|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
2-372 |
0e+00 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 713.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 2 AELMRGLEGVIAAETKISSIIDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHF 81
Cdd:PRK14035 1 AELQRGLEGVIAAETKISSIIDSQLTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 82 EEYTTDKVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYML 161
Cdd:PRK14035 81 EEYSTDHVHPMTALRTSVSYLAHFDPDAEEESDEARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 162 RGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEG 241
Cdd:PRK14035 161 RGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 242 YLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGI 321
Cdd:PRK14035 241 YLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLIPNVDFYSATVYHVMGI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 504426577 322 DHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PRK14035 321 PHDLFTPIFAVSRVAGWIAHILEQYKDNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
6-360 |
0e+00 |
|
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: 602.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISSIIDSQ--LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEE 83
Cdd:cd06110 1 KGLEGVIAADSKISYIDGDAgiLIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 84 YTTDkVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRG 163
Cdd:cd06110 81 LPKD-AHPMDVLRTAVSALALYDPEADDMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 164 EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYL 243
Cdd:cd06110 160 EKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 244 QKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDH 323
Cdd:cd06110 240 KDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEKGLNPNVDFYSASVYYMLGIPV 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 504426577 324 DLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIG 360
Cdd:cd06110 320 DLFTPIFAISRVSGWCAHILEQYFNNRLIRPRAEYVG 356
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
6-372 |
0e+00 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 595.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISSIIDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEYT 85
Cdd:PRK14034 5 RGLEGVVATTSSVSSIIDDTLTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 86 TDKVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRGEK 165
Cdd:PRK14034 85 LKKVHPMSVLRTAISMLGLYDEEAEIMDEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNGEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 166 PTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYLQK 245
Cdd:PRK14034 165 PDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVESYIHN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 246 AFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDHDL 325
Cdd:PRK14034 245 KLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEKGLPPNVDFYSASVYHCLGIDHDL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504426577 326 FTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PRK14034 325 FTPIFAISRMSGWLAHILEQYENNRLIRPRADYVGPTHQVYVPIEER 371
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
1-372 |
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: 580.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 1 MAELMRGLEGVIAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMY 78
Cdd:COG0372 10 KFTVDPGLEGVVAGETAISYIdgEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 79 SHFEEYTTDKvHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFL 158
Cdd:COG0372 90 EFLDGFPRDA-HPMDVLRTAVSALGAFDPDADDIDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAENFL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 159 YMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDN 238
Cdd:COG0372 169 YMLFGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 239 VEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE-----EKGLLPNVDFYSA 313
Cdd:COG0372 249 VEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEdeyfiEKKLYPNVDFYSG 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504426577 314 TVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:COG0372 329 IVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRADNRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
6-372 |
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: 516.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISSIIDSQ--LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEE 83
Cdd:TIGR01800 1 KGLEGVIAGETALSTIDGSGgiLTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 84 YTTDkVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRG 163
Cdd:TIGR01800 81 LPAE-SHPMDVLRTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 164 EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYL 243
Cdd:TIGR01800 160 EEPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 244 QKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDH 323
Cdd:TIGR01800 240 RKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEEEKGIYPNVDFFSASVYYMMGIPT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504426577 324 DLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:TIGR01800 320 DLFTPIFAMSRVTGWTAHIIEQVENNRLIRPRADYVGPEERKYVPIEER 368
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
7-355 |
7.64e-178 |
|
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: 497.80 E-value: 7.64e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEY 84
Cdd:pfam00285 1 GLRGVAAGETEISYIdgEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 85 TTDkVHPMTALRTSVSYLAHFDENADDNDEEaLQERAIR--IQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLR 162
Cdd:pfam00285 81 PRD-AHPMAVLRAAVSALAAFDPEAISDKAD-YWENALRddLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 163 GEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGY 242
Cdd:pfam00285 159 GYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 243 LQKAFA-NKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE-----EKGLLPNVDFYSATVY 316
Cdd:pfam00285 239 IRKVLNkGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEdlyfvEKNLYPNVDFYSGVLY 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 504426577 317 HSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPR 355
Cdd:pfam00285 319 HALGIPTDMFTPLFAISRTAGWLAHWIEQLADNRIIRPR 357
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
6-358 |
1.27e-173 |
|
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: 487.49 E-value: 1.27e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISsIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFE 82
Cdd:cd06118 1 PGLEGVKAKETSIS-YIDGDegiLRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 83 EYTTDkVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLR 162
Cdd:cd06118 80 LLPKN-AHPMDVLRTAVSALGSFDPFARDKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 163 GEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGY 242
Cdd:cd06118 159 GEEPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 243 LQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE---EKGLLPNVDFYSATVYHSM 319
Cdd:cd06118 239 IWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEvlgEKGIYPNVDFYSGVVYKAL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 504426577 320 GIDHDLFTPIFAVSRTSGWTAHILEQLRDN-RIMRPRATY 358
Cdd:cd06118 319 GFPTELFTPLFAVSRAVGWLAHIIEYRENNqRLIRPRAEY 358
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
1-372 |
2.80e-145 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 416.28 E-value: 2.80e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 1 MAELMRGLEGVIAAETKISSIiDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPR- 76
Cdd:PRK14036 1 VCEYRPGLEGVPATQSSISYV-DGQkgiLEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 77 --MYSHFEEYTtdkvHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYA 154
Cdd:PRK14036 80 rdMMKCFPETG----HPMDALQASAAALGLFYSRRALDDPEYIRDAVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 155 ANFLYMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIG 234
Cdd:PRK14036 156 ANFLYMLTEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 235 SVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE---EKGLLPNVDFY 311
Cdd:PRK14036 236 SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVAEErlgPKGIYPNVDFY 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504426577 312 SATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PRK14036 316 SGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGANRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
7-369 |
1.20e-142 |
|
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: 409.51 E-value: 1.20e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISsIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPR---MYSH 80
Cdd:cd06112 4 GLAGVPAAESSIS-YIDGKngiLEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNirdMMKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 81 FEEyttdKVHPMTALRTSVSYLAHF--DENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFL 158
Cdd:cd06112 83 FPE----TGHPMDMLQATVAALGMFypKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 159 YMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDN 238
Cdd:cd06112 159 YMLFGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPEN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 239 VEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQ-SELFDVSVKIAEIMKE---EKGLLPNVDFYSAT 314
Cdd:cd06112 239 VKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCEEllgHKGVYPNVDFYSGI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504426577 315 VYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPI 369
Cdd:cd06112 319 VYKELGIPADLFTPIFAVARVAGWLAHWKEQLGDNRIFRPTQIYIGEIDRKYVPL 373
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
3-369 |
4.75e-140 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 402.79 E-value: 4.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 3 ELMRGLEGVIAAETKISSII--DSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSH 80
Cdd:PRK14033 8 EIKKGLAGVVVDTTAISKVVpeTNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 81 FEEYTTDkVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYM 160
Cdd:PRK14033 88 IDKLPTT-CHPMDVVRTAVSYLGAEDPEADDSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 161 LRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVE 240
Cdd:PRK14033 167 CFGEVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 241 GYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMG 320
Cdd:PRK14033 247 EWLRDALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAEATGIKPNLDFPAGPAYYLMG 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504426577 321 IDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPI 369
Cdd:PRK14033 327 FDIDFFTPIFVMSRITGWTAHIMEQRASNALIRPLSEYNGPEQREVPPI 375
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
7-369 |
8.51e-135 |
|
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: 388.97 E-value: 8.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEY 84
Cdd:cd06108 2 GLAGVVAGQTAISTVGKGGkgLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 85 TTDkVHPMTALRTSVSYLAHFDENADDNDEealQERAIRIQAKIASLVASFAR-VREGKEPVKPDPALSYAANFLYMLRG 163
Cdd:cd06108 82 PKD-SHPMDVMRTGCSMLGCLEPENEFSQQ---YEIAIRLLAIFPSILLYWYHySHSGKRIETETDEDSIAGHFLHLLHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 164 EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYL 243
Cdd:cd06108 158 KKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 244 QKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDH 323
Cdd:cd06108 238 LEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEKKLFPNLDFYSASAYHFCGIPT 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 504426577 324 DLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPI 369
Cdd:cd06108 318 ELFTPIFVMSRVTGWAAHIMEQRANNRLIRPSADYIGPEPRPFVPI 363
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
6-365 |
4.57e-134 |
|
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: 387.15 E-value: 4.57e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISSIID--SQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEE 83
Cdd:cd06111 1 KGLAGVVADTTAISKVMPetNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 84 yTTDKVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRG 163
Cdd:cd06111 81 -LPKNCHPMDVLRTAVSVLGAEDSETDDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 164 EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYL 243
Cdd:cd06111 160 EVPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 244 QKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDH 323
Cdd:cd06111 240 LDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAMVAAKGIKPNLDFPAGPAYYLMGFDI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504426577 324 DLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRK 365
Cdd:cd06111 320 DFFTPIFVMARITGWTAHIMEQRADNALIRPLSEYNGPEQRP 361
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
7-360 |
6.23e-131 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 379.45 E-value: 6.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKIS--SIIDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEY 84
Cdd:PRK12349 8 GLDGVIAAETKISflDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 85 --TTdkvHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLR 162
Cdd:PRK12349 88 pkET---HPMDGLRTGVSALAGYDNDIEDRSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSANFLYMLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 163 GEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGY 242
Cdd:PRK12349 165 GKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 243 LQKAFANKDKVMGFGHRVY-KNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGI 321
Cdd:PRK12349 245 LQKKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEKIMEKEKGLYPNLDYYAAPVYWMLGI 324
|
330 340 350
....*....|....*....|....*....|....*....
gi 504426577 322 DHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIG 360
Cdd:PRK12349 325 PIQLYTPIFFSSRTVGLCAHVIEQHANNRLFRPRVNYIG 363
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
2-372 |
1.03e-127 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 371.65 E-value: 1.03e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 2 AELMRGLEGVIAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLnPRMYS 79
Cdd:NF041157 1 MEISKGLENVFIKYTSLTYIdgEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEV-PDHVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 80 HFEEYTTDKVHPMTALRTSVSYLAHFDENADDNDEEalQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLY 159
Cdd:NF041157 80 SIIRSLPRDSDALAMMETAFSALASIENYKWNKEND--REKALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 160 MLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNV 239
Cdd:NF041157 158 ATFGRKPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 240 EGYLQ-KAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEI-MKE--EKGLLPNVDFYSATV 315
Cdd:NF041157 238 EKWFNeNIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEELgIKHfgSKGIYPNTDFYSGIV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 504426577 316 YHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD-NRIMRPRATYIGDVNRKYVPIEER 372
Cdd:NF041157 318 FYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEEqHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
7-372 |
5.74e-118 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 346.91 E-value: 5.74e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEY 84
Cdd:PRK12351 11 ALSGVVAGNTALCTVgkSGNDLHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 85 TTDkVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVASFARV-REGK--EPVKPDPalSYAANFLYML 161
Cdd:PRK12351 91 PAA-AHPMDVMRTGVSVLGCLLPEKEDHNFSGARDIADRLLASLGSILLYWYHYsHNGRriEVETDDD--SIGGHFLHLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 162 RGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEG 241
Cdd:PRK12351 168 HGKKPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 242 YLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGI 321
Cdd:PRK12351 248 DIRRRVENKEVVIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGV 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 504426577 322 DHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PRK12351 328 PTAMFTPLFVISRTTGWAAHVIEQRQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
6-360 |
3.03e-116 |
|
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: 341.21 E-value: 3.03e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISSIiDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPrmysHFE 82
Cdd:cd06109 1 PGLEGVVAAETVLSDV-DGEagrLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPD----VVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 83 EYTTDKVH--PMTALRTSVSYLahfdenaddNDEEALQErAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYM 160
Cdd:cd06109 76 ALLPALAGldPMDALRALLALL---------PDSPDLAT-ALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 161 LRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVE 240
Cdd:cd06109 146 LTGEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 241 GYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSEL-FDVSVKIAEIMKEEK---GLLPNVDFYSATVY 316
Cdd:cd06109 226 AWLREALARGERLMGFGHRVYRVRDPRADVLKAAAERLGAPDERLEFaEAVEQAALALLREYKpgrPLETNVEFYTALLL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 504426577 317 HSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIG 360
Cdd:cd06109 306 EALGLPREAFTPTFAAGRTAGWTAHVLEQARTGRLIRPQSRYVG 349
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
26-360 |
1.05e-113 |
|
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: 336.86 E-value: 1.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 26 LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEYTTDkVHPMTALRTSVSYLAHF 105
Cdd:cd06114 51 LRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRD-AHPMAILSAMVNALSAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 106 D-ENADDNDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRGE-----KPTDVEVEGFNKALI 179
Cdd:cd06114 130 YpDSLDVNDPEQRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVpyepyEVDPVVVKALDTILI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 180 LHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYLQKAfanKDK-----VM 254
Cdd:cd06114 210 LHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKA---KDKndpfrLM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 255 GFGHRVYKNGDPRAKYLKEMSQKITNETGQSE-LFDVSVKIAEIMKE-----EKGLLPNVDFYSATVYHSMGIDHDLFTP 328
Cdd:cd06114 287 GFGHRVYKNYDPRAKILKKTCDEVLAELGKDDpLLEIAMELEEIALKddyfiERKLYPNVDFYSGIILRALGIPTEMFTV 366
|
330 340 350
....*....|....*....|....*....|....
gi 504426577 329 IFAVSRTSGWTAHILEQLRD--NRIMRPRATYIG 360
Cdd:cd06114 367 LFALGRTPGWIAQWREMHEDpeLKIGRPRQLYTG 400
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
6-358 |
6.01e-110 |
|
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: 322.34 E-value: 6.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLEGVIAAETKISsIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPtkkelselkeklfeymtlnprmyshfe 82
Cdd:cd06101 1 PGLRGVAALESEIS-VIDGDeggLRYRGYPIEELAENSSFEEVAYLLLTGELP--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 83 eyttdkvhpmtalrtsvsylahfdenaddndeealqerairiqakiaslvasfarvregkepvkpdpalSYAANFLYMLR 162
Cdd:cd06101 53 ---------------------------------------------------------------------SYAENFLYMLG 63
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 163 GEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSV--DNVE 240
Cdd:cd06101 64 GEEPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPknEPAE 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 241 GYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSV---KIAEIMKEEKGLLPNVDFYSATVYH 317
Cdd:cd06101 144 AYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAeleKIAPEVLYEKKLYPNVDFYSGVLYK 223
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504426577 318 SMGIDHDLFTPIFAVSRTSGWTAHILEQLRDN-RIMRPRATY 358
Cdd:cd06101 224 AMGFPTELFTPLFAVSRAVGWLAHLIEQREDGqRIIRPRAEY 265
|
|
| gltA |
PRK05614 |
citrate synthase; |
15-360 |
2.88e-107 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 321.06 E-value: 2.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 15 ETKISsIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEYTTDkVHP 91
Cdd:PRK05614 56 ESKIT-YIDGDkgiLLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRD-AHP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 92 MTALRTSVSYLAHFDENADD-NDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRG-----EK 165
Cdd:PRK05614 134 MAVLCGVVGALSAFYHDSLDiNDPEHREIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFAtpceeYE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 166 PTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYLQK 245
Cdd:PRK05614 214 VNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIAR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 246 AfanKDK-----VMGFGHRVYKNGDPRAKYLKEMSQKITNETG-QSELFDVSVKIAEIMKE-----EKGLLPNVDFYSAT 314
Cdd:PRK05614 294 A---KDKndgfrLMGFGHRVYKNYDPRAKIMRETCHEVLKELGlNDPLLEVAMELEEIALNdeyfiERKLYPNVDFYSGI 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504426577 315 VYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD--NRIMRPRATYIG 360
Cdd:PRK05614 371 ILKALGIPTSMFTVIFALARTVGWIAHWNEMHSDpeQKIGRPRQLYTG 418
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
152-358 |
6.26e-102 |
|
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: 300.02 E-value: 6.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 152 SYAANFLYMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLT 231
Cdd:cd06099 1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 232 EIGSV--DNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSV---KIAEIMKEEKGLLP 306
Cdd:cd06099 81 EIGTPknEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAeleKIAEEVLYEKKLYP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504426577 307 NVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDN-RIMRPRATY 358
Cdd:cd06099 161 NVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNfKIIRPRSEY 213
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
8-369 |
9.85e-101 |
|
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: 302.53 E-value: 9.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 8 LEGVIAAETKISSIIDS--QLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLnPRMYSHFEEYT 85
Cdd:cd06117 3 LSGVAAGNTALCTVGRSgnDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGL-PANVKTALEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 86 TDKVHPMTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVA---SFARVREGKEPVKPDPalSYAANFLYMLR 162
Cdd:cd06117 82 PAAAHPMDVMRTGVSVLGCVLPEKEDHPVSGARDIADRLMASLGSILLywyHYSHNGKRIEVETDDD--SIGGHFLHLLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 163 GEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGY 242
Cdd:cd06117 160 GEKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 243 LQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGID 322
Cdd:cd06117 240 IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWEEKKMFPNLDWFSAVSYHMMGVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504426577 323 HDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRKYVPI 369
Cdd:cd06117 320 TAMFTPLFVIARTTGWSAHIIEQRQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
7-360 |
2.76e-99 |
|
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: 299.35 E-value: 2.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISsIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEE 83
Cdd:cd06107 8 GYLNTAVCESSIT-YIDGDkgiLLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 84 YTTDkVHPMTALRTSVSYLAHFDENADD--------NDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAA 155
Cdd:cd06107 87 FPRD-AHPMGILCAGLSALSAFYPEAIPahtgdlyqNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRANLSYIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 156 NFLYML-----RGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQML 230
Cdd:cd06107 166 NFLYMMgyvdqEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKML 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 231 TEIGSVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE-----EKGLL 305
Cdd:cd06107 246 REIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEdeyfvSRKLY 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 504426577 306 PNVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD--NRIMRPRATYIG 360
Cdd:cd06107 326 PNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDplQRIWRPRQVYTG 382
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
1-372 |
3.36e-99 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 298.97 E-value: 3.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 1 MAELMRGLEGVIAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMY 78
Cdd:PRK14037 1 MSVISKGLENVIIKVTNLTFIdgEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 79 SHFEEYTTDKvHPMTALRTSVSYLAHFDENADDNDEEalQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFL 158
Cdd:PRK14037 81 DSIYLMPRDS-DAIGLMEAAFAALASIDKNFKWKEND--KEKAISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 159 YMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDN 238
Cdd:PRK14037 158 LASFAREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 239 VEGYLQ-KAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKIT-NETGQSELFDVSVKIAEIMKEE---KGLLPNVDFYSA 313
Cdd:PRK14037 238 VEMWFNdKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIeRNSEAKKYFEIAQKLEELGIKQfgsKGIYPNTDFYSG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 314 TVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD-NRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PRK14037 318 IVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
5-372 |
4.14e-95 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 291.16 E-value: 4.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 5 MRGLEGVIAAetkiSSIIDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHF 81
Cdd:PLN02456 68 YRNTAPVLSE----ISLIDGDegiLRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 82 EEYTTDkVHPMTALRTSVSYLAHFDENADD--------NDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSY 153
Cdd:PLN02456 144 DALPHD-AHPMTQLVSGVMALSTFSPDANAylrgqhkyKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 154 AANFLYML-----RGEKPTDVEVEGFNKALILHADHELNASAFTARCAV-SSLSDMYSGVTAAVSSLKGPLHGGANERVM 227
Cdd:PLN02456 223 AENFLYMLgslgdRSYKPDPRLARLLDLYFIIHADHEGGCSTAAARHLVgSSGVDPYTSVAAGVNALAGPLHGGANEAVL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 228 QMLTEIGSVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEE-----K 302
Cdd:PLN02456 303 KMLKEIGTVENIPEYVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVALLDeyfkvR 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426577 303 GLLPNVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQL--RDNRIMRPRATYIGDVNRKYVPIEER 372
Cdd:PLN02456 383 KLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALglPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
6-372 |
2.09e-90 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 278.71 E-value: 2.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGL-----EGVIAAETKISSI------------IDSQLTYAGYDIDDLTENAQ------FEEIVFLLWNYRLPTKKELSE 62
Cdd:PRK14032 31 RGLrnedgTGVLVGLTNIGDVhgyeiddgekipDEGKLYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 63 LKEKLFEYMTLnPrmyshfEEYTTD---KVHP---MTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVA--- 133
Cdd:PRK14032 111 FTELLGDYREL-P------DGFTRDmilKAPSkdiMNSLARSVLALYSYDDNPDDTSIDNVLRQSISLIARFPTLAVyay 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 134 -SFARVREGKEPV--KPDPALSYAANFLYMLRGE-KPTDVEVEGFNKALILHADHEL-NASAFTARCAVSSLSDMYSGVT 208
Cdd:PRK14032 184 qAYRHYHDGKSLYihPPKPELSTAENILYMLRPDnKYTELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 209 AAVSSLKGPLHGGANERVMQMLTEI-------GSVDNVEGYLQK-----AFANKDKVMGFGHRVYKNGDPRAKYLKEMSQ 276
Cdd:PRK14032 264 AAIGSLKGPKHGGANIKVMEMFEDIkenvkdwEDEDEIADYLTKilnkeAFDKSGLIYGMGHAVYTISDPRAVILKKFAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 277 KITNETGQSELFDVSVKIA----EIMKEE----KGLLPNVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQL-R 347
Cdd:PRK14032 344 KLAKEKGREEEFNLYEKIEklapELIAEErgiyKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELvN 423
|
410 420
....*....|....*....|....*
gi 504426577 348 DNRIMRPRATYIGDvNRKYVPIEER 372
Cdd:PRK14032 424 GGKIIRPAYKSVLE-RREYVPLEER 447
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
12-368 |
1.73e-88 |
|
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: 272.78 E-value: 1.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 12 IAAETKISSI--IDSQLTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEYTTDKv 89
Cdd:cd06115 33 AVVRSKISYIdgDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHDA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 90 HPMTALRTSVSYLAHFDENADD--------NDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYML 161
Cdd:cd06115 112 HPMGMLVSAISALSAFHPEANPalagqdiyKNKQVRDKQIVRILGKAPTIAAAAYRRRAGRPPNLPSQDLSYTENFLYML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 162 -----RGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSV 236
Cdd:cd06115 192 dslgeRKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAEIGTV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 237 DNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKE-----EKGLLPNVDFY 311
Cdd:cd06115 272 ENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKDPLIEIAVALEKAALSdeyfvKRKLYPNVDFY 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504426577 312 SATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD--NRIMRPRATYIGDVNRKYVP 368
Cdd:cd06115 352 SGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDpdTKIMRPQQLYTGVWLRHYVP 410
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
26-369 |
3.66e-88 |
|
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: 270.93 E-value: 3.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 26 LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEYTTDkVHPMTALRTSVSYLAHF 105
Cdd:cd06116 29 LRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYD-AHPMGILISSVAALSTF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 106 DENADDNDEEALQERAI-RIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYML-----RGEKPTDVEVEGFNKALI 179
Cdd:cd06116 108 YPEAKNIGDEEQRNKQIiRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNFLSMLfkmtePKYEPNPVLAKALDVLFI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 180 LHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYLQKAFANKDKVMGFGHR 259
Cdd:cd06116 188 LHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPDFIETVKQGKERLMGFGHR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 260 VYKNGDPRAKYLKEMSQKITNETGQSELFDVSVKIAEIMKEE-----KGLLPNVDFYSATVYHSMGIDHDLFTPIFAVSR 334
Cdd:cd06116 268 VYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDeyfisRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIPR 347
|
330 340 350
....*....|....*....|....*....|....*..
gi 504426577 335 TSGWTAHILEQLRD--NRIMRPRATYIGDVNRKYVPI 369
Cdd:cd06116 348 TSGWLAQWIEMLRDpeQKIARPRQVYTGPRDRDYVPI 384
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
7-366 |
8.51e-88 |
|
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: 270.88 E-value: 8.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLTENAQFEEIVFLLWNYRLPTKKELSELKEKLFEYMTLNPRMYSHFEEY 84
Cdd:TIGR01798 35 GFTSTASCESKITFIDGDKgiLLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 85 TTDkVHPMTALRTSVSYLAHFDENADD-NDEEALQERAIRIQAKIASLVASFARVREGKEPVKPDPALSYAANFLYMLRG 163
Cdd:TIGR01798 115 RRD-AHPMAVMVGVVGALSAFYHDALDiNDPRHREISAIRLIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 164 -----EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDN 238
Cdd:TIGR01798 194 tpcedYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKN 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 239 VEGYLQKAFANKD--KVMGFGHRVYKNGDPRAKYLKEMSQKITNETGQ--SELFDVSVKIAEIMKE-----EKGLLPNVD 309
Cdd:TIGR01798 274 IDEFIKKVKDKNDpfRLMGFGHRVYKNYDPRAKVMRETCHEVLKELGLhdDPLFKLAMELEKIALNdpyfiERKLYPNVD 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504426577 310 FYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDN--RIMRPRATYIGDVNRKY 366
Cdd:TIGR01798 354 FYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPgqKIGRPRQLYTGETQRDY 412
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
6-360 |
2.03e-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: 262.20 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 6 RGLE-----GVIAAETKISSI------------IDSQLTYAGYDIDDLTENAQ------FEEIVFLLWNYRLPTKKELSE 62
Cdd:cd06113 1 RGLRnedgtGVLAGLTNISDVvgykiidgekvpCPGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 63 LKEKLFEYMTLNPrmyshfeEYTTDKVHP------MTALRTSVSYLAHFDENADDNDEEALQERAIRIQAKIASLVA--- 133
Cdd:cd06113 81 FCEILSSYRTLPD-------NFVEDVILKapskdiMNKLQRSVLALYSYDDKPDDISLENVLRQSIQLIARLPTIAVyay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 134 -SFARVREGKEPV--KPDPALSYAANFLYMLRGEKP-TDVEVEGFNKALILHADHEL-NASAFTARCAVSSLSDMYSGVT 208
Cdd:cd06113 154 qAKRHYYDGESLYihHPQPELSTAENILSMLRPDKKyTELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 209 AAVSSLKGPLHGGANERVMQMLTEI-------GSVDNVEGYLQK-----AFANKDKVMGFGHRVYKNGDPRAKYLKEMSQ 276
Cdd:cd06113 234 AAIGSLKGPRHGGANIKVMEMLEDIkenvkdwTDEDEVRAYLRKilnkeAFDKSGLIYGMGHAVYTLSDPRAVVLKKYAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 277 KITNETGQSELFDVSVKIA----EIMKEE----KGLLPNVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQL-R 347
Cdd:cd06113 314 SLAKEKGREEEFALYERIErlapEVIAEErgigKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELlN 393
|
410
....*....|...
gi 504426577 348 DNRIMRPRATYIG 360
Cdd:cd06113 394 SGRIIRPAYKYVG 406
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
7-365 |
8.90e-77 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 240.64 E-value: 8.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 7 GLEGVIAAETKISSIiDSQ---LTYAGYDIDDLTENAQFEEIVFLLWNYR---LPTKKELSELKeklfeymtlnprmySH 80
Cdd:PRK12350 4 GLEGVVAFETEIAEP-DGDggaLRYRGVDIEDLVGRVTFEDVWALLVDGRfgpGLPPAEPFPLP--------------VH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 81 FEEYTTDkVHPMTALRTSV-SYLAHFDEnaddnDEEALQERAIRIQAKIASLVASFARvreGKE-PVKPDPALSYAANFL 158
Cdd:PRK12350 69 LGDARVD-VQAALAMLAPVwGFRPLLDI-----DDLTARLDLARASVMALSAVAQSAR---GIGqPAVPQREIDHAATIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 159 YMLRG---EKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGS 235
Cdd:PRK12350 140 ERFMGrwrGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVER 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 236 VDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKItnetgQSELFDVSVKIA----EIMKEEKGLLP---NV 308
Cdd:PRK12350 220 TGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRL-----GAPRYEVAEAVEqaalAELRERRPDRPletNV 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 504426577 309 DFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPRATYIGDVNRK 365
Cdd:PRK12350 295 EFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKRTGRLVRPSARYVGPAPRS 351
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
175-360 |
1.25e-51 |
|
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: 173.22 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 175 NKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQMLTEIGSVDNVEGYLQKAFANKDKVM 254
Cdd:cd06102 102 RRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVRERLRRGEALP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 255 GFGHRVYKNGDPRAKYLKEMSQKitnetGQSELFDVSVKIAEIMKEEKGLLPNVDFYSATVYHSMGIDHDLFTPIFAVSR 334
Cdd:cd06102 182 GFGHPLYPDGDPRAAALLAALRP-----LGPAAPPAARALIEAARALTGARPNIDFALAALTRALGLPAGAAFALFALGR 256
|
170 180
....*....|....*....|....*.
gi 504426577 335 TSGWTAHILEQLRDNRIMRPRATYIG 360
Cdd:cd06102 257 SAGWIAHALEQRAQGKLIRPRARYVG 282
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
2-342 |
1.61e-36 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 137.19 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 2 AELMRGLEGVIAAETKISSIiDSQ--LTYAGYDIDDLTEN---------AQFEEIVFLLWNYRLPTKKELSELKEKLfey 70
Cdd:PRK09569 36 EQCIGGARDIRSLVTDISYL-DPQegIRFRGKTIPETFEAlpkapgseyPTVESFWYFLLTGEVPTQEQVQEVVAEW--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 71 mtlnpRMYSHFEEYTTDKV-------HPMTALRTSVSYLAHFDENADD---------NDEEALQERAIRIQAKIASLVAS 134
Cdd:PRK09569 112 -----KKRQNVPQYVIDAIralprdsHPMVMLSVGILAMQRESKFAKFynegkfnkmDAWEYMYEDASDLVARIPVIAAY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 135 FARVR-EGKEPVKPDPALSYAANFLYMLRGEKPTDVEVEGFNkalILHADHEL-NASAFTARCAVSSLSDMYSGVTAAVS 212
Cdd:PRK09569 187 IYNLKyKGDKQIPSDPELDYGANFAHMIGQPKPYKDVARMYF---ILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 213 SLKGPLHGGANERV----MQMLTEIGSV----DNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKITNEtgq 284
Cdd:PRK09569 264 GLAGPLHGLANQEVlgwiQQFQEKLGGEeptkEQVEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPD--- 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 285 selfDVSVKIAEIMKEE-KGLL----------PNVDFYSATVYHSMGI-DHDLFTPIFAVSRTSGWTAHI 342
Cdd:PRK09569 341 ----DPLFKLVAMIFEVaPGVLtehgktknpwPNVDAQSGVIQWYYGVkEWDFYTVLFGVGRALGVMANI 406
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
5-346 |
2.38e-34 |
|
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: 131.27 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 5 MRGLEGVIAaETkisSIIDSQ--LTYAGYDIDDLTENAQ---------FEEIVFLLWNYRLPTKKELSELKEKLFEYMTL 73
Cdd:cd06103 40 MRGMKGLVY-ET---SVLDPDegIRFRGKTIPECQELLPkadgggeplPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 74 nPRMYSHFEEYTTDKVHPMTALRTSVSYLAH-------FDE---NADDNDEEALqERAIRIQAKIASLVASFAR--VREG 141
Cdd:cd06103 116 -PSHVVKMIDNLPRNLHPMTQLSAAILALQSeskfakaYAEgkiNKTTYWEYVY-EDAMDLIAKLPVVAAKIYRrkYRKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 142 KEPVKPDPALSYAANFLYMLRGEKPTDVEV-EGFnkaLILHADHEL-NASAFTARCAVSSLSDMYSGVTAAVSSLKGPLH 219
Cdd:cd06103 194 GEIGAIDSKLDWSANFAHMLGYEDEEFTDLmRLY---LTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 220 GGANERVM----QMLTEIG---SVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKitnETGQSELFDVSV 292
Cdd:cd06103 271 GLANQEVLkwllKMQKELGkdvSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALK---HLPDDPLFKLVA 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426577 293 KIAEIM-------KEEKGLLPNVDFYSATVYHSMGIDH-DLFTPIFAVSRTSGwtahILEQL 346
Cdd:cd06103 348 QCYKIIpgvlkehGKVKNPYPNVDAHSGVLLQHYGMTEpQYYTVLFGVSRALG----VLAQL 405
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
151-365 |
2.07e-29 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 114.20 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 151 LSYAANFLYMLRGEKPTDVEVEGFNKALILHADHELNASAFTARCAVSSLSDMYSGVTAAVSSLkGPLHGGANERVMQML 230
Cdd:PRK06224 35 LSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGEQAAELL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 231 TEI----GSVDNVEGY----LQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQkitnETGQS-ELFDVSVKIAEIMKEE 301
Cdd:PRK06224 114 QEIaaaaDAGADLDAAaraiVAEYRAAGKRVPGFGHPLHKPVDPRAPRLLALAR----EAGVAgRHCRLAEALEAALAAA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426577 302 KG--LLPNVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRD---NRIMRPR---ATYIGDVNRK 365
Cdd:PRK06224 190 KGkpLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQpigFRIWDPAeeaVEYTGPPPRE 261
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
43-356 |
4.53e-29 |
|
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: 116.83 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 43 EEIVFLLWNYRLPTKKELSELKEKLFEYmtlnprmySHFEEYTTDKV-------HPMTALRTSVSYLAHfDENADDNDEE 115
Cdd:cd06106 85 ESMLWLLLTGKVPTFEQARGLSKELAER--------GKLPHYIEKLLdslpktlHPMTQLSIGVAALNH-DSKFAAAYEK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 116 ALQ---------ERAIRIQAKIASLVASFAR--VREGKEPVKPDPALSYAANFLYMLRGEKPTDVeVEGFNKALILHADH 184
Cdd:cd06106 156 GIKkteyweptlEDSLNLIARLPALAARIYRnvYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLDF-VDLLRLYIALHGDH 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 185 EL-NASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGANERVMQ----MLTEIGSV---DNVEGYLQKAFANKDKVMGF 256
Cdd:cd06106 235 EGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRwileMQKNIGSKatdQDIRDYLWKTLKSGRVVPGY 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 257 GHRVYKNGDPRAKYLKEMSQKiTNETGQSELFDVSVKIAEI----MKEE---KGLLPNVDFYSATVYHSMGIDHDLF-TP 328
Cdd:cd06106 315 GHAVLRKPDPRFTALMEFAQT-RPELENDPVVQLVQKLSEIapgvLTEHgktKNPFPNVDAASGVLFYHYGIREFLYyTV 393
|
330 340 350
....*....|....*....|....*....|...
gi 504426577 329 IFAVSRTSGwtahILEQLRDNRIM-----RPRA 356
Cdd:cd06106 394 IFGVSRALG----PLTQLVWDRILglpieRPKS 422
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
151-355 |
9.60e-28 |
|
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: 108.81 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 151 LSYAANFLYMLRGEKPTDVEVEGFNKALILHADHELNA-SAFTARCAVSS-LSDMYSGVTAAVSSLkGPLHGGANERVMQ 228
Cdd:cd06100 11 ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATpSAHAARLTASAgPEDLQSAVAAGLLGI-GDRFGGAGEGAAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 229 MLTEI-----GSVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKitnETGQSELFDVSVKIAEIMKEEKG 303
Cdd:cd06100 90 LFKEAvdsgdALDAAAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARE---LGPAGPHLDYALAVEKALTAAKG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504426577 304 -LLP-NVDFYSATVYHSMGIDHDLFTPIFAVSRTSGWTAHILEQLRDNRIMRPR 355
Cdd:cd06100 167 kPLPlNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRH 220
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
5-356 |
4.31e-26 |
|
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: 108.22 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 5 MRGLEGVIAaETkisSIIDSQ--LTYAGYDIDDLTE---NAQF------EEIVFLLWNYRLPTKKELSELKEKLFEYMTL 73
Cdd:cd06105 40 MRGIKGLVW-ET---SVLDPEegIRFRGLSIPECQKllpKAPGgeeplpEGLFWLLLTGEVPTKEQVSALSKEWAARAAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 74 NPRMYSHFEEYTTDkVHPMTALRTSVSYLAHFDENADDNDE--------EALQERAIRIQAKIASLVAS-FARVREGKEP 144
Cdd:cd06105 116 PSHVVTMLDNFPTN-LHPMSQLSAAITALNSESKFAKAYAEgihkskywEYVYEDSMDLIAKLPCVAAKiYRNLYRGGKI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 145 VKPDPALSYAANFLYMLRGEKPTDVEVegFNKALILHADHEL-NASAFTARCAVSSLSDMYSGVTAAVSSLKGPLHGGAN 223
Cdd:cd06105 195 IAIDSNLDWSANFANMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLAN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426577 224 ERV----MQMLTEIG---SVDNVEGYLQKAFANKDKVMGFGHRVYKNGDPRAKYLKEMSQKitnETGQSELFDVSVKIAE 296
Cdd:cd06105 273 QEVlvwlTKLQKEVGkdvSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALK---HLPNDPLFKLVSQLYK 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504426577 297 IMKE---EKGLL----PNVDFYSATVYHSMGI-DHDLFTPIFAVSRTSGwtahILEQLRDNRIM-----RPRA 356
Cdd:cd06105 350 IVPPvltEQGKAknpwPNVDAHSGVLLQYYGLtEMNYYTVLFGVSRALG----VLSQLIWDRALglpleRPKS 418
|
|
| |
