDVLRTAVSVLGaeDSETDDsSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLG-IAENFLHMCFGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 168 APSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQ 247
Cdd:cd06111  161 VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWML 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 248 AKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPTK 327
Cdd:cd06111  241 DALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDID 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 516389467 328 LFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPR 367
Cdd:cd06111  321 FFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPEQR 360
PRK14035 PRK14035
citrate synthase; Provisional
11-375 3.21e-118

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 347.52  E-value: 3.21e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVgkSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTL-PAALLEVLER 89
Cdd:PRK14035   6 GLEGVIAAETKISSI--IDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLnDRVYQHFEEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEP---EDGFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:PRK14035  84 STDHVHPMTALRTSVSYLAHFDPdaeEESDEARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLS-YAANFLYMLRG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 167 KAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARREL 246
Cdd:PRK14035 163 ELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVDAYL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 247 QAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYMGIPT 326
Cdd:PRK14035 243 DEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGIPH 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 516389467 327 KLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK14035 323 DLFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
PRK14034 PRK14034
citrate synthase; Provisional
11-375 3.13e-116

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 342.51  E-value: 3.13e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGtgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:PRK14034   6 GLEGVVATTSSVSSIIDDT--LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PAD-AHPMDVLRTGCSMLG--DLEPE-DGFEHEHEVADRLLAAFPGILLywyKFSHdgVRIALD----TDEECIGGHFLA 162
Cdd:PRK14034  84 DLKkVHPMSVLRTAISMLGlyDEEAEiMDEEANYRKAVRLQAKVPTIVA---AFSR--IRKGLDpvepRKDLSLAANFLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 163 LLHQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQA 242
Cdd:PRK14034 159 MLNGEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 243 RRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEEKELFPNADFFHASAYHYM 322
Cdd:PRK14034 239 ESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCL 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516389467 323 GIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK14034 319 GIDHDLFTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
PRK12349 PRK12349
citrate synthase;
11-368 6.31e-114

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 336.31  E-value: 6.31e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:PRK12349   8 GLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 PADAHPMDVLRTGCSMLG--DLEPED-GFEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDtDEECIGGHFLALLHQK 167
Cdd:PRK12349  88 PKETHPMDGLRTGVSALAgyDNDIEDrSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPL-KELSYSANFLYMLTGK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 168 APSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQ 247
Cdd:PRK12349 167 KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEELLQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 248 AKLAAKEKIMGFGHAVY-RTSDPRNVIIKGWSAKLAEAVGDDRLYRVsCEA-EKVMWEEKELFPNADFFHASAYHYMGIP 325
Cdd:PRK12349 247 KKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEM-CEAgEKIMEKEKGLYPNLDYYAAPVYWMLGIP 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 516389467 326 TKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGpaPRH 368
Cdd:PRK12349 326 IQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIG--ERH 366
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-372 2.64e-112

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: 332.47  E-value: 2.64e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTV-GKSGTgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06112    4 GLAGVPAAESSISYIdGKNGI-LEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPEDGF-----EHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALL 164
Cdd:cd06112   83 FPETGHPMDMLQATVAALGMFYPKPEVlkpnpDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLD-YAENFLYML 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 165 HQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARR 244
Cdd:cd06112  162 FGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVKA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 245 ELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGD-DRLYRVSCEAEKVMWE---EKELFPNADFFHASAYH 320
Cdd:cd06112  242 YLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCEEllgHKGVYPNVDFYSGIVYK 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516389467 321 YMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSL 372
Cdd:cd06112  322 ELGIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYVPL 373
PRK14036 PRK14036
citrate synthase; Provisional
11-375 5.43e-111

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 329.23  E-value: 5.43e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTV-GKSGTgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:PRK14036   7 GLEGVPATQSSISYVdGQKGI-LEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPEDGF---EHEHEVADRLLAAFPGILLYWY--KFSHDGVRIALDTDeecIGGHFLALL 164
Cdd:PRK14036  86 FPETGHPMDALQASAAALGLFYSRRALddpEYIRDAVVRLIAKIPTMVAAFQliRKGNDPIQPRDDLD---YAANFLYML 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 165 HQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARR 244
Cdd:PRK14036 163 TEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSVENVRP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 245 ELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE---EKELFPNADFFHASAYHY 321
Cdd:PRK14036 243 YLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVAEErlgPKGIYPNVDFYSGLVYRK 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516389467 322 MGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK14036 323 LGIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-361 2.57e-99

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: 295.38  E-value: 2.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDeqqledykrtlrslrtlpaallevleri 90
Cdd:cd06101    2 GLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPS---------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 padahpmdvlrtgcsmlgdlepedgfehehevadrllaafpgillywykfshdgvrialdtdeecIGGHFLALLHQKAPS 170
Cdd:cd06101   54 -----------------------------------------------------------------YAENFLYMLGGEEPD 68
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 171 ELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQ--ARRELQA 248
Cdd:cd06101   69 PEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKNepAEAYIRK 148
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 249 KLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE---EKELFPNADFFHASAYHYMGIP 325
Cdd:cd06101  149 KLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEvlyEKKLYPNVDFYSGVLYKAMGFP 228
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 516389467 326 TKLFTPIFVCSRVTGWCAHVMEQREHN-RIIRPSADY 361
Cdd:cd06101  229 TELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
11-363 3.42e-93

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: 282.66  E-value: 3.42e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERI 90
Cdd:cd06109    2 GLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  91 pADAHPMDVLRTGCSMLGDlepedgfEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECiGGHFLALLHQKAPS 170
Cdd:cd06109   82 -AGLDPMDALRALLALLPD-------SPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSH-AADYLRMLTGEPPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 171 ELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAKL 250
Cdd:cd06109  153 EAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREAL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 251 AAKEKIMGFGHAVYRTSDPRNVIIKGwsaKLAEAVGDDRLYRVSCEAEKVMWEE-------KELFPNADFFHASAYHYMG 323
Cdd:cd06109  233 ARGERLMGFGHRVYRVRDPRADVLKA---AAERLGAPDERLEFAEAVEQAALALlreykpgRPLETNVEFYTALLLEALG 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 516389467 324 IPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVG 363
Cdd:cd06109  310 LPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
156-361 3.29e-86

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: 259.96  E-value: 3.29e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 156 IGGHFLALLHQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIE- 234
Cdd:cd06099    2 YAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLEe 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 235 ---PWQDEAQArrELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE---EKELF 308
Cdd:cd06099   82 igtPKNEPAEA--YIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEvlyEKKLY 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516389467 309 PNADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHN-RIIRPSADY 361
Cdd:cd06099  160 PNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
11-363 2.37e-84

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: 261.82  E-value: 2.37e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLR-----GQSAGETSICTV--------------GKsgtgLTYRGYDIQELADGAQ------FEEVAYLLLKGELPDEQQ 65
Cdd:cd06113    2 GLRnedgtGVLAGLTNISDVvgykiidgekvpcpGK----LYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  66 LEDYKRTLRSLRTLPAALLE-VLERIPAdAHPMDVLRTGCSMLG--DLEPED-GFEHEHEVADRLLAAFPGILLYWY--- 138
Cdd:cd06113   78 LEEFCEILSSYRTLPDNFVEdVILKAPS-KDIMNKLQRSVLALYsyDDKPDDiSLENVLRQSIQLIARLPTIAVYAYqak 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 139 --KFSHDGVRIALDTDEECIGGHFLALL-HQKAPSELERRVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAI 214
Cdd:cd06113  157 rhYYDGESLYIHHPQPELSTAENILSMLrPDKKYTELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 215 GTLRGPLHGGANEAAMAMIE-------PWQDEAQARRELQaKLAAKEK------IMGFGHAVYRTSDPRNVIIKGWSAKL 281
Cdd:cd06113  237 GSLKGPRHGGANIKVMEMLEdikenvkDWTDEDEVRAYLR-KILNKEAfdksglIYGMGHAVYTLSDPRAVVLKKYARSL 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 282 AEAVGDDR----LYRVSCEAEKVMWEEKELF----PNADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREH-N 352
Cdd:cd06113  316 AKEKGREEefalYERIERLAPEVIAEERGIGktvcANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNsG 395
                        410
                 ....*....|.
gi 516389467 353 RIIRPSADYVG 363
Cdd:cd06113  396 RIIRPAYKYVG 406
PRK14032 PRK14032
citrate synthase; Provisional
32-375 5.30e-82

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 257.14  E-value: 5.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQ------FEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLE--VLERIPADAhpMDVL-Rt 102
Cdd:PRK14032  68 LYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRdmILKAPSKDI--MNSLaR- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 103 gcSMLG----DLEPED-GFEHEHEVADRLLAAFPGILLYWY-----KFSHDGVRIALDTDEECIGGHFLALLHQ-KAPSE 171
Cdd:PRK14032 145 --SVLAlysyDDNPDDtSIDNVLRQSISLIARFPTLAVYAYqayrhYHDGKSLYIHPPKPELSTAENILYMLRPdNKYTE 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 172 LERRVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIE-------PWQDEAQAR 243
Cdd:PRK14032 223 LEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEdikenvkDWEDEDEIA 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 244 RELQaKLAAKEK------IMGFGHAVYRTSDPRNVIIKGWSAKLAEAVG---DDRLY-RVSCEAEKVMWEE----KELFP 309
Cdd:PRK14032 303 DYLT-KILNKEAfdksglIYGMGHAVYTISDPRAVILKKFAEKLAKEKGreeEFNLYeKIEKLAPELIAEErgiyKGVSA 381
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516389467 310 NADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQR-EHNRIIRPSADYVGPaPRHFVSLQQR 375
Cdd:PRK14032 382 NVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELvNGGKIIRPAYKSVLE-RREYVPLEER 447
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
26-363 9.04e-82

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: 255.20  E-value: 9.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  26 GKSGTgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLrtgCS 105
Cdd:cd06114   46 GEKGI-LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAIL---SA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 106 MLG--------DLEPEDGfEHEHEVADRLLAAFPGILLYWYKFSHDGVRIALDTDEECIGgHFLALLH-----QKAPSEL 172
Cdd:cd06114  122 MVNalsafypdSLDVNDP-EQRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYVE-NFLHMMFavpyePYEVDPV 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 173 ERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEpwqdEAQARRELQAKLA- 251
Cdd:cd06114  200 VVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLE----EIGSVGNVDKYIAk 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 252 AKEK-----IMGFGHAVYRTSDPRNVIIKGWSAK-LAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYH 320
Cdd:cd06114  276 AKDKndpfrLMGFGHRVYKNYDPRAKILKKTCDEvLAELGKDDPLLEIAMELEEIALKddyfiERKLYPNVDFYSGIILR 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 516389467 321 YMGIPTKLFTPIFVCSRVTGWCAHVMEQRE--HNRIIRPSADYVG 363
Cdd:cd06114  356 ALGIPTEMFTVLFALGRTPGWIAQWREMHEdpELKIGRPRQLYTG 400
PRK14037 PRK14037
citrate synthase; Provisional
32-375 5.40e-79

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 247.35  E-value: 5.40e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLRTGCSMLGDLE 111
Cdd:PRK14037  28 LRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGLMEAAFAALASID 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 112 PEDGF-EHEHEVADRLLAAFPGILLYWYKfSHDGVRIALDTDEECIGGHFLALLHQKAPSELERRVMHVSLILYAEHEFN 190
Cdd:PRK14037 108 KNFKWkENDKEKAISIIAKMATIVANVYR-RKEGNKPRIPEPSDSFAESFLLASFAREPTAEEIKAMDAALILYTDHEVP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 191 ASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAK-LAAKEKIMGFGHAVYRTSDP 269
Cdd:PRK14037 187 ASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKiINGKKRLMGFGHRVYKTYDP 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 270 RNVIIKGWSAKLAEAVGD-DRLYRVSCEAEKV---MWEEKELFPNADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHV 345
Cdd:PRK14037 267 RAKIFKELAETLIERNSEaKKYFEIAQKLEELgikQFGSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHI 346
                        330       340       350
                 ....*....|....*....|....*....|.
gi 516389467 346 MEQ-REHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PRK14037 347 IEYvEEQHRLIRPRALYVGPEHREYVPIDKR 377
PLN02456 PLN02456
citrate synthase
32-375 2.81e-77

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 245.32  E-value: 2.81e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLRTGCSMLGDLE 111
Cdd:PLN02456  88 LRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 112 PE-------DGFEHEHEVAD----RLLAAFPGILLYWYKFSHDGVRIALDTDEEcIGGHFLALL-----HQKAPSELERR 175
Cdd:PLN02456 168 PDanaylrgQHKYKSWEVRDedivRLIGKLPTLAAAIYRRMYGRGPVIPDNSLD-YAENFLYMLgslgdRSYKPDPRLAR 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 176 VMHVSLILYAEHEFNASTFAAR-VCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAKLAAKE 254
Cdd:PLN02456 247 LLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 255 KIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVM-----WEEKELFPNADFFHASAYHYMGIPTKLF 329
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVAlldeyFKVRKLYPNVDFYSGVLLRALGFPEEFF 406
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 516389467 330 TPIFVCSRVTGWCAHVMEQR--EHNRIIRPSADYVGPAPRHFVSLQQR 375
Cdd:PLN02456 407 TVLFAVSRAAGYLSQWDEALglPDERIMRPKQVYTGEWLRHYCPKAER 454
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
11-363 2.44e-76

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: 240.42  E-value: 2.44e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTV-GKSGTgLTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLER 89
Cdd:cd06107    8 GYLNTAVCESSITYIdGDKGI-LLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  90 IPADAHPMDVLRTGCSMLGDLEPE-------DGFEHEHEVAD----RLLAAFPGILLYWYKFsHDGVRIAL-DTDEECIG 157
Cdd:cd06107   87 FPRDAHPMGILCAGLSALSAFYPEaipahtgDLYQNNPEVRDkqiiRTLAKMPTIAAAAYCH-RIGRPFVYpRANLSYIE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 158 GHFLALLHQKA----PSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMI 233
Cdd:cd06107  166 NFLYMMGYVDQepyePNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKML 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 234 EpwqdEAQARRELQAKLA----AKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----E 304
Cdd:cd06107  246 R----EIGTPENVPAFIErvknGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEdeyfvS 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516389467 305 KELFPNADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQRE--HNRIIRPSADYVG 363
Cdd:cd06107  322 RKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEdpLQRIWRPRQVYTG 382
gltA PRK05614
citrate synthase;
32-363 9.64e-71

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 227.07  E-value: 9.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSlRTLpaaLLEVLERI----PADAHPMDVLrtgCSML 107
Cdd:PRK05614  69 LLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTR-HTM---VHEQLKRFfrgfRRDAHPMAVL---CGVV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 108 G--------DLEPEDgfEHEHEVAD-RLLAAFPGILLYWYKFShdgvrialdtdeecIG-------------GHFLALL- 164
Cdd:PRK05614 142 GalsafyhdSLDIND--PEHREIAAiRLIAKMPTLAAMAYKYS--------------IGqpfvyprndlsyaENFLRMMf 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 165 ----HQKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEA 240
Cdd:PRK05614 206 atpcEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVD 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 241 QArRELQAKLAAKE---KIMGFGHAVYRTSDPRNVIIKGWSAK-LAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNA 311
Cdd:PRK05614 286 NI-PEFIARAKDKNdgfRLMGFGHRVYKNYDPRAKIMRETCHEvLKELGLNDPLLEVAMELEEIALNdeyfiERKLYPNV 364
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516389467 312 DFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQRE--HNRIIRPSADYVG 363
Cdd:PRK05614 365 DFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSdpEQKIGRPRQLYTG 418
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
32-370 7.29e-70

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: 224.63  E-value: 7.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLRTGCSMLGDLE 111
Cdd:cd06115   49 LRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 112 PE-------DGFEHEHEVAD----RLLAAFPGILLYWYKfSHDGVRIALDTDEECIGGHFLALL-----HQKAPSELERR 175
Cdd:cd06115  129 PEanpalagQDIYKNKQVRDkqivRILGKAPTIAAAAYR-RRAGRPPNLPSQDLSYTENFLYMLdslgeRKYKPNPRLAR 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 176 VMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAKLAAKEK 255
Cdd:cd06115  208 ALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRK 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 256 IMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYHYMGIPTKLFT 330
Cdd:cd06115  288 LSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKDPLIEIAVALEKAALSdeyfvKRKLYPNVDFYSGLIYRAMGFPTDFFP 367
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 516389467 331 PIFVCSRVTGWCAHVMEQREH--NRIIRPSADYVGPAPRHFV 370
Cdd:cd06115  368 VLFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYV 409
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
32-370 4.72e-63

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: 206.22  E-value: 4.72e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLRTGCSMLGDLE 111
Cdd:cd06116   29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 112 PEDGFEHEHEV----ADRLLAAFPGILLYWYKFSHdGVRIALDTDEECIGGHFLALLHQKAPSELE-----RRVMHVSLI 182
Cdd:cd06116  109 PEAKNIGDEEQrnkqIIRLIGKMPTIAAFAYRHRL-GLPYVLPDNDLSYTGNFLSMLFKMTEPKYEpnpvlAKALDVLFI 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 183 LYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAKLAAKEKIMGFGHA 262
Cdd:cd06116  188 LHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGHR 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 263 VYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAEKVMWEE-----KELFPNADFFHASAYHYMGIPTKLFTPIFVCSR 337
Cdd:cd06116  268 VYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDeyfisRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIPR 347
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 516389467 338 VTGWCAHVMEQRE--HNRIIRPSADYVGPAPRHFV 370
Cdd:cd06116  348 TSGWLAQWIEMLRdpEQKIARPRQVYTGPRDRDYV 382
PRK12350 PRK12350
citrate synthase 2; Provisional
11-367 3.75e-61

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 200.58  E-value: 3.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSGTGLTYRGYDIQELADGAQFEEVAYLLLKGE----LPDEQQLEdykrtlrslrtLPAALLEV 86
Cdd:PRK12350   4 GLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRfgpgLPPAEPFP-----------LPVHLGDA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  87 LERIPAdahpmdvlrtgcsMLGDLEPEDGF-----EHEHEVADRLLAAFPGILLYWYKfSHDGVRIALDTDEECIGGH-F 160
Cdd:PRK12350  73 RVDVQA-------------ALAMLAPVWGFrplldIDDLTARLDLARASVMALSAVAQ-SARGIGQPAVPQREIDHAAtI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 161 LALLH---QKAPSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQ 237
Cdd:PRK12350 139 LERFMgrwRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 238 DEAQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAvgddrLYRVSCEAEKVMWEE-KELFP------N 310
Cdd:PRK12350 219 RTGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGAP-----RYEVAEAVEQAALAElRERRPdrpletN 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516389467 311 ADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRPSADYVGPAPR 367
Cdd:PRK12350 294 VEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPAPR 350
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
32-369 1.31e-60

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: 200.78  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467   32 LTYRGYDIQELADGAQFEEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLrtgCSMLGDLE 111
Cdd:TIGR01798  56 LLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVM---VGVVGALS 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  112 P--EDGF-----EHEHEVADRLLAAFPGILLYWYKFSHdGVRIALDTDEECIGGHFLALL-----HQKAPSELERRVMHV 179
Cdd:TIGR01798 133 AfyHDALdindpRHREISAIRLIAKIPTLAAMSYKYSI-GQPFVYPRNNLSYAENFLHMMfatpcEDYKVNPVLARAMDR 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  180 SLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARrELQAKLAAKE---KI 256
Cdd:TIGR01798 212 IFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNID-EFIKKVKDKNdpfRL 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  257 MGFGHAVYRTSDPRNVIIKGWSAKLAEAVG--DDRLYRVSCEAEKVMWE-----EKELFPNADFFHASAYHYMGIPTKLF 329
Cdd:TIGR01798 291 MGFGHRVYKNYDPRAKVMRETCHEVLKELGlhDDPLFKLAMELEKIALNdpyfiERKLYPNVDFYSGIILKAMGIPTSMF 370
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 516389467  330 TPIFVCSRVTGWCAHVMEQREHN--RIIRPSADYVGPAPRHF 369
Cdd:TIGR01798 371 TVIFALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
19-363 5.25e-41

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 145.87  E-value: 5.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  19 ETSICTVgkSGTGLTYRGYDIQELADGAQFEEVAYLLLKGELPdeqqledykrtlrslrtlpAALLevleRIPADAhpmd 98
Cdd:cd06102   22 ESAITLI--TEGRLFYRGRDAVELAETATLEEVAALLWDGDEA-------------------ARLL----RLLAAA---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  99 vlrtgcsMLGDlEPEDGFEHEhevadRLLAAFpgillywykfshdgvriALDTDEEcigghflallhqkapsELERRVmh 178
Cdd:cd06102   73 -------LLGA-APSDAPVHR-----RLARAW-----------------GLDPAAA----------------DLLRRA-- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 179 vsLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEAQARRELQAKLAAKEKIMG 258
Cdd:cd06102  105 --LVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRGEALPG 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 259 FGHAVYRTSDPRNVIIkgWSAKLAEAVGDDRLYRvscEAEKVMWEEKELFPNADFFHASAYHYMGIPTKLFTPIFVCSRV 338
Cdd:cd06102  183 FGHPLYPDGDPRAAAL--LAALRPLGPAAPPAAR---ALIEAARALTGARPNIDFALAALTRALGLPAGAAFALFALGRS 257
                        330       340
                 ....*....|....*....|....*
gi 516389467 339 TGWCAHVMEQREHNRIIRPSADYVG 363
Cdd:cd06102  258 AGWIAHALEQRAQGKLIRPRARYVG 282
PRK09569 PRK09569
citrate (Si)-synthase;
11-357 1.37e-36

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 137.57  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSAGETSICTVGKSgTGLTYRGYDIQEL------ADGAQF---EEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPA 81
Cdd:PRK09569  41 GARDIRSLVTDISYLDPQ-EGIRFRGKTIPETfealpkAPGSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQ 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  82 ALLEVLERIPADAHPMDVLRTGCSML------------GDLEPEDGFEHEHEVADRLLAAFPGILLYWYKFSH-DGVRIA 148
Cdd:PRK09569 120 YVIDAIRALPRDSHPMVMLSVGILAMqreskfakfyneGKFNKMDAWEYMYEDASDLVARIPVIAAYIYNLKYkGDKQIP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 149 LDTDEECiGGHFLALLHQKAPSElerRVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANE 227
Cdd:PRK09569 200 SDPELDY-GANFAHMIGQPKPYK---DVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQ 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 228 AAMAMIEPWQDE--------AQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLaeaVGDDRLYRVSC---- 295
Cdd:PRK09569 276 EVLGWIQQFQEKlggeeptkEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKH---LPDDPLFKLVAmife 352
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516389467 296 EAEKVMWEE---KELFPNADFFHASAYHYMGIPT-KLFTPIFVCSRVTGwcahVMEQREHNR-----IIRP 357
Cdd:PRK09569 353 VAPGVLTEHgktKNPWPNVDAQSGVIQWYYGVKEwDFYTVLFGVGRALG----VMANITWDRglgyaIERP 419
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
11-348 2.94e-29

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: 117.02  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  11 GLRGQSA--GETSICtvgKSGTGLTYRGYDIQEL------ADGAQF---EEVAYLLLKGELPDEQQLEDYKRTLRSLRTL 79
Cdd:cd06103   39 GMRGMKGlvYETSVL---DPDEGIRFRGKTIPECqellpkADGGGEplpEGLFWLLLTGEVPTEEQVDELSKEWAKRAEV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  80 PAALLEVLERIPADAHPMDVLRTGCSML------------GDLEPEDGFEHEHEVADRLLAAFPGILLYWY--KFSHDGV 145
Cdd:cd06103  116 PSHVVKMIDNLPRNLHPMTQLSAAILALqseskfakayaeGKINKTTYWEYVYEDAMDLIAKLPVVAAKIYrrKYRKGGE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 146 RIALDTDEECiGGHFLALLHQKAPSELErrVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGG 224
Cdd:cd06103  196 IGAIDSKLDW-SANFAHMLGYEDEEFTD--LMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGL 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 225 ANEAAMAMIEPWQDEA-------QARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKlaeAVGDDRLYRVSCEA 297
Cdd:cd06103  273 ANQEVLKWLLKMQKELgkdvsdeELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALK---HLPDDPLFKLVAQC 349
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516389467 298 EKVMWEE-------KELFPNADFFHASAYHYMGIP-TKLFTPIFVCSRVTGwcahVMEQ 348
Cdd:cd06103  350 YKIIPGVlkehgkvKNPYPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALG----VLAQ 404
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
31-340 1.67e-22

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: 97.96  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  31 GLTYRGYDIQEL-------ADGAQF--EEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLR 101
Cdd:cd06106   58 GIRFHGKTIPECqkelpkaPIGGEMlpESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 102 TGCSMLGD-----------LEPEDGFEHEHEVADRLLAAFPGILLYWYKFSHDGV--RIALDTDEEcIGGHFLALLhQKA 168
Cdd:cd06106  138 IGVAALNHdskfaaayekgIKKTEYWEPTLEDSLNLIARLPALAARIYRNVYGEGhgLGKIDPEVD-WSYNFTSML-GYG 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 169 PSELERRVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEA------- 240
Cdd:cd06106  216 DNLDFVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIgskatdq 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 241 QARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRVSCEAE---KVMWEE---KELFPNADff 314
Cdd:cd06106  296 DIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPELENDPVVQLVQKLSEiapGVLTEHgktKNPFPNVD-- 373
                        330       340
                 ....*....|....*....|....*....
gi 516389467 315 HASA---YHYMGIPTKLFTPIFVCSRVTG 340
Cdd:cd06106  374 AASGvlfYHYGIREFLYYTVIFGVSRALG 402
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
31-270 2.96e-21

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: 94.36  E-value: 2.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467  31 GLTYRGYDIQEL------ADGAQF---EEVAYLLLKGELPDEQQLEDYKRTLRSLRTLPAALLEVLERIPADAHPMDVLR 101
Cdd:cd06105   58 GIRFRGLSIPECqkllpkAPGGEEplpEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 102 TGCSMLgdlEPEDGF--------------EHEHEVADRLLAAFPGILLYWYKFSH-DGVRIALDTDEEcIGGHFLALLHQ 166
Cdd:cd06105  138 AAITAL---NSESKFakayaegihkskywEYVYEDSMDLIAKLPCVAAKIYRNLYrGGKIIAIDSNLD-WSANFANMLGY 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 167 KAPSELErrVMHVSLILYAEHEF-NASTFAARVCASTLSDMFSCVTAAIGTLRGPLHGGANEAAMAMIEPWQDEA----- 240
Cdd:cd06105  214 TDPQFTE--LMRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVgkdvs 291
                        250       260       270
                 ....*....|....*....|....*....|..
gi 516389467 241 --QARRELQAKLAAKEKIMGFGHAVYRTSDPR 270
Cdd:cd06105  292 deQLREYVWKTLNSGRVVPGYGHAVLRKTDPR 323
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
156-357 1.56e-19

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: 86.47  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 156 IGGHFLALLHQKAPSELERRVMHVSLILYAEH-EFNASTFAARVCAST-LSDMFSCVTAAIGTLrGPLHGGANEAAMAMI 233
Cdd:cd06100   13 FGDVLYLLLKGRLPTPYEARLLEALLVALADHgPATPSAHAARLTASAgPEDLQSAVAAGLLGI-GDRFGGAGEGAARLF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 234 -----EPWQDEAQARRELQAKLAAKEKIMGFGHAVYRTSDPRNVIIKGWSAKLAEAVGDDRLYRvscEAEKVMWEEKE-- 306
Cdd:cd06100   92 keavdSGDALDAAAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPAGPHLDYAL---AVEKALTAAKGkp 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516389467 307 LFPNADFFHASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREHNRIIRP 357
Cdd:cd06100  169 LPLNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYR 219
PRK06224 PRK06224
citryl-CoA lyase;
169-369 9.05e-19

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 84.92  E-value: 9.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 169 PSELERRVMHVSLILYAEHEFNASTFAARVCASTLSDMFSCVTAAIGTLrGPLHGGANEAAMAM---IEPWQD-----EA 240
Cdd:PRK06224  50 PTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELlqeIAAAADagadlDA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516389467 241 QARRELQAKLAAKEKIMGFGHAVYRTSDPRnviikgwSAKLAEAVGDDRLYRVSCEA----EKVMWEE--KELFPNADFF 314
Cdd:PRK06224 129 AARAIVAEYRAAGKRVPGFGHPLHKPVDPR-------APRLLALAREAGVAGRHCRLaealEAALAAAkgKPLPLNVDGA 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516389467 315 HASAYHYMGIPTKLFTPIFVCSRVTGWCAHVMEQREH---NRIIRPSAD---YVGPAPRHF 369
Cdd:PRK06224 202 IAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQpigFRIWDPAEEaveYTGPPPREL 262
 
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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