|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
1-377 |
0e+00 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 733.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 1 MSVVSKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVL 80
Cdd:PRK14037 1 MSVISKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 81 DTIYLMPKEADAIGLLEVGTAALASIDKNFKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLAS 160
Cdd:PRK14037 81 DSIYLMPRDSDAIGLMEAAFAALASIDKNFKWKENDKEKAISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 161 FAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQN 240
Cdd:PRK14037 161 FAREPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 241 WFNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADARRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVF 320
Cdd:PRK14037 241 WFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGIYPNTDFYSGIVF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524537080 321 YALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PRK14037 321 YALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
2-377 |
0e+00 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 720.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 2 SVVSKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLD 81
Cdd:NF041157 1 MEISKGLENVFIKYTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 82 TIYLMPKEADAIGLLEVGTAALASIDKNFKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASF 161
Cdd:NF041157 81 IIRSLPRDSDALAMMETAFSALASIENYKWNKENDREKALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 162 AREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNW 241
Cdd:NF041157 161 GRKPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 242 FNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNaDARRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVFY 321
Cdd:NF041157 241 FNENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTN-EAKKYLEIAEKLEELGIKHFGSKGIYPNTDFYSGIVFY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524537080 322 ALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:NF041157 320 SLGFPVYMFTSLFALSRVLGWLAHIIEYVEEQHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
6-363 |
0e+00 |
|
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: 557.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASIDKNF--KWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR 163
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFArdKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:cd06118 161 EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPENVEAYIW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKvVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIErNADARRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVFYAL 323
Cdd:cd06118 241 KK-LANKRRIMGFGHRVYKTYDPRAKILKELAEELAE-EKGDDKLFEIAEELEEIALEVLGEKGIYPNVDFYSGVVYKAL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALY 363
Cdd:cd06118 319 GFPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
4-377 |
4.35e-179 |
|
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: 502.32 E-value: 4.35e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 4 VSKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTI 83
Cdd:COG0372 13 VDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 84 YLMPKEADAIGLLEVGTAALASIDKN--FKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASF 161
Cdd:COG0372 93 DGFPRDAHPMDVLRTAVSALGAFDPDadDIDPEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAENFLYMLF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 162 AREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNW 241
Cdd:COG0372 173 GEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDNVEEY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 242 FnDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADaRRYFEIAQKLEELGIKQ--FSSKGIYPNTDFYSGIV 319
Cdd:COG0372 253 I-RKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGD-DPLLEIAEELEEVALEDeyFIEKKLYPNVDFYSGIV 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524537080 320 FYALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:COG0372 331 YHALGIPTDMFTPIFAISRVAGWIAHWLEQRAD-NRIIRPRQIYVGPEDRDYVPIEER 387
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
6-377 |
9.73e-170 |
|
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: 478.01 E-value: 9.73e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:TIGR01800 1 KGLEGVIAGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASIDKN-FKW-KENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR 163
Cdd:TIGR01800 81 LPAESHPMDVLRTAVSYLGALDPEkFGHtPEEARDIAIRLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLHGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:TIGR01800 161 EPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADArRYFEIAQKLEELGIKqfsSKGIYPNTDFYSGIVFYAL 323
Cdd:TIGR01800 241 KALEN-KERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSS-KWYEIAERLEDVMEE---EKGIYPNVDFFSASVYYMM 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEEQhRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:TIGR01800 316 GIPTDLFTPIFAMSRVTGWTAHIIEQVENN-RLIRPRADYVGPEERKYVPIEER 368
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
7-360 |
6.01e-165 |
|
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
Pssm-ID: 459747 [Multi-domain] Cd Length: 357 Bit Score: 465.44 E-value: 6.01e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLM 86
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 87 PKEADAIGLLEVGTAALASIDKNFKWKENDKEKAI---SIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR 163
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAISDKADYWENAlrdDLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYMLFGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:pfam00285 161 EPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPDEVEEYIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADaRRYFEIAQKLEELGIK--QFSSKGIYPNTDFYSGIVFY 321
Cdd:pfam00285 241 KVLNKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGD-DPLLELAEELEEVAPEdlYFVEKNLYPNVDFYSGVLYH 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 1524537080 322 ALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPR 360
Cdd:pfam00285 320 ALGIPTDMFTPLFAISRTAGWLAHWIEQLAD-NRIIRPR 357
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
6-365 |
6.04e-132 |
|
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: 381.62 E-value: 6.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06110 1 KGLEGVIAADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASIDKNFK--WKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR 163
Cdd:cd06110 81 LPKDAHPMDVLRTAVSALALYDPEADdmSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYMLTGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:cd06110 161 KPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKvVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERnADARRYFEIAQKLEELGIKQfssKGIYPNTDFYSGIVFYAL 323
Cdd:cd06110 241 DK-LANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKE-TGEPKWYEMSEAIEQAMRDE---KGLNPNVDFYSASVYYML 315
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVG 365
Cdd:cd06110 316 GIPVDLFTPIFAISRVSGWCAHILEQYFN-NRLIRPRAEYVG 356
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
7-374 |
3.13e-125 |
|
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: 365.21 E-value: 3.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLM 86
Cdd:cd06112 4 GLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 87 PKEADAIGLLEVGTAALASIDKNFKWKENDKEK----AISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFA 162
Cdd:cd06112 84 PETGHPMDMLQATVAALGMFYPKPEVLKPNPDYidaaTVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYMLFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 163 REPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWF 242
Cdd:cd06112 164 EEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGSPENVKAYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 243 NDKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADARRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVFYA 322
Cdd:cd06112 244 DKKLAN-KQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGELSKLYEIALEVERLCEELLGHKGVYPNVDFYSGIVYKE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1524537080 323 LGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEYQEYVSI 374
Cdd:cd06112 323 LGIPADLFTPIFAVARVAGWLAHWKEQLGD-NRIFRPTQIYIGEIDRKYVPL 373
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
19-365 |
8.94e-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: 334.55 E-value: 8.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 19 TFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEV 98
Cdd:cd06114 42 TYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 99 GTAALA-----SIDKNFkwKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR-----EPTTD 168
Cdd:cd06114 122 MVNALSafypdSLDVND--PEQRELAAIRLIAKVPTIAAMAYRYSIGQPFIYPDNDLSYVENFLHMMFAVpyepyEVDPV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 169 EINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN---DK 245
Cdd:cd06114 200 VVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAkakDK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 246 vvNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADARRYFEIAQKLEELGIKQ--FSSKGIYPNTDFYSGIVFYAL 323
Cdd:cd06114 280 --NDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDDPLLEIAMELEEIALKDdyFIERKLYPNVDFYSGIILRAL 357
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVG 365
Cdd:cd06114 358 GIPTEMFTVLFALGRTPGWIAQWREMHEDpELKIGRPRQLYTG 400
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
7-377 |
2.63e-111 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 330.00 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLM 86
Cdd:PRK14036 7 GLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 87 PKEADAIGLLEVGTAALASIdknFKWKENDKEKAI-----SIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASF 161
Cdd:PRK14036 87 PETGHPMDALQASAAALGLF---YSRRALDDPEYIrdavvRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYAANFLYMLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 162 AREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNW 241
Cdd:PRK14036 164 EREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEIGSVENVRPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 242 FNDKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIER-NADarRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVF 320
Cdd:PRK14036 244 LDERLAN-KQKIMGFGHREYKVKDPRATILQKLAEELFARfGHD--EYYEIALELERVAEERLGPKGIYPNVDFYSGLVY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524537080 321 YALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PRK14036 321 RKLGIPRDLFTPIFAIARVAGWLAHWREQLGA-NRIFRPTQIYTGSHNRRYIPLEER 376
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
7-365 |
2.06e-110 |
|
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: 327.86 E-value: 2.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLM 86
Cdd:cd06107 8 GYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 87 PKEADAIGLLEVGTAALASIDKN----------FKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSF 156
Cdd:cd06107 88 PRDAHPMGILCAGLSALSAFYPEaipahtgdlyQNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRANLSYIENF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 157 LLASFAREPTTDEIN-----AMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIE 231
Cdd:cd06107 168 LYMMGYVDQEPYEPNprlarALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKMLRE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 232 IGDPNRVQNwFNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLA---LTLIERNAdarrYFEIAQKLEELGIKQ--FSSK 306
Cdd:cd06107 248 IGTPENVPA-FIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDP----LLKVAMELERIALEDeyFVSR 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 307 GIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVG 365
Cdd:cd06107 323 KLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDpLQRIWRPRQVYTG 382
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
6-363 |
7.29e-109 |
|
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: 319.64 E-value: 7.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPtkkelndlkaklneeyevpqevldtiyl 85
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELP---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 mpkeadaigllevgtaalasidknfkwkendkekaisiiakmatlvanvyrrkegnkpripepsdSFAKSFLLASFAREP 165
Cdd:cd06101 53 -----------------------------------------------------------------SYAENFLYMLGGEEP 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 166 TTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPN--RVQNWFN 243
Cdd:cd06101 68 DPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKnePAEAYIR 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKvVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIErNADARRYFEIAQKLEELGIKQFSSKGIYPNTDFYSGIVFYAL 323
Cdd:cd06101 148 KK-LNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLK-EKGLDPMFELAAELEKIAPEVLYEKKLYPNVDFYSGVLYKAM 225
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALY 363
Cdd:cd06101 226 GFPTELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
4-377 |
2.35e-104 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 312.08 E-value: 2.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 4 VSKGLENVIIKVTNLT-FIDGEkgiLRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDT 82
Cdd:PRK14034 3 VTRGLEGVVATTSSVSsIIDDT---LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 83 IYLMP-KEADAIGLLEVGTAALASIDKNFKW--KENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLA 159
Cdd:PRK14034 80 LKQYDlKKVHPMSVLRTAISMLGLYDEEAEImdEEANYRKAVRLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 160 SFAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQ 239
Cdd:PRK14034 160 LNGEEPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 240 NWFNDKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADArRYFEIAQKLEELGIKQfssKGIYPNTDFYSGIV 319
Cdd:PRK14034 240 SYIHNKLQN-KEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEE-KWYNMSIKIEEIVTKE---KGLPPNVDFYSASV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524537080 320 FYALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PRK14034 315 YHCLGIDHDLFTPIFAISRMSGWLAHILEQYEN-NRLIRPRADYVGPTHQVYVPIEER 371
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
19-377 |
3.06e-101 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 306.95 E-value: 3.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 19 TFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEV 98
Cdd:PLN02456 79 SLIDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 99 GTAALAS-----------IDKNFKWKENDKEkAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFL-------LAS 160
Cdd:PLN02456 159 GVMALSTfspdanaylrgQHKYKSWEVRDED-IVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLymlgslgDRS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 161 FAREPTTDEinAMDKALILYTDHEVPASTTAAL-VAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQ 239
Cdd:PLN02456 238 YKPDPRLAR--LLDLYFIIHADHEGGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 240 NwFNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADaRRYFEIAQKLEELGI--KQFSSKGIYPNTDFYSG 317
Cdd:PLN02456 316 E-YVEGVKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGD-DPLFKVASALEEVALldEYFKVRKLYPNVDFYSG 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524537080 318 IVFYALGFPVYMFTALFALSRTLGWLAHIIEYV-EEQHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PLN02456 394 VLLRALGFPEEFFTVLFAVSRAAGYLSQWDEALgLPDERIMRPKQVYTGEWLRHYCPKAER 454
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
5-369 |
3.98e-101 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 303.95 E-value: 3.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 5 SKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIY 84
Cdd:PRK12349 6 SPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNILK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 85 LMPKEADAIGLLEVGTAALASIDKNF--KWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFA 162
Cdd:PRK12349 86 ALPKETHPMDGLRTGVSALAGYDNDIedRSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYSANFLYMLTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 163 REPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWF 242
Cdd:PRK12349 166 KKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYMLLEAGTVEKFEELL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 243 NDKVVNqKNRLMGFGHRVY-KTYDPRAKIFKKLALTLIERNADARRYfEIAQKLEELGIKQfssKGIYPNTDFYSGIVFY 321
Cdd:PRK12349 246 QKKLYN-KEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLY-EMCEAGEKIMEKE---KGLYPNLDYYAAPVYW 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1524537080 322 ALGFPVYMFTALFALSRTLGWLAHIIeyveEQH---RLIRPRALYVGPEYQ 369
Cdd:PRK12349 321 MLGIPIQLYTPIFFSSRTVGLCAHVI----EQHannRLFRPRVNYIGERHV 367
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
6-370 |
9.35e-101 |
|
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: 302.41 E-value: 9.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06111 1 KGLAGVVADTTAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASIDKNFKWKEND--KEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAR 163
Cdd:cd06111 81 LPKNCHPMDVLRTAVSVLGAEDSETDDSSPDanLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMCFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:cd06111 161 VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKvVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNaDARRYFEIAQKLEELgikQFSSKGIYPNTDFYSGIVFYAL 323
Cdd:cd06111 241 DA-LARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVH-DGQKWLAMYDALEDA---MVAAKGIKPNLDFPAGPAYYLM 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPEYQE 370
Cdd:cd06111 316 GFDIDFFTPIFVMARITGWTAHIMEQRAD-NALIRPLSEYNGPEQRP 361
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
6-377 |
2.56e-100 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 301.68 E-value: 2.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKgiLRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEY----EVPQEVLD 81
Cdd:PRK14035 5 RGLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMtlndRVYQHFEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 82 --TIYLMPKEAdaiglLEVGTAALASIDKNFKWK--ENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFL 157
Cdd:PRK14035 83 ysTDHVHPMTA-----LRTSVSYLAHFDPDAEEEsdEARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 158 LASFAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNR 237
Cdd:PRK14035 158 YMLRGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 238 VQNWFNDKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIErNADARRYFEIAQKLEELgIKQfsSKGIYPNTDFYSG 317
Cdd:PRK14035 238 VDAYLDEKFAN-KEKIMGFGHRVYKDGDPRAKYLREMSRKITK-GTGREELFEMSVKIEKR-MKE--EKGLIPNVDFYSA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 318 IVFYALGFPVYMFTALFALSRTLGWLAHIIEYvEEQHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PRK14035 313 TVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQ-YKDNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| gltA |
PRK05614 |
citrate synthase; |
19-365 |
1.36e-98 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 299.10 E-value: 1.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 19 TFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEV 98
Cdd:PRK05614 60 TYIDGDKGILLYRGYPIEQLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 99 GTAALA-----SIDKNfkwKENDKEK-AISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFA-----REPTT 167
Cdd:PRK05614 140 VVGALSafyhdSLDIN---DPEHREIaAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFAtpceeYEVNP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 168 DEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNwFNDKVV 247
Cdd:PRK05614 217 VLVRALDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPE-FIARAK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 248 NqKN---RLMGFGHRVYKTYDPRAKIFKKLALTLIERNADARRYFEIAQKLEELGIKQ--FSSKGIYPNTDFYSGIVFYA 322
Cdd:PRK05614 296 D-KNdgfRLMGFGHRVYKNYDPRAKIMRETCHEVLKELGLNDPLLEVAMELEEIALNDeyFIERKLYPNVDFYSGIILKA 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1524537080 323 LGFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVG 365
Cdd:PRK05614 375 LGIPTSMFTVIFALARTVGWIAHWNEMHSDpEQKIGRPRQLYTG 418
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
4-367 |
7.27e-98 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 295.71 E-value: 7.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 4 VSKGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTI 83
Cdd:PRK14033 9 IKKGLAGVVVDTTAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 84 YLMPKEADAIGLLEVGTAALASIDKNFKWK--ENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASF 161
Cdd:PRK14033 89 DKLPTTCHPMDVVRTAVSYLGAEDPEADDSspEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMCF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 162 AREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNW 241
Cdd:PRK14033 169 GEVPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 242 FNDKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNaDARRYFEIAQKLEELGIKQfssKGIYPNTDFYSGIVFY 321
Cdd:PRK14033 249 LRDALAR-KEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVR-DGQRWLDIYEALEKAMAEA---TGIKPNLDFPAGPAYY 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1524537080 322 ALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVGPE 367
Cdd:PRK14033 324 LMGFDIDFFTPIFVMSRITGWTAHIMEQRAS-NALIRPLSEYNGPE 368
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
7-374 |
6.80e-97 |
|
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: 292.67 E-value: 6.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIdGEKGI-LRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06108 2 GLAGVVAGQTAISTV-GKGGKgLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASIDKNFKWKENDkEKAISIIAKMATLVANVYRRKEGNKpRIPE--PSDSFAKSFLLASFAR 163
Cdd:cd06108 81 IPKDSHPMDVMRTGCSMLGCLEPENEFSQQY-EIAIRLLAIFPSILLYWYHYSHSGK-RIETetDEDSIAGHFLHLLHGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 164 EPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFN 243
Cdd:cd06108 159 KPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 244 DKVVNqKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNADaRRYFEIAQKLEELGIKQfssKGIYPNTDFYSGIVFYAL 323
Cdd:cd06108 239 EKLER-KELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGD-PLLYQISERIEEVMWEE---KKLFPNLDFYSASAYHFC 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYvEEQHRLIRPRALYVGPEYQEYVSI 374
Cdd:cd06108 314 GIPTELFTPIFVMSRVTGWAAHIMEQ-RANNRLIRPSADYIGPEPRPFVPI 363
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
7-372 |
2.97e-94 |
|
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: 287.80 E-value: 2.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLM 86
Cdd:cd06115 28 GYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 87 PKEADAIGLLEVGTAALASI--DKN--------FKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSF 156
Cdd:cd06115 108 PHDAHPMGMLVSAISALSAFhpEANpalagqdiYKNKQVRDKQIVRILGKAPTIAAAAYRRRAGRPPNLPSQDLSYTENF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 157 L-----LASFAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIE 231
Cdd:cd06115 188 LymldsLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRMLAE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 232 IGDPNRVQNwFNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLA---LTLIERNadarRYFEIAQKLEELGIKQ--FSSK 306
Cdd:cd06115 268 IGTVENIPA-FIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLAdevFEIVGKD----PLIEIAVALEKAALSDeyFVKR 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524537080 307 GIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEYQEYV 372
Cdd:cd06115 343 KLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDpDTKIMRPQQLYTGVWLRHYV 409
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
18-371 |
6.08e-90 |
|
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: 276.66 E-value: 6.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 18 LTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLE 97
Cdd:TIGR01798 46 ITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 98 VGTAALASIDKNFKWKENDKEKAISI---IAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAREPTTDEIN--- 171
Cdd:TIGR01798 126 GVVGALSAFYHDALDINDPRHREISAirlIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNpvl 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 172 --AMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFndKVVNQ 249
Cdd:TIGR01798 206 arAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFI--KKVKD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 250 KN---RLMGFGHRVYKTYDPRAKIFKKLAL-TLIERNADARRYFEIAQKLEELGIKQ--FSSKGIYPNTDFYSGIVFYAL 323
Cdd:TIGR01798 284 KNdpfRLMGFGHRVYKNYDPRAKVMRETCHeVLKELGLHDDPLFKLAMELEKIALNDpyFIERKLYPNVDFYSGIILKAM 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1524537080 324 GFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEYQEY 371
Cdd:TIGR01798 364 GIPTSMFTVIFALARTVGWISHWSEMISDpGQKIGRPRQLYTGETQRDY 412
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
6-365 |
1.41e-89 |
|
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: 273.41 E-value: 1.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 6 KGLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06109 1 PGLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MpKEADAIGLLEVGTAALASidknfkwkENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAREP 165
Cdd:cd06109 81 L-AGLDPMDALRALLALLPD--------SPDLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRMLTGEPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 166 TTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFNDK 245
Cdd:cd06109 152 SEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENAEAWLREA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 246 vVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLierNADARRYfEIAQKLE-----ELGIKQfSSKGIYPNTDFYSGIVF 320
Cdd:cd06109 232 -LARGERLMGFGHRVYRVRDPRADVLKAAAERL---GAPDERL-EFAEAVEqaalaLLREYK-PGRPLETNVEFYTALLL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1524537080 321 YALGFPVYMFTALFALSRTLGWLAHIIEYVEEqHRLIRPRALYVG 365
Cdd:cd06109 306 EALGLPREAFTPTFAAGRTAGWTAHVLEQART-GRLIRPQSRYVG 349
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
18-374 |
2.51e-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: 271.70 E-value: 2.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 18 LTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLE 97
Cdd:cd06116 19 ITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAHPMGILI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 98 VGTAALASI---DKNFKWKENDKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLLASFAREPTTDEIN--- 171
Cdd:cd06116 99 SSVAALSTFypeAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNFLSMLFKMTEPKYEPNpvl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 172 --AMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNwFNDKVVNQ 249
Cdd:cd06116 179 akALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQIGSPKNIPD-FIETVKQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 250 KNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNAdARRYFEIAQKLEELGIKQ--FSSKGIYPNTDFYSGIVFYALGFPV 327
Cdd:cd06116 258 KERLMGFGHRVYKNYDPRARIIKKIADEVFEATG-RNPLLDIAVELEKIALEDeyFISRKLYPNVDFYSGLIYQALGFPT 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1524537080 328 YMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEYQEYVSI 374
Cdd:cd06116 337 EAFTVLFAIPRTSGWLAQWIEMLRDpEQKIARPRQVYTGPRDRDYVPI 384
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
151-363 |
6.04e-86 |
|
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.
Pssm-ID: 99853 [Multi-domain] Cd Length: 213 Bit Score: 259.19 E-value: 6.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 151 SFAKSFLLASFAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFI 230
Cdd:cd06099 1 SYAENFLYMLGGEEPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKMLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 231 EIGDPN--RVQNWFNdKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIErNADARRYFEIAQKLEELGIKQFSSKGI 308
Cdd:cd06099 81 EIGTPKnePAEAYIR-KKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLK-EDGDDPMFELAAELEKIAEEVLYEKKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524537080 309 YPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALY 363
Cdd:cd06099 159 YPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
28-377 |
3.54e-80 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 250.23 E-value: 3.54e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 28 LRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEVGTAALASI- 106
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 107 ----DKNFkwkENDKEKAISIIAKMATLVANVYRRKEGNKpRIPEPS--DSFAKSFLLASFAREPTTDEINAMDKALILY 180
Cdd:PRK12351 112 pekeDHNF---SGARDIADRLLASLGSILLYWYHYSHNGR-RIEVETddDSIGGHFLHLLHGKKPSESWVKAMHTSLILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 181 TDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAF---KQF-----IEIGDPNRVQNwfndkvvnqKNR 252
Cdd:PRK12351 188 AEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFeiqQRYdtpdeAEADIRRRVEN---------KEV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 253 LMGFGHRVYKTYDPRAKIFKKLALTLIERNADaRRYFEIAQKLEELgikQFSSKGIYPNTDFYSGIVFYALGFPVYMFTA 332
Cdd:PRK12351 259 VIGFGHPVYTISDPRNKVIKEVAKKLSKEAGD-TKLYDIAERLETV---MWEEKKMFPNLDWFSAVSYHMMGVPTAMFTP 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1524537080 333 LFALSRTLGWLAHIIEYvEEQHRLIRPRALYVGPEYQEYVSIDKR 377
Cdd:PRK12351 335 LFVISRTTGWAAHVIEQ-RQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
28-374 |
2.13e-75 |
|
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: 237.82 E-value: 2.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 28 LRYRGYNIEDLVNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEVGTAALASI- 106
Cdd:cd06117 23 LHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLGCVl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 107 -DKNFKWKENDKEKAISIIAKMATLVANVYR-RKEGNKPRIPEPSDSFAKSFLLASFAREPTTDEINAMDKALILYTDHE 184
Cdd:cd06117 103 pEKEDHPVSGARDIADRLMASLGSILLYWYHySHNGKRIEVETDDDSIGGHFLHLLHGEKPSESWEKAMHISLILYAEHE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 185 VPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNRVQNWFNDKVVNqKNRLMGFGHRVYKTY 264
Cdd:cd06117 183 FNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVEN-KEVVIGFGHPVYTIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 265 DPRAKIFKKLALTLIERNADArRYFEIAQKLEELgikQFSSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLA 344
Cdd:cd06117 262 DPRNQVIKEVAKQLSKEGGDM-KMFDIAERLETV---MWEEKKMFPNLDWFSAVSYHMMGVPTAMFTPLFVIARTTGWSA 337
|
330 340 350
....*....|....*....|....*....|
gi 1524537080 345 HIIEYvEEQHRLIRPRALYVGPEYQEYVSI 374
Cdd:cd06117 338 HIIEQ-RQDGKIIRPSANYTGPEDLKFVPI 366
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
4-365 |
3.34e-74 |
|
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: 236.01 E-value: 3.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 4 VSKGLENvIIKVTNLTFIDGEK----GILRYRGYNIEDLVN-------YGsYEETIYLMLYGKLPTKKELNDLKAKLNEE 72
Cdd:cd06113 11 VLAGLTN-ISDVVGYKIIDGEKvpcpGKLYYRGYDVEDLVNgaqkenrFG-FEETAYLLLFGYLPNKEELEEFCEILSSY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 73 YEVPQEVLDTIYLMPKEADAIGLLEVGTAALASIDKNFKWK--ENDKEKAISIIAKMATLVA---NVYRRKEGNKP---R 144
Cdd:cd06113 89 RTLPDNFVEDVILKAPSKDIMNKLQRSVLALYSYDDKPDDIslENVLRQSIQLIARLPTIAVyayQAKRHYYDGESlyiH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 145 IPEPSDSFAKSFL-LASFAREPTTDEINAMDKALILYTDHEVPA-STTAALVAASTLSDMYSSLTAALAALKGPLHGGAA 222
Cdd:cd06113 169 HPQPELSTAENILsMLRPDKKYTELEAKLLDLCLVLHAEHGGGNnSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGAN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 223 EEAFKQFIEIgdPNRVQNWFNDKVVNQK-NRLM------------GFGHRVYKTYDPRAKIFKKLALTL-IERNADARry 288
Cdd:cd06113 249 IKVMEMLEDI--KENVKDWTDEDEVRAYlRKILnkeafdksgliyGMGHAVYTLSDPRAVVLKKYARSLaKEKGREEE-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 289 FEIAQKLEELGIKQFS-----SKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEEQHRLIRPRALY 363
Cdd:cd06113 325 FALYERIERLAPEVIAeergiGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLNSGRIIRPAYKY 404
|
..
gi 1524537080 364 VG 365
Cdd:cd06113 405 VG 406
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
7-367 |
1.84e-68 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 219.45 E-value: 1.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLML---YGKLPTKKELNDLKAKLNEeyeVPQEVLDti 83
Cdd:PRK12350 4 GLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVdgrFGPGLPPAEPFPLPVHLGD---ARVDVQA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 84 ylmpkeadaigllevGTAALASIDkNFK--WKENDKEKAISIIAKMATLVANVYRRKEGN-KPRIPEPSDSFAKSFL--- 157
Cdd:PRK12350 79 ---------------ALAMLAPVW-GFRplLDIDDLTARLDLARASVMALSAVAQSARGIgQPAVPQREIDHAATILerf 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 158 LASFAREPTTDEINAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIEIGDPNR 237
Cdd:PRK12350 143 MGRWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVERTGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 238 VQNWFnDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLiernaDARRYfEIAQKLEELGIKQFSSKG----IYPNTD 313
Cdd:PRK12350 223 ARGWV-KGALDRGERLMGFGHRVYRAEDPRARVLRATAKRL-----GAPRY-EVAEAVEQAALAELRERRpdrpLETNVE 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524537080 314 FYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIeyveEQH---RLIRPRALYVGPE 367
Cdd:PRK12350 296 FWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHIL----EQKrtgRLVRPSARYVGPA 348
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
4-377 |
3.69e-67 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 219.01 E-value: 3.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 4 VSKGLEN-----VIIKVTNL------TFIDGEK----GILRYRGYNIEDLVN-------YGsYEETIYLMLYGKLPTKKE 61
Cdd:PRK14032 29 VKRGLRNedgtgVLVGLTNIgdvhgyEIDDGEKipdeGKLYYRGYDIKDLVNgflkekrFG-FEEVAYLLLFGELPTKEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 62 LNDLKAKLNEEYEVPQEVLDTIYLMPKEADAIGLLEVGTAALASIDKNFK--WKENDKEKAISIIAKMATLVA---NVYR 136
Cdd:PRK14032 108 LAEFTELLGDYRELPDGFTRDMILKAPSKDIMNSLARSVLALYSYDDNPDdtSIDNVLRQSISLIARFPTLAVyayQAYR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 137 RKEGNKPRI---PEPSDSFAKSFLL-----ASFAREpttdEINAMDKALILYTDHEV-PASTTAALVAASTLSDMYSSLT 207
Cdd:PRK14032 188 HYHDGKSLYihpPKPELSTAENILYmlrpdNKYTEL----EARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 208 AALAALKGPLHGGAAEEAFKQFIEIGDpnRVQNWFND--------KVVN-----QKNRLMGFGHRVYKTYDPRAKIFKKL 274
Cdd:PRK14032 264 AAIGSLKGPKHGGANIKVMEMFEDIKE--NVKDWEDEdeiadyltKILNkeafdKSGLIYGMGHAVYTISDPRAVILKKF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 275 ALTL-IERNADARryFEIAQKLEELGIKQFS-----SKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIE 348
Cdd:PRK14032 342 AEKLaKEKGREEE--FNLYEKIEKLAPELIAeergiYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIE 419
|
410 420
....*....|....*....|....*....
gi 1524537080 349 YVEEQHRLIRPRALYVGPEyQEYVSIDKR 377
Cdd:PRK14032 420 ELVNGGKIIRPAYKSVLER-REYVPLEER 447
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
7-377 |
6.83e-45 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 159.92 E-value: 6.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGIlRYRGYNIEDL---------VNYGSYEETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQ 77
Cdd:PRK09569 41 GARDIRSLVTDISYLDPQEGI-RFRGKTIPETfealpkapgSEYPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 78 EVLDTIYLMPKEADAIGLLEVGTAALASIDKNFK------------WkENDKEKAISIIAKMATLVANVYRRK-EGNKPR 144
Cdd:PRK09569 120 YVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKfynegkfnkmdaW-EYMYEDASDLVARIPVIAAYIYNLKyKGDKQI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 145 IPEPSDSFAKSFLLASFAREPTTDeinAMDKALILYTDHE---VPASTTAALvaASTLSDMYSSLTAALAALKGPLHGGA 221
Cdd:PRK09569 199 PSDPELDYGANFAHMIGQPKPYKD---VARMYFILHSDHEsgnVSAHTTHLV--ASALSDAYYSYSAGLNGLAGPLHGLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 222 AEEAFK---QFIE-IGDPNRVQNWFND---KVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNAdarrYFEIAQK 294
Cdd:PRK09569 274 NQEVLGwiqQFQEkLGGEEPTKEQVEQalwDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLKHLPDDP----LFKLVAM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 295 LEELGIKQFSSKGI----YPNTDFYSGIVFYALGFPVYMF-TALFALSRTLGWLAHIIEYVEEQHRLIRPRALYVGpEYQ 369
Cdd:PRK09569 350 IFEVAPGVLTEHGKtknpWPNVDAQSGVIQWYYGVKEWDFyTVLFGVGRALGVMANITWDRGLGYAIERPKSVTTE-MLE 428
|
....*...
gi 1524537080 370 EYVSIDKR 377
Cdd:PRK09569 429 KWAAEGGR 436
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
7-347 |
3.33e-42 |
|
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: 152.45 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 7 GLENVIIKVTNLTFIDGEKGIlRYRGYNIEDL------VNYGSY---EETIYLMLYGKLPTKKELNDLKAKLNEEYEVPQ 77
Cdd:cd06103 39 GMRGMKGLVYETSVLDPDEGI-RFRGKTIPECqellpkADGGGEplpEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 78 EVLDTIYLMPKEADAIGLLEVGTAALASiDKNFKWKENDK------------EKAISIIAKMATLVANVYRRKEGNKPRI 145
Cdd:cd06103 118 HVVKMIDNLPRNLHPMTQLSAAILALQS-ESKFAKAYAEGkinkttyweyvyEDAMDLIAKLPVVAAKIYRRKYRKGGEI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 146 PEPSDSFAKSFLLASFAREPTTDEINAMDKALILYTDHE---VPASTTAaLVAaSTLSDMYSSLTAALAALKGPLHGGAA 222
Cdd:cd06103 197 GAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEggnVSAHTSH-LVG-SALSDPYLSFSAALNGLAGPLHGLAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 223 EEAFK---QFIEIGDPN----RVQNWFNDkVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALT---------LIERNADAr 286
Cdd:cd06103 275 QEVLKwllKMQKELGKDvsdeELEKYIWD-TLNSGRVVPGYGHAVLRKTDPRFTCQREFALKhlpddplfkLVAQCYKI- 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524537080 287 ryfeIAQKLEELGikqfSSKGIYPNTDFYSGIVFYALGFPVY-MFTALFALSRTLGWLAHII 347
Cdd:cd06103 353 ----IPGVLKEHG----KVKNPYPNVDAHSGVLLQHYGMTEPqYYTVLFGVSRALGVLAQLV 406
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
146-365 |
6.18e-39 |
|
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: 140.09 E-value: 6.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 146 PEPSDSFAKSFLLASF-AREPTTDeinAMDKALILYTDHEVPASTTAALVAASTLSDMYSSLTAALAALKGPLHGGAAEE 224
Cdd:cd06102 76 AAPSDAPVHRRLARAWgLDPAAAD---LLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATAR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 225 A---FKQFIEIGDPNRVQnwfnDKVVNQKNRLMGFGHRVYKTYDPRAK-IFKKLALTLIERNADARRYFEIAqklEELGi 300
Cdd:cd06102 153 VealLDEALRAGDAEAAV----RERLRRGEALPGFGHPLYPDGDPRAAaLLAALRPLGPAAPPAARALIEAA---RALT- 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524537080 301 kqfsskGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVeEQHRLIRPRALYVG 365
Cdd:cd06102 225 ------GARPNIDFALAALTRALGLPAGAAFALFALGRSAGWIAHALEQR-AQGKLIRPRARYVG 282
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
19-347 |
2.18e-33 |
|
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: 128.78 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 19 TFIDGEKGIlRYRGYNIED----LVNYGSYEETI-----YLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYLMPKE 89
Cdd:cd06106 51 SVLDAEEGI-RFHGKTIPEcqkeLPKAPIGGEMLpesmlWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 90 ADAIGLLEVGTAAL-----------ASIDKNFKWKENdKEKAISIIAKMATLVANVYRRKEGNKPRIPEPSDSFAKSFLL 158
Cdd:cd06106 130 LHPMTQLSIGVAALnhdskfaaayeKGIKKTEYWEPT-LEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 159 AS-FAREPTTDEINAMDKALILYTDHE---VPASTTAaLVAaSTLSDMYSSLTAALAALKGPLHGGAAEEAFKQFIE--- 231
Cdd:cd06106 209 TSmLGYGDNLDFVDLLRLYIALHGDHEggnVSAHTTH-LVG-SALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEmqk 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 232 -IGDPNRVQN-----WfndKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNAD-----ARRYFEIAQK-LEELG 299
Cdd:cd06106 287 nIGSKATDQDirdylW---KTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPELENDpvvqlVQKLSEIAPGvLTEHG 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1524537080 300 ikqfSSKGIYPNTDFYSGIVFYALGF--PVYmFTALFALSRTLGWLAHII 347
Cdd:cd06106 364 ----KTKNPFPNVDAASGVLFYHYGIreFLY-YTVIFGVSRALGPLTQLV 408
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
15-347 |
2.30e-27 |
|
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: 112.07 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 15 VTNLTFIDGEKGIlRYRGYNI----EDLVNYGSYEETI-----YLMLYGKLPTKKELNDLKAKLNEEYEVPQEVLDTIYL 85
Cdd:cd06105 47 VWETSVLDPEEGI-RFRGLSIpecqKLLPKAPGGEEPLpeglfWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 86 MPKEADAIGLLEVGTAALASiDKNF-----------KWKENDKEKAISIIAKMATLVANVYRRK-EGNKPRIPEPSDSFA 153
Cdd:cd06105 126 FPTNLHPMSQLSAAITALNS-ESKFakayaegihksKYWEYVYEDSMDLIAKLPCVAAKIYRNLyRGGKIIAIDSNLDWS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 154 KSFL-LASFAREPTTDeinAMDKALILYTDHE---VPASTTAaLVAaSTLSDMYSSLTAALAALKGPLHGGAAEEAFKQF 229
Cdd:cd06105 205 ANFAnMLGYTDPQFTE---LMRLYLTIHSDHEggnVSAHTTH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 230 IEI-----GDPNRVQ----NWfndKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLALTLIERNAdarrYFEIAQKLEEL-- 298
Cdd:cd06105 280 TKLqkevgKDVSDEQlreyVW---KTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDP----LFKLVSQLYKIvp 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1524537080 299 GI--KQFSSKGIYPNTDFYSGIV--FYALGFPVYmFTALFALSRTLGWLAHII 347
Cdd:cd06105 353 PVltEQGKAKNPWPNVDAHSGVLlqYYGLTEMNY-YTVLFGVSRALGVLSQLI 404
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
151-348 |
1.30e-24 |
|
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: 100.33 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 151 SFAKSFLLASFAREPTTDEINAMDKALILYTDH--EVPASTTAALVAASTLSDMYSSLTAALAALkGPLHGGAAEEAFKQ 228
Cdd:cd06100 12 SFGDVLYLLLKGRLPTPYEARLLEALLVALADHgpATPSAHAARLTASAGPEDLQSAVAAGLLGI-GDRFGGAGEGAARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 229 FIEIGDPNRVQNWFNDKVVN----QKNRLMGFGHRVYKTYDPRAKIFKKLAltliERNADARRYFEIAQKLEELGIKQfS 304
Cdd:cd06100 91 FKEAVDSGDALDAAAAEFVAeyraAKKRIPGFGHPVHKNPDPRVPRLLELA----RELGPAGPHLDYALAVEKALTAA-K 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1524537080 305 SKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIIE 348
Cdd:cd06100 166 GKPLPLNVDGAIAAILLDLGFPPGALRGLFVLGRSPGLIAHALE 209
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
151-367 |
1.43e-20 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 89.93 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 151 SFAKSFLLASFAREPTTDEINAMDKALILYTDHEVPASTTAA-LVAASTLSdmyssLTAALAA---LKGPLHGGAAEEAF 226
Cdd:PRK06224 36 SFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPSAAAArMTASGGES-----LQGAVAAgllALGSVHGGAGEQAA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 227 KQFIEI-------GDPNRVQNWFNDKVVNQKNRLMGFGHRVYKTYDPRAKIFKKLAltliERNADARRYFEIAQKLEELG 299
Cdd:PRK06224 111 ELLQEIaaaadagADLDAAARAIVAEYRAAGKRVPGFGHPLHKPVDPRAPRLLALA----REAGVAGRHCRLAEALEAAL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524537080 300 IKQfSSKGIYPNTDFYSGIVFYALGFPVYMFTALFALSRTLGWLAHIieyVEEQHRLIRPRAL--------YVGPE 367
Cdd:PRK06224 187 AAA-KGKPLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHV---WEELQQPIGFRIWdpaeeaveYTGPP 258
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
173-366 |
3.65e-09 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 58.29 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 173 MDKALILYTDHEvPASTTA--ALVAASTLSDMYSSLTAALAALkGPLHGGAAEEAFKQFIEIGDPNRVQNWFNDKVVNQK 250
Cdd:PLN02522 403 IEMCIMLCADHG-PCVSGAhnTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKG 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524537080 251 NRLMGFGHRVYK--TYDPRAKIFKKLALTLIERNadarRYFEIAQKLEELGIKQfsSKGIYPNTDFYSGIVFYALGFPVY 328
Cdd:PLN02522 481 IRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSV----KYMEYAVQVETYTLSK--ANNLVLNVDGAIGSLFLDLLAGSG 554
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524537080 329 MFT--------------ALFALSRTLGWLAHIIeyveEQHRLIRPraLYVGP 366
Cdd:PLN02522 555 MFTkqeideiveigylnGLFVLARSIGLIGHTF----DQKRLKQP--LYRHP 600
|
|
| |
