|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
10-386 |
0e+00 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 836.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 10 TGFKPKKSVALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPL 89
Cdd:PRK12351 2 AAFKPKKSVALSGVVAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 90 ALQTALETLPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQTDDDSIGA 169
Cdd:PRK12351 82 AVKTVLEAIPAAAHPMDVMRTGVSVLGCLLPEKEDHNFSGARDIADRLLASLGSILLYWYHYSHNGRRIEVETDDDSIGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 170 HFLHLLHGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYEN 249
Cdd:PRK12351 162 HFLHLLHGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 250 PDQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVS 329
Cdd:PRK12351 242 PDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVS 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 497071235 330 YHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:PRK12351 322 YHMMGVPTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
18-383 |
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: 745.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 18 VALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALET 97
Cdd:cd06117 1 VALSGVAAGNTALCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 98 LPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQTDDDSIGAHFLHLLHG 177
Cdd:cd06117 81 LPAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGARDIADRLMASLGSILLYWYHYSHNGKRIEVETDDDSIGGHFLHLLHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 178 EKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDI 257
Cdd:cd06117 161 EKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPT 337
Cdd:cd06117 241 RRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVPT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497071235 338 AMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPL 383
Cdd:cd06117 321 AMFTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
18-383 |
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: 641.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 18 VALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALET 97
Cdd:cd06108 1 GGLAGVVAGQTAISTVGKGGKGLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 98 LPAHSHPMDVMRTAVSVLGCVLPEKDDhnlPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQTDDDSIGAHFLHLLHG 177
Cdd:cd06108 81 IPKDSHPMDVMRTGCSMLGCLEPENEF---SQQYEIAIRLLAIFPSILLYWYHYSHSGKRIETETDEDSIAGHFLHLLHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 178 EKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDI 257
Cdd:cd06108 158 KKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPT 337
Cdd:cd06108 238 LEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPT 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497071235 338 AMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPL 383
Cdd:cd06108 318 ELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
18-386 |
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: 566.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 18 VALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALET 97
Cdd:TIGR01800 1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 98 LPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQtDDDSIGAHFLHLLHG 177
Cdd:TIGR01800 81 LPAESHPMDVLRTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPK-DDDSIAGNFLYMLHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 178 EKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDI 257
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPT 337
Cdd:TIGR01800 240 RKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497071235 338 AMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:TIGR01800 320 DLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
1-386 |
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: 563.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 1 MSSTENTPStgfKPKKSVALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQK 80
Cdd:COG0372 1 MSSEIDIRA---KFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 81 LKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHnGEMIDV 160
Cdd:COG0372 78 LARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADDIDPEARLEKAIRLIAKLPTIAAYAYRYRR-GLPPVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 161 QTDDDSIGAHFLHLLHGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVA 240
Cdd:COG0372 157 PDPDLSYAENFLYMLFGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 241 FEIQKRYENPDQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWE-----V 315
Cdd:COG0372 237 LEMLEEIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497071235 316 KKMFPNLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:COG0372 317 KKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
20-368 |
5.31e-165 |
|
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: 466.21 E-value: 5.31e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:pfam00285 2 LRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRALP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIA-DRLMACLGSALLYWYHYSHNGEMIDVQtDDDSIGAHFLHLLHGE 178
Cdd:pfam00285 82 RDAHPMAVLRAAVSALAAFDPEAISDKADYWENALrDDLIAKLPTIAAYIYRHRRGLPPIYPD-PDLSYAENFLYMLFGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:pfam00285 161 EPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVE-NKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEV-----KKMFPNLDWFSAVSYHT 332
Cdd:pfam00285 241 KVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEDlyfveKNLYPNVDFYSGVLYHA 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 497071235 333 MGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRP 368
Cdd:pfam00285 321 LGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRP 356
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
19-372 |
9.44e-161 |
|
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: 455.52 E-value: 9.44e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 19 ALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETL 98
Cdd:cd06118 2 GLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 99 PAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYsHNGEMIDVQTDDDSIGAHFLHLLHGE 178
Cdd:cd06118 82 PKNAHPMDVLRTAVSALGSFDPFARDKSPEARYEKAIRLIAKLPTIAANIYRN-REGLEIIAPDPDLSYAENFLYMLFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:cd06118 161 EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYIW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEV---KKMFPNLDWFSAVSYHTMGV 335
Cdd:cd06118 241 KKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVlgeKGIYPNVDFYSGVVYKALGF 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 497071235 336 PTAMFTPLFVIARTAGWAAHIIEQRVDN-KIIRPTANY 372
Cdd:cd06118 321 PTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
20-374 |
4.26e-131 |
|
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: 380.08 E-value: 4.26e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:cd06110 3 LEGVIAADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWyHYSHNGEMIdVQTDDD-SIGAHFLHLLHGE 178
Cdd:cd06110 83 KDAHPMDVLRTAVSALALYDPEADDMSREANLRKAIRLIAKMPTIVAAF-HRIRNGLEP-VAPDPDlSHAANFLYMLTGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:cd06110 161 KPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPTA 338
Cdd:cd06110 241 DKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIPVD 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 497071235 339 MFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIG 374
Cdd:cd06110 321 LFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
20-383 |
1.77e-128 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 373.90 E-value: 1.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:PRK14033 13 LAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGCVLPEKDDHNlPDA-RDIADRLMACLGSALLYWYHYSHNGEMIDVQtDDDSIGAHFLHLLHGE 178
Cdd:PRK14033 93 TTCHPMDVVRTAVSYLGAEDPEADDSS-PEAnLAKALRLFAVLPTIVAADQRRRRGLDPIAPR-SDLGYAENFLHMCFGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:PRK14033 171 VPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPTA 338
Cdd:PRK14033 251 DALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMGFDID 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497071235 339 MFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPL 383
Cdd:PRK14033 331 FFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVPPI 375
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
20-376 |
5.81e-125 |
|
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: 364.81 E-value: 5.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:cd06111 3 LAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGCVLPEKDDHNlPDA-RDIADRLMACLGSALLYWYHYSHNGEMIDvQTDDDSIGAHFLHLLHGE 178
Cdd:cd06111 83 KNCHPMDVLRTAVSVLGAEDSETDDSS-PDAnLAKAIRLLAQLPTVVAADIRRRKGLDPIP-PDSDLGIAENFLHMCFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:cd06111 161 VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPTA 338
Cdd:cd06111 241 DALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDID 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 497071235 339 MFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPE 376
Cdd:cd06111 321 FFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPE 358
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
19-372 |
6.68e-107 |
|
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: 315.02 E-value: 6.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 19 ALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNrdelraykqklkrlrglplalqtaletl 98
Cdd:cd06101 2 GLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPS---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 99 pahshpmdvmrtavsvlgcvlpekddhnlpdardiadrlmaclgsallywyhYSHNgemidvqtdddsigahFLHLLHGE 178
Cdd:cd06101 54 ----------------------------------------------------YAEN----------------FLYMLGGE 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENP--DQAEED 256
Cdd:cd06101 66 EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPknEPAEAY 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 257 IRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEV---KKMFPNLDWFSAVSYHTM 333
Cdd:cd06101 146 IRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVlyeKKLYPNVDFYSGVLYKAM 225
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497071235 334 GVPTAMFTPLFVIARTAGWAAHIIEQRVDN-KIIRPTANY 372
Cdd:cd06101 226 GFPTELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
20-383 |
2.53e-106 |
|
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: 317.44 E-value: 2.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:cd06112 5 LAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGCVLP--EKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDvQTDDDSIGAHFLHLLHG 177
Cdd:cd06112 85 ETGHPMDMLQATVAALGMFYPkpEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIE-PRPDLDYAENFLYMLFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 178 EKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDI 257
Cdd:cd06112 164 EEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVKAYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTR-MFDIAERLESVMWEV---KKMFPNLDWFSAVSYHTM 333
Cdd:cd06112 244 DKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSkLYEIALEVERLCEELlghKGVYPNVDFYSGIVYKEL 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 497071235 334 GVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPL 383
Cdd:cd06112 324 GIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYVPL 373
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
20-386 |
4.47e-106 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 316.70 E-value: 4.47e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVgrSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGL-PLALQTALETL 98
Cdd:PRK14035 7 LEGVIAAETKISSI--IDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLnDRVYQHFEEYS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 99 PAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSaLLYWYHYSHNGEMIDVQTDDDSIGAHFLHLLHGE 178
Cdd:PRK14035 85 TDHVHPMTALRTSVSYLAHFDPDAEEESDEARYERAIRIQAKVAS-LVTAFARVRQGKEPLKPRPDLSYAANFLYMLRGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:PRK14035 164 LPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVDAYLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPTA 338
Cdd:PRK14035 244 EKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGIPHD 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 497071235 339 MFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:PRK14035 324 LFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
12-379 |
1.35e-105 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 315.51 E-value: 1.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 12 FKPkksvALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLAL 91
Cdd:PRK12349 5 FSP----GLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 92 QTALETLPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIdvQTDDD-SIGAH 170
Cdd:PRK12349 81 FNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPI--EPLKElSYSAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 171 FLHLLHGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENP 250
Cdd:PRK12349 159 FLYMLTGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 251 DQAEEDIRKRVENKEVIIGFGHPVYTIS-DPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVS 329
Cdd:PRK12349 239 EKFEELLQKKLYNKEKIMGFGHRVYMKKmDPRALMMKEALKQLCDVKGDYTLYEMCEAGEKIMEKEKGLYPNLDYYAAPV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 497071235 330 YHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQS 379
Cdd:PRK12349 319 YWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIGERHVL 368
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
20-386 |
4.31e-101 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 303.99 E-value: 4.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVgrSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLP 99
Cdd:PRK14034 7 LEGVVATTSSVSSI--IDDTLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHS-HPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQTDDdSIGAHFLHLLHGE 178
Cdd:PRK14034 85 LKKvHPMSVLRTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDL-SLAANFLYMLNGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 179 KPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIR 258
Cdd:PRK14034 164 EPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVESYIH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 259 KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGVPTA 338
Cdd:PRK14034 244 NKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGIDHD 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 497071235 339 MFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:PRK14034 324 LFTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
12-386 |
1.67e-100 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 302.65 E-value: 1.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 12 FKPkksvALSGVVAGNTALCTV-GRSGNdLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLA 90
Cdd:PRK14036 4 YRP----GLEGVPATQSSISYVdGQKGI-LEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 91 LQTALETLPAHSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYHYShNGEmiD-VQTDDD-SIG 168
Cdd:PRK14036 79 IRDMMKCFPETGHPMDALQASAAALGLFYSRRALDDPEYIRDAVVRLIAKIPTMVAAFQLIR-KGN--DpIQPRDDlDYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 169 AHFLHLLHGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYE 248
Cdd:PRK14036 156 ANFLYMLTEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 249 NPDQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEV---KKMFPNLDWF 325
Cdd:PRK14036 236 SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVAEERlgpKGIYPNVDFY 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497071235 326 SAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPENQSFVPLDQR 386
Cdd:PRK14036 316 SGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
166-372 |
5.65e-97 |
|
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: 287.70 E-value: 5.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 166 SIGAHFLHLLHGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQK 245
Cdd:cd06099 1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 246 RYENP--DQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWEV---KKMFP 320
Cdd:cd06099 81 EIGTPknEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVlyeKKLYP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497071235 321 NLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDN-KIIRPTANY 372
Cdd:cd06099 161 NVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
20-374 |
9.08e-90 |
|
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: 274.57 E-value: 9.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPlALQTALETLP 99
Cdd:cd06109 3 LEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALP-DVVAALLPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 100 AHSHPMDVMRTAVSVLGcvlpekDDHNLPDARdiadRLMACLGSALLYWYHYSHNGEMIDvqtDDDSIG--AHFLHLLHG 177
Cdd:cd06109 82 AGLDPMDALRALLALLP------DSPDLATAL----RLLAAAPVITAALLRLSRGKQPIA---PDPSLShaADYLRMLTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 178 EKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDI 257
Cdd:cd06109 149 EPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAvadGNTRMFDIAERLE----SVMWEVK---KMFPNLDWFSAVSY 330
Cdd:cd06109 229 REALARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEqaalALLREYKpgrPLETNVEFYTALLL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 497071235 331 HTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIG 374
Cdd:cd06109 306 EALGLPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
40-374 |
1.43e-84 |
|
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: 262.90 E-value: 1.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:cd06114 51 LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEKDDHNLPDARDI-ADRLMACLGSALLYWYHYSHNGEMIdvQTDDD-SIGAHFLHLLHGE-----KPSAEWEKAMHVSL 192
Cdd:cd06114 131 PDSLDVNDPEQRELaAIRLIAKVPTIAAMAYRYSIGQPFI--YPDNDlSYVENFLHMMFAVpyepyEVDPVVVKALDTIL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 193 NLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRKrVENKEV---IIG 269
Cdd:cd06114 209 ILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAK-AKDKNDpfrLMG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 270 FGHPVYTISDPRNEVIKSVAKE-LAVADGNTRMFDIAERLESVMWE-----VKKMFPNLDWFSAVSYHTMGVPTAMFTPL 343
Cdd:cd06114 288 FGHRVYKNYDPRAKILKKTCDEvLAELGKDDPLLEIAMELEEIALKddyfiERKLYPNVDFYSGIILRALGIPTEMFTVL 367
|
330 340 350
....*....|....*....|....*....|...
gi 497071235 344 FVIARTAGWAAHIIEQRVD--NKIIRPTANYIG 374
Cdd:cd06114 368 FALGRTPGWIAQWREMHEDpeLKIGRPRQLYTG 400
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
21-374 |
3.73e-84 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) a carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) hydrolysis of citryl-CoA to produce citrate and CoA. CSs are found in two structural types: type I (homodimeric) and type II CSs (homohexameric). Type II CSs are unique to gram-negative bacteria. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria. Type I CS is active as a homodimer, both subunits participating in the active site. Type II CS is a hexamer of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99866 Cd Length: 406 Bit Score: 261.82 E-value: 3.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 21 SGVVAGNTALCTV--------------GRsgndLHYRGYDILDLAQACE------FEEVAHLLIHGKLPNRDELRAYKQK 80
Cdd:cd06113 9 TGVLAGLTNISDVvgykiidgekvpcpGK----LYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 81 LKRLRGLPLA-LQTALETLPAhSHPMDVMRTAVSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWY----HYSHNG 155
Cdd:cd06113 85 LSSYRTLPDNfVEDVILKAPS-KDIMNKLQRSVLALYSYDDKPDDISLENVLRQSIQLIARLPTIAVYAYqakrHYYDGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 156 EM-IDVQTDDDSIGAHFLHLLHGEKPSAEWE-KAMHVSLNLYAEHEF-NASTFTSRVIAGTGSDFYSAIAGAIGALRGPK 232
Cdd:cd06113 164 SLyIHHPQPELSTAENILSMLRPDKKYTELEaKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 233 HGGAN-------EVAFEIQKRYENPDQAEEDIRKRVeNKEV------IIGFGHPVYTISDPRNEVIKSVAKELAVADGNT 299
Cdd:cd06113 244 HGGANikvmemlEDIKENVKDWTDEDEVRAYLRKIL-NKEAfdksglIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGRE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 300 RMFDIAERLE----SVMWEVKKMF----PNLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRV-DNKIIRPTA 370
Cdd:cd06113 323 EEFALYERIErlapEVIAEERGIGktvcANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLnSGRIIRPAY 402
|
....
gi 497071235 371 NYIG 374
Cdd:cd06113 403 KYVG 406
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
17-386 |
7.79e-80 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 250.05 E-value: 7.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 17 SVALSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALE 96
Cdd:PRK14037 5 SKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 97 TLPAHSHPMDVMRTAVSVLGCVlpEKDDHNLPDARDIADRLMACLGSALLYWYHYSHNGEMIDVQTDDdSIGAHFLHLLH 176
Cdd:PRK14037 85 LMPRDSDAIGLMEAAFAALASI--DKNFKWKENDKEKAISIIAKMATIVANVYRRKEGNKPRIPEPSD-SFAESFLLASF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 177 GEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEED 256
Cdd:PRK14037 162 AREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 257 IR-KRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTR-MFDIAERLESVMWEV---KKMFPNLDWFSAVSYH 331
Cdd:PRK14037 242 FNdKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKkYFEIAQKLEELGIKQfgsKGIYPNTDFYSGIVFY 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 497071235 332 TMGVPTAMFTPLFVIARTAGWAAHIIEQrVDN--KIIRPTANYIGPENQSFVPLDQR 386
Cdd:PRK14037 322 ALGFPVYMFTALFALSRTLGWLAHIIEY-VEEqhRLIRPRALYVGPEHREYVPIDKR 377
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
39-386 |
3.70e-79 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 250.21 E-value: 3.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 39 DLHYRGYDILDLAQACE------FEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALqTALETLPAHSHP-MDVMRTA 111
Cdd:PRK14032 67 KLYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGF-TRDMILKAPSKDiMNSLARS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 112 VSVLGCVLPEKDDHNLPDARDIADRLMACLGSALLYWYH---YSHNGE--MIDVQTDDDSIGAHFLHLLHGEKPSAEWEK 186
Cdd:PRK14032 146 VLALYSYDDNPDDTSIDNVLRQSISLIARFPTLAVYAYQayrHYHDGKslYIHPPKPELSTAENILYMLRPDNKYTELEA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 187 AM-HVSLNLYAEHEF-NASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQ-------KRYENPDQAEEDI 257
Cdd:PRK14032 226 RLlDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFedikenvKDWEDEDEIADYL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 258 RKRVeNKEV------IIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLES----VMWEVKKMF----PNLD 323
Cdd:PRK14032 306 TKIL-NKEAfdksglIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEKlapeLIAEERGIYkgvsANVD 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497071235 324 WFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRV-DNKIIRPTANYIGPEnQSFVPLDQR 386
Cdd:PRK14032 385 FYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVnGGKIIRPAYKSVLER-REYVPLEER 447
|
|
| gltA |
PRK05614 |
citrate synthase; |
40-374 |
1.84e-70 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 227.07 E-value: 1.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:PRK05614 69 LLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEKDDHNLPDARDIAD-RLMACLGSALLYWYHYShNGEMIDVQTDDDSIGAHFLHLLHG-----EKPSAEWEKAMHVSLN 193
Cdd:PRK05614 149 HDSLDINDPEHREIAAiRLIAKMPTLAAMAYKYS-IGQPFVYPRNDLSYAENFLRMMFAtpceeYEVNPVLVRALDRIFI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 194 LYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRKrVENKEV---IIGF 270
Cdd:PRK05614 228 LHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIAR-AKDKNDgfrLMGF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 271 GHPVYTISDPRNEVIKSVAKE-LAVADGNTRMFDIAERLESVMWE-----VKKMFPNLDWFSAVSYHTMGVPTAMFTPLF 344
Cdd:PRK05614 307 GHRVYKNYDPRAKIMRETCHEvLKELGLNDPLLEVAMELEEIALNdeyfiERKLYPNVDFYSGIILKALGIPTSMFTVIF 386
|
330 340 350
....*....|....*....|....*....|..
gi 497071235 345 VIARTAGWAAHIIEQRVD--NKIIRPTANYIG 374
Cdd:PRK05614 387 ALARTVGWIAHWNEMHSDpeQKIGRPRQLYTG 418
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
26-374 |
3.56e-67 |
|
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: 217.30 E-value: 3.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 26 GNTALCTVGRSGND-----LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPA 100
Cdd:cd06107 10 LNTAVCESSITYIDgdkgiLLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 101 HSHPMDVMRTAVSVLGCVLPEKDD-------HNLPDARDIAD-RLMACLgSALLYWYHYSHNGEMIDVQTDDDSIGAHFL 172
Cdd:cd06107 90 DAHPMGILCAGLSALSAFYPEAIPahtgdlyQNNPEVRDKQIiRTLAKM-PTIAAAAYCHRIGRPFVYPRANLSYIENFL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 173 HLL-----HGEKPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRY 247
Cdd:cd06107 169 YMMgyvdqEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLREI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 248 ENPDQAEEDIRkRVENKEV-IIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWE-----VKKMFPN 321
Cdd:cd06107 249 GTPENVPAFIE-RVKNGKRrLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEdeyfvSRKLYPN 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 497071235 322 LDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQ--RVDNKIIRPTANYIG 374
Cdd:cd06107 328 VDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMmeDPLQRIWRPRQVYTG 382
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
40-387 |
1.01e-64 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 212.96 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:PLN02456 88 LRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEK-------DDHNLPDARDIAD-RLMACLGSALLYWYHYSHNGEMIdVQTDDDSIGAHFLHLLHG-----EKPSAEWEK 186
Cdd:PLN02456 168 PDAnaylrgqHKYKSWEVRDEDIvRLIGKLPTLAAAIYRRMYGRGPV-IPDNSLDYAENFLYMLGSlgdrsYKPDPRLAR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 187 AMHVSLNLYAEHEFNASTFTSRVIAG-TGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRKRVENKE 265
Cdd:PLN02456 247 LLDLYFIIHADHEGGCSTAAARHLVGsSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 266 VIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVM-----WEVKKMFPNLDWFSAVSYHTMGVPTAMF 340
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVAlldeyFKVRKLYPNVDFYSGVLLRALGFPEEFF 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497071235 341 TPLFVIARTAGWAAHIIEQRVD--NKIIRPTANYIGPENQSFVPLDQRP 387
Cdd:PLN02456 407 TVLFAVSRAAGYLSQWDEALGLpdERIMRPKQVYTGEWLRHYCPKAERT 455
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
40-383 |
1.18e-63 |
|
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.
Pssm-ID: 99869 Cd Length: 384 Bit Score: 208.14 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:cd06116 29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILISSVAALSTFY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEKDDHNLPDARDIAD-RLMACLGSalLYWYHYSHNGEMIDVQTDDD-SIGAHFLHLL-----HGEKPSAEWEKAMHVSL 192
Cdd:cd06116 109 PEAKNIGDEEQRNKQIiRLIGKMPT--IAAFAYRHRLGLPYVLPDNDlSYTGNFLSMLfkmtePKYEPNPVLAKALDVLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 193 NLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRKRVENKEVIIGFGH 272
Cdd:cd06116 187 ILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGH 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 273 PVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWE-----VKKMFPNLDWFSAVSYHTMGVPTAMFTPLFVIA 347
Cdd:cd06116 267 RVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEdeyfiSRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIP 346
|
330 340 350
....*....|....*....|....*....|....*...
gi 497071235 348 RTAGWAAHIIE--QRVDNKIIRPTANYIGPENQSFVPL 383
Cdd:cd06116 347 RTSGWLAQWIEmlRDPEQKIARPRQVYTGPRDRDYVPI 384
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
40-382 |
1.21e-63 |
|
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: 208.83 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:cd06115 49 LRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEKD----DHNLPDARDIADR-LMACLGSA--LLYWYHYSHNGEMIDVQTDDDSIGAHFLHLLHG-----EKPSAEWEKA 187
Cdd:cd06115 129 PEANpalaGQDIYKNKQVRDKqIVRILGKAptIAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSlgerkYKPNPRLARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 188 MHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRKRVENKEVI 267
Cdd:cd06115 209 LDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRKL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 268 IGFGHPVYTISDPRNEVIKSVAKELAVADGNTRMFDIAERLESVMWE-----VKKMFPNLDWFSAVSYHTMGVPTAMFTP 342
Cdd:cd06115 289 SGFGHRVYKNYDPRAKIIKKLADEVFEIVGKDPLIEIAVALEKAALSdeyfvKRKLYPNVDFYSGLIYRAMGFPTDFFPV 368
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497071235 343 LFVIARTAGWAAHIIEQRVD--NKIIRPTANYIGPENQSFVP 382
Cdd:cd06115 369 LFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYVP 410
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
20-376 |
7.76e-61 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 199.80 E-value: 7.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 20 LSGVVAGNTALCTVGRSGNDLHYRGYDILDLAQACEFEEVAHLLIHGklpnrdelrAYKQKLKRLRGLPLA--------- 90
Cdd:PRK12350 5 LEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDG---------RFGPGLPPAEPFPLPvhlgdarvd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 91 LQTALETLP------------AHSHPMDVMRTAVSVLGCVL--------PEKDDHNLPDARDIADRLMAclgsallYWyh 150
Cdd:PRK12350 76 VQAALAMLApvwgfrplldidDLTARLDLARASVMALSAVAqsargigqPAVPQREIDHAATILERFMG-------RW-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 151 yshngemidvqtdddsigahflhllHGEkPSAEWEKAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRG 230
Cdd:PRK12350 147 -------------------------RGE-PDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 231 PKHGGANEVAFEIQKRYENPDQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADgntrmFDIAERLE- 309
Cdd:PRK12350 201 PLHGGAPARVLPMLDAVERTGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGAPR-----YEVAEAVEq 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497071235 310 SVMWEVKKMFP------NLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPTANYIGPE 376
Cdd:PRK12350 276 AALAELRERRPdrpletNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPA 348
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
40-380 |
4.50e-58 |
|
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: 194.61 E-value: 4.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQACEFEEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGCVL 119
Cdd:TIGR01798 56 LLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 120 PEKDDHNLPDARDIAD-RLMACLGSALLYWYHYsHNGEMIDVQTDDDSIGAHFLHLLHG-----EKPSAEWEKAMHVSLN 193
Cdd:TIGR01798 136 HDALDINDPRHREISAiRLIAKIPTLAAMSYKY-SIGQPFVYPRNNLSYAENFLHMMFAtpcedYKVNPVLARAMDRIFI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 194 LYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYENPDQAEEDIRK-RVENKEV-IIGFG 271
Cdd:TIGR01798 215 LHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKvKDKNDPFrLMGFG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 272 HPVYTISDPRNEVIKSVAKEL--AVADGNTRMFDIAERLESVMWE-----VKKMFPNLDWFSAVSYHTMGVPTAMFTPLF 344
Cdd:TIGR01798 295 HRVYKNYDPRAKVMRETCHEVlkELGLHDDPLFKLAMELEKIALNdpyfiERKLYPNVDFYSGIILKAMGIPTSMFTVIF 374
|
330 340 350
....*....|....*....|....*....|....*...
gi 497071235 345 VIARTAGWAAHIIEQRVDN--KIIRPTANYIGPENQSF 380
Cdd:TIGR01798 375 ALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
13-374 |
1.61e-43 |
|
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: 152.80 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 13 KPKKSVALSGVVAG----NTALCTVGRSGndLHYRGYDILDLAQACEFEEVAHLLIHGklpnrdelraykqklkrlrglp 88
Cdd:cd06102 4 RPRAAVAAAALDWGepvlESAITLITEGR--LFYRGRDAVELAETATLEEVAALLWDG---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 89 lalqtaletlpahshpmdvmrtavsvlgcvlpekddhnlPDARDIADRLMACLGSAllywyhyshngemidvQTDDDSIG 168
Cdd:cd06102 60 ---------------------------------------DEAARLLRLLAAALLGA----------------APSDAPVH 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 169 AHFLHLLHGEKPSAEwekAMHVSLNLYAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGANEVAFEIQKRYE 248
Cdd:cd06102 85 RRLARAWGLDPAAAD---LLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEAL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 249 NPDQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADGNTrmfdiAERLESVMWEVKKMFPNLDWFSAV 328
Cdd:cd06102 162 RAGDAEAAVRERLRRGEALPGFGHPLYPDGDPRAAALLAALRPLGPAAPPA-----ARALIEAARALTGARPNIDFALAA 236
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 497071235 329 SYHTMGVP-TAMFTpLFVIARTAGWAAHIIEQRVDNKIIRPTANYIG 374
Cdd:cd06102 237 LTRALGLPaGAAFA-LFALGRSAGWIAHALEQRAQGKLIRPRARYVG 282
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
40-368 |
5.35e-31 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 122.55 E-value: 5.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 40 LHYRGYDILDLAQA------CEF---EEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRT 110
Cdd:PRK09569 61 IRFRGKTIPETFEAlpkapgSEYptvESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 111 AVSVLgcvlpEKD------------------DHNLPDARDIADRLMAClgSALLYWYHYShNGEMIDVQTDDDsIGAHFL 172
Cdd:PRK09569 141 GILAM-----QREskfakfynegkfnkmdawEYMYEDASDLVARIPVI--AAYIYNLKYK-GDKQIPSDPELD-YGANFA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 173 HLLHGEKPSAEwekAMHVSLNLYAEHEF-NASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGAN-EV---AFEIQKRY 247
Cdd:PRK09569 212 HMIGQPKPYKD---VARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANqEVlgwIQQFQEKL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 248 --ENP--DQAEEDIRKRVENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADgntRMFDIAERLESVMWEV-------K 316
Cdd:PRK09569 289 ggEEPtkEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPDD---PLFKLVAMIFEVAPGVltehgktK 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497071235 317 KMFPNLDWFSAVSYHTMGVPTAMF-TPLFVIARTAGWAAHIIEQR-VDNKIIRP 368
Cdd:PRK09569 366 NPWPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANITWDRgLGYAIERP 419
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
42-360 |
1.35e-21 |
|
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: 95.44 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 42 YRGYDILDLaqaCEF------------EEVAHLLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMR 109
Cdd:cd06103 61 FRGKTIPEC---QELlpkadgggeplpEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 110 TAVSVL------------GCVLpeKDDH---NLPDARDIADRLMAClgSALLYWYHYSHNGEMIDVQTDDDsIGAHFLHL 174
Cdd:cd06103 138 AAILALqseskfakayaeGKIN--KTTYweyVYEDAMDLIAKLPVV--AAKIYRRKYRKGGEIGAIDSKLD-WSANFAHM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 175 LHGEKPsaEWEKAMHVSLNLYAEHEF-NASTFTSRVIAGTGSDFYSAIAGAIGALRGPKHGGAN-EVAFEIQKRYEN--P 250
Cdd:cd06103 213 LGYEDE--EFTDLMRLYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANqEVLKWLLKMQKElgK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 251 DQAEEDIRKRVEN----KEVIIGFGHPVYTISDPRNEVIKSVAKELAVADgntRMFDIAERLESVMWEV-------KKMF 319
Cdd:cd06103 291 DVSDEELEKYIWDtlnsGRVVPGYGHAVLRKTDPRFTCQREFALKHLPDD---PLFKLVAQCYKIIPGVlkehgkvKNPY 367
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497071235 320 PNLDWFSAVSYHTMGVP-TAMFTPLFVIARTAGWAAHIIEQR 360
Cdd:cd06103 368 PNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQLVWSR 409
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
174-380 |
1.97e-21 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 92.63 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 174 LLHGEKPSaEWEK----AMHVSLnlyAEHEFNASTFTSRVIAGTGSDFYSAIAGAIGALrGPKHGGANEVA----FEIQK 245
Cdd:PRK06224 44 LLRGRLPT-PNEArlldAVLVAL---VDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAaellQEIAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 246 RYENPDQAEEDIRKRV----ENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVADgntRMFDIAERLESVMWEV--KKMF 319
Cdd:PRK06224 119 AADAGADLDAAARAIVaeyrAAGKRVPGFGHPLHKPVDPRAPRLLALAREAGVAG---RHCRLAEALEAALAAAkgKPLP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497071235 320 PNLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIR----PTAN--YIGPENQSF 380
Cdd:PRK06224 196 LNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQPIGFRiwdpAEEAveYTGPPPREL 262
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
166-369 |
5.73e-21 |
|
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: 90.32 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 166 SIGAHFLHLLHGEKPSAEWEKAMHVSLNLYAEH-EFNASTFTSRVIAGTGS-DFYSAIAGAIGALrGPKHGGANEVAFEI 243
Cdd:cd06100 12 SFGDVLYLLLKGRLPTPYEARLLEALLVALADHgPATPSAHAARLTASAGPeDLQSAVAAGLLGI-GDRFGGAGEGAARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 244 QKR----YENPDQAEEDIRKR-VENKEVIIGFGHPVYTISDPRNEVIKSVAKELAVAdgnTRMFDIAERLESVMWEVK-K 317
Cdd:cd06100 91 FKEavdsGDALDAAAAEFVAEyRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPA---GPHLDYALAVEKALTAAKgK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497071235 318 MFP-NLDWFSAVSYHTMGVPTAMFTPLFVIARTAGWAAHIIEQRVDNKIIRPT 369
Cdd:cd06100 168 PLPlNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRH 220
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
62-351 |
8.77e-18 |
|
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: 84.48 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 62 LLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVL------------GCVLPEKDDHNLPD 129
Cdd:cd06106 90 LLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALnhdskfaaayekGIKKTEYWEPTLED 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 130 ARDIADRLMAClgSALLYWYHYSHNGEMIDVQTDDDSIGaHFLHLLhGEKPSAEWEKAMHVSLNLYAEHE-FNASTFTSR 208
Cdd:cd06106 170 SLNLIARLPAL--AARIYRNVYGEGHGLGKIDPEVDWSY-NFTSML-GYGDNLDFVDLLRLYIALHGDHEgGNVSAHTTH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 209 VIAGTGSDFYSAIAGAIGALRGPKHGGANE--VAFEIQKRYENPDQA-EEDIR----KRVENKEVIIGFGHPVYTISDPR 281
Cdd:cd06106 246 LVGSALSDPYLSYSAGLMGLAGPLHGLAAQevLRWILEMQKNIGSKAtDQDIRdylwKTLKSGRVVPGYGHAVLRKPDPR 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497071235 282 NEVIKSVAKELAVADGN------TRMFDIAERLESVMWEVKKMFPNLDWFSAVSYHTMGV-PTAMFTPLFVIARTAG 351
Cdd:cd06106 326 FTALMEFAQTRPELENDpvvqlvQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIrEFLYYTVIFGVSRALG 402
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
62-360 |
4.34e-16 |
|
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: 79.33 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 62 LLIHGKLPNRDELRAYKQKLKRLRGLPLALQTALETLPAHSHPMDVMRTAVSVLGcvlPE------------KDDHNLPD 129
Cdd:cd06105 90 LLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALN---SEskfakayaegihKSKYWEYV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 130 ARDIADrLMACLG--SALLYWYHYShNGEMIDVQTDDDsIGAHFLHLL-HGEKPSAEwekAMHVSLNLYAEHEF-NASTF 205
Cdd:cd06105 167 YEDSMD-LIAKLPcvAAKIYRNLYR-GGKIIAIDSNLD-WSANFANMLgYTDPQFTE---LMRLYLTIHSDHEGgNVSAH 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 206 TSRVIAGTGSDFYSAIAGAIGALRGPKHGGAN-EVAFEIQKRYE--NPDQAEEDIRKRVENK----EVIIGFGHPVYTIS 278
Cdd:cd06105 241 TTHLVGSALSDPYLSFAAAMNGLAGPLHGLANqEVLVWLTKLQKevGKDVSDEQLREYVWKTlnsgRVVPGYGHAVLRKT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497071235 279 DPRNEVIKSVA-KELAvadgNTRMFDIAERLESVMWEV-------KKMFPNLDWFSAVSYHTMGVpTAM--FTPLFVIAR 348
Cdd:cd06105 321 DPRYTCQREFAlKHLP----NDPLFKLVSQLYKIVPPVlteqgkaKNPWPNVDAHSGVLLQYYGL-TEMnyYTVLFGVSR 395
|
330
....*....|..
gi 497071235 349 TAGWAAHIIEQR 360
Cdd:cd06105 396 ALGVLSQLIWDR 407
|
|
| |
