|
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: 776.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 1 MAEAKVLSGAGLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLP 80
Cdd:PRK12351 1 MAAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 81 QALKEVLERIPADAHPMDVMRTGCSFLGNIEPEKD---FSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVSDEPSIG 157
Cdd:PRK12351 81 AAVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEdhnFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 158 GHFLHLLHGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFS 237
Cdd:PRK12351 161 GHFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 238 SPQAAVEGTLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHAS 317
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 520814243 318 AYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 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: 702.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 10 AGLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:cd06108 1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEPEKDFSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVSDEPSIGGHFLHLLHGKTP 169
Cdd:cd06108 81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHGKKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 170 SELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGM 249
Cdd:cd06108 161 GELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLLEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 250 LERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTKLF 329
Cdd:cd06108 241 LERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPTELF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 520814243 330 TPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPI 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: 563.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:COG0372 16 GLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFLDGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPE---KDFSAQHDVTDRLLAAFPAIMCYWYRFSHDaKRIDCVSDEPSIGGHFLHLLHGK 167
Cdd:COG0372 96 PRDAHPMDVLRTAVSALGAFDPDaddIDPEARLEKAIRLIAKLPTIAAYAYRYRRG-LPPVYPDPDLSYAENFLYMLFGE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 168 TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTL 247
Cdd:COG0372 175 EPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEYIR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAYHFM 322
Cdd:COG0372 255 KALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSGIVYHAL 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 520814243 323 GIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 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: 557.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 10 AGLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:TIGR01800 1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEPEK---DFSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDcVSDEPSIGGHFLHLLHG 166
Cdd:TIGR01800 81 LPAESHPMDVLRTAVSYLGALDPEKfghTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIA-PKDDDSIAGNFLYMLHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 167 KTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGT 246
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 247 LGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPT 326
Cdd:TIGR01800 240 RKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 520814243 327 KLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 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 |
0e+00 |
|
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: 526.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 12 LRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIP 91
Cdd:cd06117 3 LSGVAAGNTALCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 92 ADAHPMDVMRTGCSFLGNIEPEKD---FSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVSDEPSIGGHFLHLLHGKT 168
Cdd:cd06117 83 AAAHPMDVMRTGVSVLGCVLPEKEdhpVSGARDIADRLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLHGEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 169 PSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLG 248
Cdd:cd06117 163 PSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 249 MLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTKL 328
Cdd:cd06117 243 RVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPTAM 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 520814243 329 FTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPI 372
Cdd:cd06117 323 FTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
11-358 |
1.12e-169 |
|
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: 477.38 E-value: 1.12e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPE----KDFSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDcVSDEPSIGGHFLHLLHG 166
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEaisdKADYWENALRDDLIAKLPTIAAYIYRHRRGLPPIY-PDPDLSYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 167 KTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGT 246
Cdd:pfam00285 160 YEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 247 LGMLER-KDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAYH 320
Cdd:pfam00285 240 RKVLNKgKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEdlyfvEKNLYPNVDFYSGVLYH 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 520814243 321 FMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPS 358
Cdd:pfam00285 320 ALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
11-363 |
1.40e-152 |
|
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: 434.01 E-value: 1.40e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:cd06110 2 GLEGVIAADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPEKD---FSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDcVSDEPSIGGHFLHLLHGK 167
Cdd:cd06110 82 PKDAHPMDVLRTAVSALALYDPEADdmsREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVA-PDPDLSHAANFLYMLTGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 168 TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTL 247
Cdd:cd06110 161 KPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTK 327
Cdd:cd06110 241 DKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIPVD 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 520814243 328 LFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIG 363
Cdd:cd06110 321 LFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
11-361 |
8.02e-150 |
|
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: 427.02 E-value: 8.02e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTV-GQAGaGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:cd06118 2 GLEGVKAKETSISYIdGDEG-ILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEPEKD---FSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVSDEpSIGGHFLHLLHG 166
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFARdksPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDL-SYAENFLYMLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 167 KTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGT 246
Cdd:cd06118 160 EEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 247 LGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQ---KKLFPNADFYHASAYHFMG 323
Cdd:cd06118 240 WKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVlgeKGIYPNVDFYSGVVYKALG 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 520814243 324 IPTKLFTPIFVCSRLTGWAAHVFEQRANN-RIIRPSAEY 361
Cdd:cd06118 320 FPTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
11-372 |
2.75e-147 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 421.28 E-value: 2.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:PRK14033 12 GLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPE-KDFSAQHDVTD--RLLAAFPAIMCYWYRFSHDAKRIDCVSDEpSIGGHFLHLLHGK 167
Cdd:PRK14033 92 PTTCHPMDVVRTAVSYLGAEDPEaDDSSPEANLAKalRLFAVLPTIVAADQRRRRGLDPIAPRSDL-GYAENFLHMCFGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 168 TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTL 247
Cdd:PRK14033 171 VPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTK 327
Cdd:PRK14033 251 DALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMGFDID 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 520814243 328 LFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPI 372
Cdd:PRK14033 331 FFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVPPI 375
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
11-368 |
5.16e-140 |
|
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: 402.56 E-value: 5.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:cd06111 2 GLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPE-KDFSAQH--DVTDRLLAAFPAIMCYWYRFSHdAKRIDCVSDEPSIGGHFLHLLHGK 167
Cdd:cd06111 82 PKNCHPMDVLRTAVSVLGAEDSEtDDSSPDAnlAKAIRLLAQLPTVVAADIRRRK-GLDPIPPDSDLGIAENFLHMCFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 168 TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTL 247
Cdd:cd06111 161 VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTK 327
Cdd:cd06111 241 DALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDID 320
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 520814243 328 LFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRK 368
Cdd:cd06111 321 FFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPEQRP 361
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
11-375 |
2.27e-126 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 367.93 E-value: 2.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVgqAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDL-PQALKEVLER 89
Cdd:PRK14035 6 GLEGVIAAETKISSI--IDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLnDRVYQHFEEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEP---EKDFSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVSDEpSIGGHFLHLLHG 166
Cdd:PRK14035 84 STDHVHPMTALRTSVSYLAHFDPdaeEESDEARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDL-SYAANFLYMLRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 167 KTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSpQAAVEGT 246
Cdd:PRK14035 163 ELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRS-IGDVDAY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 247 LG-MLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIP 325
Cdd:PRK14035 242 LDeKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGIP 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 520814243 326 TKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:PRK14035 322 HDLFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
11-375 |
3.53e-118 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 347.14 E-value: 3.53e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVgqAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:PRK14034 6 GLEGVVATTSSVSSI--IDDTLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PAD-AHPMDVMRTGCSFLGNIEPEKDF---SAQHDVTDRLLAAFPAIMCywyRFSHDAKRIDCVS--DEPSIGGHFLHLL 164
Cdd:PRK14034 84 DLKkVHPMSVLRTAISMLGLYDEEAEImdeEANYRKAVRLQAKVPTIVA---AFSRIRKGLDPVEprKDLSLAANFLYML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 165 HGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVE 244
Cdd:PRK14034 161 NGEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 245 GTLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGI 324
Cdd:PRK14034 241 YIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 520814243 325 PTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:PRK14034 321 DHDLFTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
11-372 |
4.31e-115 |
|
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: 339.40 E-value: 4.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTV-GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:cd06112 4 GLAGVPAAESSISYIdGKNGI-LEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEPEKDFSA-----QHDVTDRLLAAFPAIMCYWYRFSHDAKRIDcVSDEPSIGGHFLHLL 164
Cdd:cd06112 83 FPETGHPMDMLQATVAALGMFYPKPEVLKpnpdyIDAATVKLIAKMPTLVAMWARIRNGDDPIE-PRPDLDYAENFLYML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 165 HGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVE 244
Cdd:cd06112 162 FGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVKA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 245 GTLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGD-TVLFPVSEAIDKTMWE---QKKLFPNADFYHASAYH 320
Cdd:cd06112 242 YLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCEEllgHKGVYPNVDFYSGIVYK 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 520814243 321 FMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPI 372
Cdd:cd06112 322 ELGIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYVPL 373
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
11-363 |
1.87e-113 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 335.15 E-value: 1.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERI 90
Cdd:PRK12349 8 GLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 PADAHPMDVMRTGCSFLGNIEPEKD---FSAQHDVTDRLLAAFPAIMCYWYRFSHDAKRIDCVsDEPSIGGHFLHLLHGK 167
Cdd:PRK12349 88 PKETHPMDGLRTGVSALAGYDNDIEdrsLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPL-KELSYSANFLYMLTGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 168 TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSpqaaVEGTL 247
Cdd:PRK12349 167 KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGT----VEKFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLE----RKDKIMGFGHAIY-KDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFM 322
Cdd:PRK12349 243 ELLQkklyNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEKIMEKEKGLYPNLDYYAAPVYWML 322
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 520814243 323 GIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIG 363
Cdd:PRK12349 323 GIPIQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIG 363
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
11-375 |
6.02e-108 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 321.52 E-value: 6.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTV-GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:PRK14036 7 GLEGVPATQSSISYVdGQKGI-LEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IPADAHPMDVMRTGCSFLGNIEPEKDFSAQ---HDVTDRLLAAFPAIMCYWYRFShdaKRIDCV--SDEPSIGGHFLHLL 164
Cdd:PRK14036 86 FPETGHPMDALQASAAALGLFYSRRALDDPeyiRDAVVRLIAKIPTMVAAFQLIR---KGNDPIqpRDDLDYAANFLYML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 165 HGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVE 244
Cdd:PRK14036 163 TEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSVENVRP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 245 GTLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE---QKKLFPNADFYHASAYHF 321
Cdd:PRK14036 243 YLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVAEErlgPKGIYPNVDFYSGLVYRK 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 520814243 322 MGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:PRK14036 323 LGIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
20-375 |
7.20e-102 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 305.78 E-value: 7.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 20 TALSTV-GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMD 98
Cdd:NF041157 15 TSLTYIdGEKGI-LRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 99 VMRTGCSFLGNIEPEKdfsaQHDVTDR-----LLAAFPAIMCYWYRfshdAKR-IDCVSDEPSiGGH---FLHLLHGKTP 169
Cdd:NF041157 94 MMETAFSALASIENYK----WNKENDRekalkIIGKASTIVANVYR----HKEgLKPRIPEPS-ESYaesFLRATFGRKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 170 SELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPqAAVEGTL-- 247
Cdd:NF041157 165 SEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSP-DNVEKWFne 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 248 GMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDK---TMWEQKKLFPNADFYHASAYHFMGI 324
Cdd:NF041157 244 NIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEElgiKHFGSKGIYPNTDFYSGIVFYSLGF 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 520814243 325 PTKLFTPIFVCSRLTGWAAHVFEQRAN-NRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:NF041157 324 PVYMFTSLFALSRVLGWLAHIIEYVEEqHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
11-363 |
8.85e-99 |
|
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: 296.91 E-value: 8.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTV-GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLER 89
Cdd:cd06109 2 GLEGVVAAETVLSDVdGEAGR-LIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 90 IpADAHPMDVMRTGCSFLGniepekdfsAQHDVTD--RLLAAFPAIMCYWYRFShdaKRIDCVSDEPSIG--GHFLHLLH 165
Cdd:cd06109 81 L-AGLDPMDALRALLALLP---------DSPDLATalRLLAAAPVITAALLRLS---RGKQPIAPDPSLShaADYLRMLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 166 GKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEG 245
Cdd:cd06109 148 GEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 246 TLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLAdevGDTVLFPVSEAIDKTMWE-------QKKLFPNADFYHASA 318
Cdd:cd06109 228 LREALARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEQAALAllreykpGRPLETNVEFYTALL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 520814243 319 YHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIG 363
Cdd:cd06109 305 LEALGLPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
11-361 |
7.46e-97 |
|
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: 288.83 E-value: 7.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPtqaqlaayqaklgklrdlpqalkevleri 90
Cdd:cd06101 2 GLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 91 padahpmdvmrtgcsflgniepekdfsaqhdvtdrllaafpaimcywyrfshdakridcvsdepSIGGHFLHLLHGKTPS 170
Cdd:cd06101 53 ----------------------------------------------------------------SYAENFLYMLGGEEPD 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 171 ELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQA--AVEGTLG 248
Cdd:cd06101 69 PEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKNepAEAYIRK 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 249 MLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE---QKKLFPNADFYHASAYHFMGIP 325
Cdd:cd06101 149 KLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEvlyEKKLYPNVDFYSGVLYKAMGFP 228
|
330 340 350
....*....|....*....|....*....|....*..
gi 520814243 326 TKLFTPIFVCSRLTGWAAHVFEQRANN-RIIRPSAEY 361
Cdd:cd06101 229 TELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
26-363 |
1.42e-88 |
|
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: 272.53 E-value: 1.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 26 GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMRTGCS 105
Cdd:cd06114 46 GEKGI-LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 106 FLGNIEPE----KDFSAQHDVTDRLLAAFPAIMCYWYRFSHDAK----RIDCvsdepSIGGHFLHLLHGkTPSE------ 171
Cdd:cd06114 125 ALSAFYPDsldvNDPEQRELAAIRLIAKVPTIAAMAYRYSIGQPfiypDNDL-----SYVENFLHMMFA-VPYEpyevdp 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 172 LHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSpqaaVEGTLGMLE 251
Cdd:cd06114 199 VVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGS----VGNVDKYIA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 252 R-KDK-----IMGFGHAIYKDNDPRNEVIKGWSKKLADEVG-DTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAY 319
Cdd:cd06114 275 KaKDKndpfrLMGFGHRVYKNYDPRAKILKKTCDEVLAELGkDDPLLEIAMELEEIALKddyfiERKLYPNVDFYSGIIL 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 520814243 320 HFMGIPTKLFTPIFVCSRLTGWAAHVFEQRAN--NRIIRPSAEYIG 363
Cdd:cd06114 355 RALGIPTEMFTVLFALGRTPGWIAQWREMHEDpeLKIGRPRQLYTG 400
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
155-361 |
1.08e-87 |
|
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: 263.81 E-value: 1.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 155 SIGGHFLHLLHGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIE 234
Cdd:cd06099 1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 235 RFSSPQA--AVEGTLGMLERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE---QKKLFP 309
Cdd:cd06099 81 EIGTPKNepAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEvlyEKKLYP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520814243 310 NADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANN-RIIRPSAEY 361
Cdd:cd06099 161 NVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
20-375 |
1.92e-83 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 258.52 E-value: 1.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 20 TALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDV 99
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 100 MRTGCSFLGNIEPEKDFSAQH-DVTDRLLAAFPAIMCYWYRFSHDAK-RIDCVSDepSIGGHFLHLLHGKTPSELHVKVM 177
Cdd:PRK14037 96 MEAAFAALASIDKNFKWKENDkEKAISIIAKMATIVANVYRRKEGNKpRIPEPSD--SFAESFLLASFAREPTAEEIKAM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 178 NVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPqAAVEGTL--GMLERKDK 255
Cdd:PRK14037 174 DAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDP-NNVEMWFndKIINGKKR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 256 IMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDT-VLFPVSEAIDKTMWEQ---KKLFPNADFYHASAYHFMGIPTKLFTP 331
Cdd:PRK14037 253 LMGFGHRVYKTYDPRAKIFKELAETLIERNSEAkKYFEIAQKLEELGIKQfgsKGIYPNTDFYSGIVFYALGFPVYMFTA 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 520814243 332 IFVCSRLTGWAAHVFEQRAN-NRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:PRK14037 333 LFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
32-375 |
8.98e-83 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 259.57 E-value: 8.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMRTGCSFLGNIE 111
Cdd:PLN02456 88 LRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 112 PEK-------DFSAQHDVTD----RLLAAFPAIMCYWYRfsHDAKRIDCV-SDEPSIGGHFLHLLHG-----KTPSELHV 174
Cdd:PLN02456 168 PDAnaylrgqHKYKSWEVRDedivRLIGKLPTLAAAIYR--RMYGRGPVIpDNSLDYAENFLYMLGSlgdrsYKPDPRLA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 175 KVMNVSLILYAEHEFNASTFTAR-VCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGMLERK 253
Cdd:PLN02456 246 RLLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 254 DKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTM-----WEQKKLFPNADFYHASAYHFMGIPTKL 328
Cdd:PLN02456 326 KVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVAlldeyFKVRKLYPNVDFYSGVLLRALGFPEEF 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 520814243 329 FTPIFVCSRLTGWAAHVFEQR--ANNRIIRPSAEYIGVEQRKFVPIERR 375
Cdd:PLN02456 406 FTVLFAVSRAAGYLSQWDEALglPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
32-363 |
7.97e-81 |
|
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: 251.97 E-value: 7.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMRTGCSFLGNIE 111
Cdd:cd06107 29 LLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRDAHPMGILCAGLSALSAFY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 112 PE-------KDFSAQHDVTD----RLLAAFPAI--MCYWYRfshdaKRIDCVSDEP--SIGGHFLHLLH------GKtPS 170
Cdd:cd06107 109 PEaipahtgDLYQNNPEVRDkqiiRTLAKMPTIaaAAYCHR-----IGRPFVYPRAnlSYIENFLYMMGyvdqepYE-PN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 171 ELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGML 250
Cdd:cd06107 183 PRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREIGTPENVPAFIERVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 251 ERKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAYHFMGIP 325
Cdd:cd06107 263 NGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEdeyfvSRKLYPNVDFYSGFIYKALGFP 342
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 520814243 326 TKLFTPIFVCSRLTGWAAHVFEQ--RANNRIIRPSAEYIG 363
Cdd:cd06107 343 PEFFTVLFAVARTSGWMAHWREMmeDPLQRIWRPRQVYTG 382
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
32-375 |
5.49e-80 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 252.13 E-value: 5.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQ------FEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQalkEVLERIPADAHPMDVM----R 101
Cdd:PRK14032 68 LYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPD---GFTRDMILKAPSKDIMnslaR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 102 TGCSfLGNIEPEKDFSAQHDVTD---RLLAAFPAIMCYWY---RFSHDAKR--IDCVSDEPSIGGHFLHLLHGKTP-SEL 172
Cdd:PRK14032 145 SVLA-LYSYDDNPDDTSIDNVLRqsiSLIARFPTLAVYAYqayRHYHDGKSlyIHPPKPELSTAENILYMLRPDNKyTEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 173 HVKVMNVSLILYAEHEF-NASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFS------SPQAAVEG 245
Cdd:PRK14032 224 EARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIKenvkdwEDEDEIAD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 246 TL-GMLERK--DK---IMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDK----TMWEQKKLF----PNA 311
Cdd:PRK14032 304 YLtKILNKEafDKsglIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEKlapeLIAEERGIYkgvsANV 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520814243 312 DFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRAN-NRIIRPSAEYIgVEQRKFVPIERR 375
Cdd:PRK14032 384 DFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNgGKIIRPAYKSV-LERREYVPLEER 447
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
32-363 |
8.36e-79 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) 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: 247.57 E-value: 8.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQ------FEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQA-LKEVLERIPAdAHPMDVMRTGC 104
Cdd:cd06113 38 LYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNfVEDVILKAPS-KDIMNKLQRSV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 105 SFLGNIEPE-KDFSAQH--DVTDRLLAAFPAIMCYWYRfshdAKR---------IDCVSDEPSIGGHFLHLL-HGKTPSE 171
Cdd:cd06113 117 LALYSYDDKpDDISLENvlRQSIQLIARLPTIAVYAYQ----AKRhyydgeslyIHHPQPELSTAENILSMLrPDKKYTE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 172 LHVKVMNVSLILYAEHEF-NASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIE------RFSSPQAAVE 244
Cdd:cd06113 193 LEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEdikenvKDWTDEDEVR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 245 GTLGMLERK---DK---IMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAID----KTMWEQKKLF----PN 310
Cdd:cd06113 273 AYLRKILNKeafDKsglIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERIErlapEVIAEERGIGktvcAN 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 520814243 311 ADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRAN-NRIIRPSAEYIG 363
Cdd:cd06113 353 VDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNsGRIIRPAYKYVG 406
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
32-371 |
2.20e-76 |
|
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: 241.58 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMRTGCSFLGNIE 111
Cdd:cd06115 49 LRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 112 PEKDFS-AQHDVTD----------RLLAAFPAIMCYWYRFSHDAKRIDCVSDEPSIGgHFLHLLHG-----KTPSELHVK 175
Cdd:cd06115 129 PEANPAlAGQDIYKnkqvrdkqivRILGKAPTIAAAAYRRRAGRPPNLPSQDLSYTE-NFLYMLDSlgerkYKPNPRLAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 176 VMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGMLERKDK 255
Cdd:cd06115 208 ALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 256 IMGFGHAIYKDNDPRNEVIkgwsKKLADEV----GDTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAYHFMGIPT 326
Cdd:cd06115 288 LSGFGHRVYKNYDPRAKII----KKLADEVfeivGKDPLIEIAVALEKAALSdeyfvKRKLYPNVDFYSGLIYRAMGFPT 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 520814243 327 KLFTPIFVCSRLTGWAAHVFEQRAN--NRIIRPSAEYIGVEQRKFVP 371
Cdd:cd06115 364 DFFPVLFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYVP 410
|
|
| gltA |
PRK05614 |
citrate synthase; |
26-363 |
1.81e-74 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 236.70 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 26 GQAGAgLTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMrtgCS 105
Cdd:PRK05614 64 GDKGI-LLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVL---CG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 106 FLGNIepekdfSA-QHDVTD------------RLLAAFPAI--MCYWYrfshdakridcvsdepSIG------------- 157
Cdd:PRK05614 140 VVGAL------SAfYHDSLDindpehreiaaiRLIAKMPTLaaMAYKY----------------SIGqpfvyprndlsya 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 158 GHFLHLLHGkTPSE------LHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAME 231
Cdd:PRK05614 198 ENFLRMMFA-TPCEeyevnpVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 232 MIERFSSpqaaVEGTLGMLER-KDK-----IMGFGHAIYKDNDPRNEVIkgwsKKLADEV-----GDTVLFPVSEAIDKT 300
Cdd:PRK05614 277 MLEEIGS----VDNIPEFIARaKDKndgfrLMGFGHRVYKNYDPRAKIM----RETCHEVlkelgLNDPLLEVAMELEEI 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 301 MWE-----QKKLFPNADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRAN--NRIIRPSAEYIG 363
Cdd:PRK05614 349 ALNdeyfiERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWNEMHSDpeQKIGRPRQLYTG 418
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
32-372 |
1.75e-65 |
|
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: 212.77 E-value: 1.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMRTGCSFLGNIE 111
Cdd:cd06116 29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 112 PEK----DFSAQHDVTDRLLAAFPAIMCYWYRfsHDAKRIDCVSD-EPSIGGHFLHLLHGKT-----PSELHVKVMNVSL 181
Cdd:cd06116 109 PEAknigDEEQRNKQIIRLIGKMPTIAAFAYR--HRLGLPYVLPDnDLSYTGNFLSMLFKMTepkyePNPVLAKALDVLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 182 ILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGMLERKDKIMGFGH 261
Cdd:cd06116 187 ILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGH 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 262 AIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWE-----QKKLFPNADFYHASAYHFMGIPTKLFTPIFVCS 336
Cdd:cd06116 267 RVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEdeyfiSRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIP 346
|
330 340 350
....*....|....*....|....*....|....*...
gi 520814243 337 RLTGWAAHVFE--QRANNRIIRPSAEYIGVEQRKFVPI 372
Cdd:cd06116 347 RTSGWLAQWIEmlRDPEQKIARPRQVYTGPRDRDYVPI 384
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
32-369 |
7.71e-65 |
|
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: 211.95 E-value: 7.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 32 LTYRGYDVRELAADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMDVMrtgCSFLGNIe 111
Cdd:TIGR01798 56 LLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVM---VGVVGAL- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 112 pekdfSA-QHDVTD------------RLLAAFP--AIMCYWYR----FSHDAKRIdcvsdepSIGGHFLHLLHGkTPSE- 171
Cdd:TIGR01798 132 -----SAfYHDALDindprhreisaiRLIAKIPtlAAMSYKYSigqpFVYPRNNL-------SYAENFLHMMFA-TPCEd 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 172 -----LHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGT 246
Cdd:TIGR01798 199 ykvnpVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 247 LGMLERKD--KIMGFGHAIYKDNDPRNEVIKGWSKKLADEVG--DTVLFPVSEAIDKTMWE-----QKKLFPNADFYHAS 317
Cdd:TIGR01798 279 KKVKDKNDpfRLMGFGHRVYKNYDPRAKVMRETCHEVLKELGlhDDPLFKLAMELEKIALNdpyfiERKLYPNVDFYSGI 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 520814243 318 AYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANN--RIIRPSAEYIGVEQRKF 369
Cdd:TIGR01798 359 ILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
11-368 |
7.65e-63 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 204.81 E-value: 7.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVGQAGAGLTYRGYDVRELAADAQFEEVAYLLL---YGELPTQAQLAAYQAKLGKLR-DLPQALkev 86
Cdd:PRK12350 4 GLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVdgrFGPGLPPAEPFPLPVHLGDARvDVQAAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 87 LERIPADAhpmdvmrtgcsfLGNIEPEKDFSAQhdvtDRLLAAFPAIMCY-------WYRFSHDAKRIDCVSDepsiggh 159
Cdd:PRK12350 81 AMLAPVWG------------FRPLLDIDDLTAR----LDLARASVMALSAvaqsargIGQPAVPQREIDHAAT------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 160 FLHLLHGK---TPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEM---I 233
Cdd:PRK12350 138 ILERFMGRwrgEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMldaV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 234 ERFSSPQAAVEGTLGmleRKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEvgdtvLFPVSEAIDKTMWE---QKK---- 306
Cdd:PRK12350 218 ERTGDARGWVKGALD---RGERLMGFGHRVYRAEDPRARVLRATAKRLGAP-----RYEVAEAVEQAALAelrERRpdrp 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520814243 307 LFPNADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYIGVEQRK 368
Cdd:PRK12350 290 LETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPAPRS 351
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
20-363 |
2.73e-40 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99856 [Multi-domain] Cd Length: 282 Bit Score: 143.94 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 20 TALSTVgqAGAGLTYRGYDVRELAADAQFEEVAYLLLYGELPtqAQLAAYQAKlgklrdlpqalkevleripadahpmdv 99
Cdd:cd06102 23 SAITLI--TEGRLFYRGRDAVELAETATLEEVAALLWDGDEA--ARLLRLLAA--------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 100 mrtgcsFLGNIEPEKDFSAQhdvtdRLLAAfpaimcyWYRFSHDAKRIdcvsdepsigghflhllhgktpselhvkvmNV 179
Cdd:cd06102 72 ------ALLGAAPSDAPVHR-----RLARA-------WGLDPAAADLL------------------------------RR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 180 SLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAAMEMIERFSSPQAAVEGTLGMLERKDKIMGF 259
Cdd:cd06102 104 ALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRGEALPGF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 260 GHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTmweqkKLFPNADFYHASAYHFMGIPTKLFTPIFVCSRLT 339
Cdd:cd06102 184 GHPLYPDGDPRAAALLAALRPLGPAAPPAARALIEAARALT-----GARPNIDFALAALTRALGLPAGAAFALFALGRSA 258
|
330 340
....*....|....*....|....
gi 520814243 340 GWAAHVFEQRANNRIIRPSAEYIG 363
Cdd:cd06102 259 GWIAHALEQRAQGKLIRPRARYVG 282
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
11-357 |
2.07e-35 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 134.49 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVgQAGAGLTYRGYDVREL---------AADAQFEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQ 81
Cdd:PRK09569 41 GARDIRSLVTDISYL-DPQEGIRFRGKTIPETfealpkapgSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 82 ALKEVLERIPADAHPMDVMRTGCSFL------------GNIEPEKDFSAQHDVTDRLLAAFPAIMCYWYRfsHDAKRIDC 149
Cdd:PRK09569 120 YVIDAIRALPRDSHPMVMLSVGILAMqreskfakfyneGKFNKMDAWEYMYEDASDLVARIPVIAAYIYN--LKYKGDKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 150 VSDEPSI--GGHFLHLLHGKTPSElhvKVMNVSLILYAEHEF-NASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGAN 226
Cdd:PRK09569 198 IPSDPELdyGANFAHMIGQPKPYK---DVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 227 EAAMEMIERFSSPQAAVEGTLGMLER--KDK------IMGFGHAIYKDNDPRNEVIKGWSKKL--ADEVGDTV--LFPVS 294
Cdd:PRK09569 275 QEVLGWIQQFQEKLGGEEPTKEQVEQalWDTlnagqvIPGYGHAVLRKTDPRYTAQREFCLKHlpDDPLFKLVamIFEVA 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520814243 295 EAIDKTMWEQKKLFPNADFYHASAYHFMGIPT-KLFTPIFVCSRLTGWAAHVFEQRA-NNRIIRP 357
Cdd:PRK09569 355 PGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEwDFYTVLFGVGRALGVMANITWDRGlGYAIERP 419
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
11-357 |
1.85e-26 |
|
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: 109.31 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGQVAGQTALSTVgQAGAGLTYRGYDVRELAADAQ---------FEEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQ 81
Cdd:cd06103 39 GMRGMKGLVYETSVL-DPDEGIRFRGKTIPECQELLPkadgggeplPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 82 ALKEVLERIPADAHPMDVMRTGCSFLgniEPEKDFSAQH----------------DVTDrLLAAFPAIMCYWYR--FSHD 143
Cdd:cd06103 118 HVVKMIDNLPRNLHPMTQLSAAILAL---QSESKFAKAYaegkinkttyweyvyeDAMD-LIAKLPVVAAKIYRrkYRKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 144 AKRIDCVSDEpSIGGHFLHLLhGKTPSELHvKVMNVSLILYAEHEF-NASTFTARVCASTLSDLYSCVTAAIGSLRGPLH 222
Cdd:cd06103 194 GEIGAIDSKL-DWSANFAHML-GYEDEEFT-DLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 223 GGANEAAMEMIERFSSpQAAVEGTLGMLER--------KDKIMGFGHAIYKDNDPRNEVIKGWSKK-LADEVGDTVLFPV 293
Cdd:cd06103 271 GLANQEVLKWLLKMQK-ELGKDVSDEELEKyiwdtlnsGRVVPGYGHAVLRKTDPRFTCQREFALKhLPDDPLFKLVAQC 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520814243 294 SEAIDKTMWEQKKL---FPNADFYHASAYHFMGIP-TKLFTPIFVCSRLTGWAAHVFEQRANNRII-RP 357
Cdd:cd06103 350 YKIIPGVLKEHGKVknpYPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQLVWSRALGLPIeRP 418
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
49-340 |
1.12e-24 |
|
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: 104.51 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 49 EEVAYLLLYGELPTQAQLAAYQAKLGKLRDLPQALKEVLERIPADAHPMD-------VMRTGCSFLGNIE---PEKDFSA 118
Cdd:cd06106 85 ESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTqlsigvaALNHDSKFAAAYEkgiKKTEYWE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 119 Q--HDVTDrLLAAFPAIMCYWYRFSH-DAKRIDCVSDEPSIGGHFLHLLhGKTPSELHVKVMNVSLILYAEHE-FNASTF 194
Cdd:cd06106 165 PtlEDSLN-LIARLPALAARIYRNVYgEGHGLGKIDPEVDWSYNFTSML-GYGDNLDFVDLLRLYIALHGDHEgGNVSAH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 195 TARVCASTLSDLYSCVTAAIGSLRGPLHGGANEAA----MEMIERFSS---PQAAVEGTLGMLERKDKIMGFGHAIYKDN 267
Cdd:cd06106 243 TTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVlrwiLEMQKNIGSkatDQDIRDYLWKTLKSGRVVPGYGHAVLRKP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 268 DPRNEVIKGWSKKLADEVGDTVLFPV---SEAIDKTMWEQKKL---FPNADFYHASAYHFMGI-PTKLFTPIFVCSRLTG 340
Cdd:cd06106 323 DPRFTALMEFAQTRPELENDPVVQLVqklSEIAPGVLTEHGKTknpFPNVDAASGVLFYHYGIrEFLYYTVIFGVSRALG 402
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
163-369 |
5.07e-22 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 94.17 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 163 LLHGKTPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLYSCVTAAIGSLrGPLHGGANEAAMEMIERF------ 236
Cdd:PRK06224 44 LLRGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELLQEIaaaada 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 237 --SSPQAAVEGTLGMLERKDKIMGFGHAIYKDNDPRNEVIkgwsKKLADEVG-----DTVLFPVSEAIDKTmwEQKKLFP 309
Cdd:PRK06224 123 gaDLDAAARAIVAEYRAAGKRVPGFGHPLHKPVDPRAPRL----LALAREAGvagrhCRLAEALEAALAAA--KGKPLPL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520814243 310 NADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRAN---NRIIRP---SAEYIGVEQRKF 369
Cdd:PRK06224 197 NVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQpigFRIWDPaeeAVEYTGPPPREL 262
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
155-357 |
5.36e-22 |
|
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: 93.02 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 155 SIGGHFLHLLHGKTPSELHVKVMNVSLILYAEH-EFNASTFTARVCAST-LSDLYSCVTAAIGSLrGPLHGGANEAAMEM 232
Cdd:cd06100 12 SFGDVLYLLLKGRLPTPYEARLLEALLVALADHgPATPSAHAARLTASAgPEDLQSAVAAGLLGI-GDRFGGAGEGAARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 233 IERF-----SSPQAAVEGTLGMLERKDKIMGFGHAIYKDNDPRNEVIKgwskKLADEVGD-TVLFPVSEAIDKTMwEQKK 306
Cdd:cd06100 91 FKEAvdsgdALDAAAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLL----ELARELGPaGPHLDYALAVEKAL-TAAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 520814243 307 LFP---NADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRP 357
Cdd:cd06100 166 GKPlplNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYR 219
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
11-270 |
1.64e-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: 95.13 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 11 GLRGqVAGQTALSTVGQAGAGLTYRGYDVREL-----AADAQFEEVA----YLLLYGELPTQAQLAAYQAKLGKLRDLPQ 81
Cdd:cd06105 39 GMRG-IKGLVWETSVLDPEEGIRFRGLSIPECqkllpKAPGGEEPLPeglfWLLLTGEVPTKEQVSALSKEWAARAALPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 82 ALKEVLERIPADAHPMDVMRTGCSFLgniEPEKDFS---------------AQHDVTDrLLAAFPAIMCYWYRFSHDAKR 146
Cdd:cd06105 118 HVVTMLDNFPTNLHPMSQLSAAITAL---NSESKFAkayaegihkskyweyVYEDSMD-LIAKLPCVAAKIYRNLYRGGK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520814243 147 IDCVSDEPSIGGHFLHLLhGKTpSELHVKVMNVSLILYAEHE-FNASTFTARVCASTLSDLYSCVTAAIGSLRGPLHGGA 225
Cdd:cd06105 194 IIAIDSNLDWSANFANML-GYT-DPQFTELMRLYLTIHSDHEgGNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 520814243 226 NEaamEMIERFSSPQAAVEGTLGMLERKDKIM----------GFGHAIYKDNDPR 270
Cdd:cd06105 272 NQ---EVLVWLTKLQKEVGKDVSDEQLREYVWktlnsgrvvpGYGHAVLRKTDPR 323
|
|
| |
