|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02456 |
PLN02456 |
citrate synthase |
32-485 |
0e+00 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 864.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 32 AIAPWCTSAHITAAPHGSLKGNLTIVDERTGKKYQVPVSEHGTVKAVDLKKITTGKDDKGLKLYDPGYLNTAPVRSSICY 111
Cdd:PLN02456 1 AAAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKAGKDDLGLKTVDPGYRNTAPVLSEISL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 112 IDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAM 191
Cdd:PLN02456 81 IDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 192 SALSIFHPDANPALSGQDIYKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLDSMGNRSYKP 271
Cdd:PLN02456 161 MALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 272 NPRLARVLDILFILHAEHEMNCSTAAARHLA-SSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEG 350
Cdd:PLN02456 241 DPRLARLLDLYFIIHADHEGGCSTAAARHLVgSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 351 VKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMG 430
Cdd:PLN02456 321 VKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15231130 431 FPPEFFTVLFAVPRMAGYLSHWRESLDDPDTRIMRPQQAYTGVWMRHYEPVRERT 485
Cdd:PLN02456 401 FPEEFFTVLFAVSRAAGYLSQWDEALGLPDERIMRPKQVYTGEWLRHYCPKAERT 455
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
71-480 |
0e+00 |
|
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: 846.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 71 EHGTVKAVDLKKITTGKDDKGLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQ 150
Cdd:cd06115 1 DHGTVKATDFKKIKAGKDDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 151 SQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFHPDANPALSGQDIYKSKQVRDKQIVRILGKAPT 230
Cdd:cd06115 81 SQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEANPALAGQDIYKNKQVRDKQIVRILGKAPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 231 IAAAAYLRTAGRPPVLPSANLSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYT 310
Cdd:cd06115 161 IAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 311 ACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRD 390
Cdd:cd06115 241 AVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 391 PLIEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPDTRIMRPQQAY 470
Cdd:cd06115 321 PLIEIAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLY 400
|
410
....*....|
gi 15231130 471 TGVWMRHYEP 480
Cdd:cd06115 401 TGVWLRHYVP 410
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
91-472 |
0e+00 |
|
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: 685.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 91 GLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGV 170
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 171 LDIIQSMPHDAHPMGVLVSAMSALSIFHPDANPALSGQDIYKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSAN 250
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 251 LSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEA 330
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 331 VLKMLAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFV 410
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEDEYFV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231130 411 KRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPDTRIMRPQQAYTG 472
Cdd:cd06107 321 SRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
84-484 |
0e+00 |
|
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440141 [Multi-domain] Cd Length: 387 Bit Score: 570.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 84 TTGKDDKGLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQH 163
Cdd:COG0372 2 SSEIDIRAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 164 SAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFHPDANPalsgqdiyKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRP 243
Cdd:COG0372 82 RELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD--------IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 244 PVLPSANLSYSENFLYMLdsmgnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPL 323
Cdd:COG0372 154 PVYPDPDLSYAENFLYML-----FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 324 HGGANEAVLKMLAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAA 403
Cdd:COG0372 229 HGGANEAVLEMLEEIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 404 LSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPVRE 483
Cdd:COG0372 309 LEDEYFIEKKLYPNVDFYSGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRA--DNRIIRPRQIYVGPEDRDYVPIEE 386
|
.
gi 15231130 484 R 484
Cdd:COG0372 387 R 387
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
76-472 |
0e+00 |
|
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: 552.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 76 KAVDLKKITTgkdDKGLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLAD 155
Cdd:cd06114 11 KVIDISSLRK---KTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 156 WEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFHPDANPALSGQDiykskqvRDKQIVRILGKAPTIAAAA 235
Cdd:cd06114 88 FREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQ-------RELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 236 YLRTAGRPPVLPSANLSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGA 315
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 316 VGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKR--KMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGR-DPL 392
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDpfRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKdDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 393 IEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPDTRIMRPQQAYTG 472
Cdd:cd06114 321 LEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYTG 400
|
|
| gltA |
PRK05614 |
citrate synthase; |
50-472 |
0e+00 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 543.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 50 LKGNLTIVDerTGKKYQVPVSEhGTV--KAVDLKKITTgkdDKGLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIE 127
Cdd:PRK05614 4 KKATLTLNG--GEASVELPILK-GTLgpDVIDIRKLYG---STGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 128 ELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFHPDAnpalsg 207
Cdd:PRK05614 78 QLAEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDS------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 208 QDIYKSKQvRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHA 287
Cdd:PRK05614 152 LDINDPEH-REIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 288 EHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKR--KMSGFGHRV 365
Cdd:PRK05614 231 DHEQNASTSTVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDgfRLMGFGHRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 366 YKNYDPRAKVIKKLADEVFSIVG-RDPLIEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPR 444
Cdd:PRK05614 311 YKNYDPRAKIMRETCHEVLKELGlNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALAR 390
|
410 420
....*....|....*....|....*...
gi 15231130 445 MAGYLSHWRESLDDPDTRIMRPQQAYTG 472
Cdd:PRK05614 391 TVGWIAHWNEMHSDPEQKIGRPRQLYTG 418
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
97-470 |
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: 540.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 97 PGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQS 176
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 177 MPHDAHPMGVLVSAMSALSIFHPDANpalsgqdiYKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSEN 256
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFAR--------DKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 257 FLYMLDSMgnrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLA 336
Cdd:cd06118 153 FLYMLFGE-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 337 EIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFvkRKLYP 416
Cdd:cd06118 228 EIGTPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVLGE--KGIYP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15231130 417 NVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPdTRIMRPQQAY 470
Cdd:cd06118 306 NVDFYSGVVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENN-QRLIRPRAEY 358
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
91-481 |
0e+00 |
|
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: 535.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 91 GLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGV 170
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 171 LDIIQSMPHDAHPMGVLVSAMSALSIFHPDAnpalsgQDIYKSKQvRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSAN 250
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEA------KNIGDEEQ-RNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 251 LSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEA 330
Cdd:cd06116 154 LSYTGNFLSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 331 VLKMLAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFV 410
Cdd:cd06116 234 VLRMLQQIGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDEYFI 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231130 411 KRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPDTRIMRPQQAYTGVWMRHYEPV 481
Cdd:cd06116 314 SRKLYPNVDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
98-466 |
0e+00 |
|
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: 522.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 98 GYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSM 177
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 178 PHDAHPMGVLVSAMSALSIFHPDANpalSGQDIYKSKQVRDkqivRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENF 257
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEAI---SDKADYWENALRD----DLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 258 LYMLdsmgnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAE 337
Cdd:pfam00285 154 LYML-----FGYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 338 IGTAENIPDFIEGVKNR-KRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFVKRKLYP 416
Cdd:pfam00285 229 IGSPDEVEEYIRKVLNKgKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEDLYFVEKNLYP 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15231130 417 NVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLddPDTRIMRP 466
Cdd:pfam00285 309 NVDFYSGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQL--ADNRIIRP 356
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
62-478 |
1.59e-160 |
|
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: 461.94 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 62 GKKYQVPVSEhGTV--KAVDLKKITTgkdDKGLKLYDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVA 139
Cdd:TIGR01798 1 NKSVELPIYS-GTLgpDVIDIRKLYK---QTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 140 YLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFHPDAnpalsgQDIYKSKQvRDK 219
Cdd:TIGR01798 77 YLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDA------LDINDPRH-REI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 220 QIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLDSMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAAR 299
Cdd:TIGR01798 150 SAIRLIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 300 HLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKR--KMSGFGHRVYKNYDPRAKVIK 377
Cdd:TIGR01798 230 LAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDpfRLMGFGHRVYKNYDPRAKVMR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 378 KLADEVFSIVGR--DPLIEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRES 455
Cdd:TIGR01798 310 ETCHEVLKELGLhdDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEM 389
|
410 420
....*....|....*....|...
gi 15231130 456 LDDPDTRIMRPQQAYTGVWMRHY 478
Cdd:TIGR01798 390 ISDPGQKIGRPRQLYTGETQRDY 412
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
95-485 |
4.99e-149 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 431.30 E-value: 4.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 95 YDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDII 174
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 175 QSMPHDAHPMGVLVSAMSALSIFHPDanpalsgQDIYKSKQVRDkQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYS 254
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSR-------RALDDPEYIRD-AVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 255 ENFLYMLDSMgnrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKM 334
Cdd:PRK14036 156 ANFLYMLTER-----EPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 335 LAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAAlsDEYFVKRKL 414
Cdd:PRK14036 231 LEEIGSVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVA--EERLGPKGI 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231130 415 YPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPVRERT 485
Cdd:PRK14036 309 YPNVDFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLG--ANRIFRPTQIYTGSHNRRYIPLEERS 377
|
|
| citrate_synt_like_1_1 |
cd06112 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
95-481 |
2.91e-138 |
|
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: 403.73 E-value: 2.91e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 95 YDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDII 174
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 175 QSMPHDAHPMGVLVSAMSALSIFHPDanPALSGQDIYKSKQVrdkqIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYS 254
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPK--PEVLKPNPDYIDAA----TVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 255 ENFLYMLDSMgnrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKM 334
Cdd:cd06112 155 ENFLYMLFGE-----EPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 335 LAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGR-DPLIEVAVALEKAALsdEYFVKRK 413
Cdd:cd06112 230 LEEIGSPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCE--ELLGHKG 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231130 414 LYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPV 481
Cdd:cd06112 308 VYPNVDFYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLG--DNRIFRPTQIYIGEIDRKYVPL 373
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
107-484 |
1.77e-130 |
|
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: 383.64 E-value: 1.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGV 186
Cdd:TIGR01800 11 TALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHPMDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 187 LVSAMSALSIFHPDANPalsgqdiYKSKQVRDKQIvRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLDsmGN 266
Cdd:TIGR01800 91 LRTAVSYLGALDPEKFG-------HTPEEARDIAI-RLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLH--GE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 267 rsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPD 346
Cdd:TIGR01800 161 ---EPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 347 FIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSdeyfvKRKLYPNVDFYSGLIY 426
Cdd:TIGR01800 238 WIRKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231130 427 RAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:TIGR01800 313 YMMGIPTDLFTPIFAMSRVTGWTAHIIEQVE--NNRLIRPRADYVGPEERKYVPIEER 368
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
97-470 |
1.99e-128 |
|
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: 374.73 E-value: 1.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 97 PGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSqsqladweftvsqhsavpqgvldiiqs 176
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPS--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 177 mphdahpmgvlvsamsalsifhpdanpalsgqdiykskqvrdkqivrilgkaptiaaaaylrtagrppvlpsanlsYSEN 256
Cdd:cd06101 54 ----------------------------------------------------------------------------YAEN 57
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 257 FLYMLDSMgnrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLA 336
Cdd:cd06101 58 FLYMLGGE-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLE 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 337 EIGTAENIPDFIEGVKNR--KRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYFvkRKL 414
Cdd:cd06101 133 EIGTPKNEPAEAYIRKKLnsKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYE--KKL 210
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231130 415 YPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPdTRIMRPQQAY 470
Cdd:cd06101 211 YPNVDFYSGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDG-QRIIRPRAEY 265
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
106-472 |
7.04e-126 |
|
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: 371.61 E-value: 7.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 106 RSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMG 185
Cdd:cd06110 10 DSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 186 VLVSAMSALSIFHPDANPalsgqdiyKSKQVRDKQIVRILGKAPTIAAA-AYLRTaGRPPVLPSANLSYSENFLYMLDsm 264
Cdd:cd06110 90 VLRTAVSALALYDPEADD--------MSREANLRKAIRLIAKMPTIVAAfHRIRN-GLEPVAPDPDLSHAANFLYMLT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 265 GNrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENI 344
Cdd:cd06110 159 GE---KPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 345 PDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSdeyfvKRKLYPNVDFYSGL 424
Cdd:cd06110 236 AAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRD-----EKGLNPNVDFYSAS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15231130 425 IYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPdtRIMRPQQAYTG 472
Cdd:cd06110 311 VYYMLGIPVDLFTPIFAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
107-484 |
2.54e-113 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 340.06 E-value: 2.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGV 186
Cdd:NF041157 15 TSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALAM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 187 LVSAMSALSifhpdanpalSGQDIYKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLdsmgn 266
Cdd:NF041157 95 METAFSALA----------SIENYKWNKENDREKALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRAT----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 267 RSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPD 346
Cdd:NF041157 160 FGRKPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 347 -FIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALsdEYFVKRKLYPNVDFYSGLI 425
Cdd:NF041157 240 wFNENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPNTDFYSGIV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231130 426 YRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDpDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:NF041157 318 FYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEE-QHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
252-470 |
4.79e-110 |
|
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: 325.83 E-value: 4.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 252 SYSENFLYMLDSMgnrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAV 331
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 332 LKMLAEIGTAENIPDFIEGVK--NRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDEYF 409
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKklESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVLYE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231130 410 vkRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPdTRIMRPQQAY 470
Cdd:cd06099 156 --KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDN-FKIIRPRSEY 213
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
107-476 |
1.70e-94 |
|
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: 291.24 E-value: 1.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGV 186
Cdd:cd06111 11 TAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 187 LVSAMSALSIFHPDAnpalsgqDIYKSKQVRDKQIvRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMldSMGN 266
Cdd:cd06111 91 LRTAVSVLGAEDSET-------DDSSPDANLAKAI-RLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHM--CFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 267 rsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPD 346
Cdd:cd06111 161 ---VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 347 FIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAAlsdeyFVKRKLYPNVDFYSGLIY 426
Cdd:cd06111 238 WMLDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAM-----VAAKGIKPNLDFPAGPAY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15231130 427 RAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMR 476
Cdd:cd06111 313 YLMGFDIDFFTPIFVMARITGWTAHIMEQRA--DNALIRPLSEYNGPEQR 360
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
107-484 |
6.61e-94 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 290.13 E-value: 6.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIDGDEgiLRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHD-AHPMG 185
Cdd:PRK14034 15 SSVSSIIDDT--LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDLKkVHPMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 186 VLVSAMSALSIFHPDAnpalsgqDIYKSKQVRDKQIvRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLDSMg 265
Cdd:PRK14034 93 VLRTAISMLGLYDEEA-------EIMDEEANYRKAV-RLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYMLNGE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 266 nrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIP 345
Cdd:PRK14034 164 ----EPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 346 DFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSDeyfvkRKLYPNVDFYSGLI 425
Cdd:PRK14034 240 SYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKE-----KGLPPNVDFYSASV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231130 426 YRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:PRK14034 315 YHCLGIDHDLFTPIFAISRMSGWLAHILEQYE--NNRLIRPRADYVGPTHQVYVPIEER 371
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
105-472 |
7.81e-94 |
|
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: 289.21 E-value: 7.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 105 VRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMpHDAHPM 184
Cdd:cd06109 9 AETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL-AGLDPM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 185 GVLVSAMSALsifhPDANpalsgqdiykskqvRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMLdsm 264
Cdd:cd06109 88 DALRALLALL----PDSP--------------DLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRML--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 265 gnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENI 344
Cdd:cd06109 147 --TGEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 345 PDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFsivGRDPLIEVAVALEKAALS--DEYFVKRKLYPNVDFYS 422
Cdd:cd06109 225 EAWLREALARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEQAALAllREYKPGRPLETNVEFYT 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15231130 423 GLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTG 472
Cdd:cd06109 302 ALLLEALGLPREAFTPTFAAGRTAGWTAHVLEQAR--TGRLIRPQSRYVG 349
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
119-477 |
8.51e-94 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 289.93 E-value: 8.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 119 LRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFH 198
Cdd:PRK14033 33 LTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDVVRTAVSYLGAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 199 PDANPALSGQDIYKSkqvrdkqiVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLYMldSMGNrsyKPNPRLARV 278
Cdd:PRK14033 113 PEADDSSPEANLAKA--------LRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHM--CFGE---VPEPEVVRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 279 LDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKRKM 358
Cdd:PRK14033 180 FEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAEWLRDALARKEKV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 359 SGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAalsdeyFVKRK-LYPNVDFYSGLIYRAMGFPPEFFT 437
Cdd:PRK14033 260 MGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKA------MAEATgIKPNLDFPAGPAYYLMGFDIDFFT 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15231130 438 VLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRH 477
Cdd:PRK14033 334 PIFVMSRITGWTAHIMEQRA--SNALIRPLSEYNGPEQRE 371
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
107-484 |
1.16e-90 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 282.02 E-value: 1.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGV 186
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 187 LVSAMSALSifhpdanpalSGQDIYKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYSENFLymLDSMGN 266
Cdd:PRK14037 96 MEAAFAALA----------SIDKNFKWKENDKEKAISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFL--LASFAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 267 rsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPD 346
Cdd:PRK14037 164 ---EPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 347 -FIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSivgRDP----LIEVAVALEKaaLSDEYFVKRKLYPNVDFY 421
Cdd:PRK14037 241 wFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIE---RNSeakkYFEIAQKLEE--LGIKQFGSKGIYPNTDFY 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231130 422 SGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDpDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:PRK14037 316 SGIVFYALGFPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
119-484 |
7.36e-90 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 279.72 E-value: 7.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 119 LRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQ----HSAVPQGVLdiIQSMPHdAHPMGVLVSAMSAL 194
Cdd:PRK14035 25 LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKymtlNDRVYQHFE--EYSTDH-VHPMTALRTSVSYL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 195 SIFHPDANPalsgqdiyKSKQVRDKQIVRILGKAPTIAAA-AYLRTaGRPPVLPSANLSYSENFLYMLdsmgnRSYKPNP 273
Cdd:PRK14035 102 AHFDPDAEE--------ESDEARYERAIRIQAKVASLVTAfARVRQ-GKEPLKPRPDLSYAANFLYML-----RGELPTD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 274 RLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKN 353
Cdd:PRK14035 168 IEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVDAYLDEKFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 354 RKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKaalsdeyFVKRK--LYPNVDFYSGLIYRAMGF 431
Cdd:PRK14035 248 NKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEK-------RMKEEkgLIPNVDFYSATVYHVMGI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15231130 432 PPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:PRK14035 321 PHDLFTPIFAVSRVAGWIAHILEQYK--DNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
95-472 |
8.53e-90 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 279.68 E-value: 8.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 95 YDPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDII 174
Cdd:PRK12349 5 FSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 175 QSMPHDAHPMGVLVSAMSALSIFHPDANPalsgqdiyKSKQVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLPSANLSYS 254
Cdd:PRK12349 85 KALPKETHPMDGLRTGVSALAGYDNDIED--------RSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 255 ENFLYMLdsMGNrsyKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKM 334
Cdd:PRK12349 157 ANFLYML--TGK---KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 335 LAEIGTAENIPDFIEGVKNRKRKMSGFGHRVY-KNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKaalsdeYFVKRK 413
Cdd:PRK12349 232 LLEAGTVEKFEELLQKKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEK------IMEKEK 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 414 -LYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTG 472
Cdd:PRK12349 306 gLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHA--NNRLFRPRVNYIG 363
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
107-481 |
2.33e-86 |
|
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: 270.33 E-value: 2.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 107 SSICYIdGDEGI-LRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMG 185
Cdd:cd06108 11 TAISTV-GKGGKgLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 186 VLVSAMSALSIFHPDANPAlSGQDIykskqvrdkqIVRILGKAPTIAAAAY-LRTAGRPPVLPSANLSYSENFLYMLdsm 264
Cdd:cd06108 90 VMRTGCSMLGCLEPENEFS-QQYEI----------AIRLLAIFPSILLYWYhYSHSGKRIETETDEDSIAGHFLHLL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 265 gnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENI 344
Cdd:cd06108 156 --HGKKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 345 PDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKAALSdeyfvKRKLYPNVDFYSGL 424
Cdd:cd06108 234 EQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSAS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231130 425 IYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPV 481
Cdd:cd06108 309 AYHFCGIPTELFTPIFVMSRVTGWAAHIMEQRA--NNRLIRPSADYIGPEPRPFVPI 363
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
119-484 |
9.51e-72 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 232.89 E-value: 9.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 119 LRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSALSIFH 198
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 199 PDAnpalsgqDIYKSKQVRDKqIVRILGKAPTIAAAAYLRTA-GRPPVLPSANLSYSENFLYMLdsmgnRSYKPNPRLAR 277
Cdd:PRK12351 112 PEK-------EDHNFSGARDI-ADRLLASLGSILLYWYHYSHnGRRIEVETDDDSIGGHFLHLL-----HGKKPSESWVK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 278 VLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPDFIEGVKNRKRK 357
Cdd:PRK12351 179 AMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIRRRVENKEV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 358 MSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEkAALSDEyfvkRKLYPNVDFYSGLIYRAMGFPPEFFT 437
Cdd:PRK12351 259 VIGFGHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLE-TVMWEE----KKMFPNLDWFSAVSYHMMGVPTAMFT 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15231130 438 VLFAVPRMAGYLSHWRESldDPDTRIMRPQQAYTGVWMRHYEPVRER 484
Cdd:PRK12351 334 PLFVISRTTGWAAHVIEQ--RQDNKIIRPSANYTGPEDRKFVPIEKR 378
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
115-484 |
4.56e-69 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 228.25 E-value: 4.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 115 DEGILRYRGYPIEELAESST------FIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLD--IIQSMPHDAhpMGV 186
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRdmILKAPSKDI--MNS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 187 LVSAMSALSIFhpDANPalsgQDIYKSKQVRdkQIVRILGKAPTIAAAAY----LRTAGRPPVL--PSANLSYSENFLYM 260
Cdd:PRK14032 142 LARSVLALYSY--DDNP----DDTSIDNVLR--QSISLIARFPTLAVYAYqayrHYHDGKSLYIhpPKPELSTAENILYM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 261 LdsMGNRSYKPNPrlARVLDILFILHAEHEM-NCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIg 339
Cdd:PRK14032 214 L--RPDNKYTELE--ARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDI- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 340 tAENIPDF--IEGVKNRKRKM------------SGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEKaaLS 405
Cdd:PRK14032 289 -KENVKDWedEDEIADYLTKIlnkeafdksgliYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEK--LA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 406 DEYFVK-RKLY----PNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPDtRIMRPqqAYTGVWM-RHYE 479
Cdd:PRK14032 366 PELIAEeRGIYkgvsANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGG-KIIRP--AYKSVLErREYV 442
|
....*
gi 15231130 480 PVRER 484
Cdd:PRK14032 443 PLEER 447
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
96-472 |
2.07e-66 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 218.29 E-value: 2.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 96 DPGYLNTAPVRSSICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLM---YGNLPSQSQladwEFTVSQHSAVpqgvld 172
Cdd:PRK12350 2 VPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVdgrFGPGLPPAE----PFPLPVHLGD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 173 iiqsmphdahpmgVLVSAMSALSIFHP-DA-NPALSGQDIykskQVRDkQIVRilgkAPTIAAAAYLRTA--GRPPVLPS 248
Cdd:PRK12350 72 -------------ARVDVQAALAMLAPvWGfRPLLDIDDL----TARL-DLAR----ASVMALSAVAQSArgIGQPAVPQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 249 ANLSYSENFLYMLdsMGNRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGAN 328
Cdd:PRK12350 130 REIDHAATILERF--MGRWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 329 EAVLKMLAEIGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSivgrdPLIEVAVALEKAALSD-- 406
Cdd:PRK12350 208 ARVLPMLDAVERTGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGA-----PRYEVAEAVEQAALAElr 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231130 407 EYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTG 472
Cdd:PRK12350 283 ERRPDRPLETNVEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKR--TGRLVRPSARYVG 346
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
101-481 |
3.57e-65 |
|
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: 215.48 E-value: 3.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 101 NTApvrssICYIDGDEGILRYRGYPIEELAESSTFIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHD 180
Cdd:cd06117 10 NTA-----LCTVGRSGNDLHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 181 AHPMGVLVSAMSALSIFHP--DANPALSGQDIykskqvrdkqIVRILGKAPTIAAAAYLRT-AGRPPVLPSANLSYSENF 257
Cdd:cd06117 85 AHPMDVMRTGVSVLGCVLPekEDHPVSGARDI----------ADRLMASLGSILLYWYHYShNGKRIEVETDDDSIGGHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 258 LYMLdsmgnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAE 337
Cdd:cd06117 155 LHLL-----HGEKPSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 338 IGTAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDPLIEVAVALEkAALSDEyfvkRKLYPN 417
Cdd:cd06117 230 YESADEAEADIRRRVENKEVVIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLE-TVMWEE----KKMFPN 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231130 418 VDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDdpDTRIMRPQQAYTGVWMRHYEPV 481
Cdd:cd06117 305 LDWFSAVSYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQ--DGKIIRPSANYTGPEDLKFVPI 366
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
115-473 |
7.39e-65 |
|
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: 215.98 E-value: 7.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 115 DEGILRYRGYPIEELAESST------FIEVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQG-VLDIIQSMPhDAHPMGVL 187
Cdd:cd06113 34 CPGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNfVEDVILKAP-SKDIMNKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 188 vsAMSALSIFHPDANPalsgQDIYKSKQVRdkQIVRILGKAPTIAAAAYL----RTAGRPPVL--PSANLSYSENFLYML 261
Cdd:cd06113 113 --QRSVLALYSYDDKP----DDISLENVLR--QSIQLIARLPTIAVYAYQakrhYYDGESLYIhhPQPELSTAENILSML 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 262 DSmgNRSYkpNPRLARVLDILFILHAEHEM-NCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIgt 340
Cdd:cd06113 185 RP--DKKY--TELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDI-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 341 AENIPDF--IEGVKNRKRKM------------SGFGHRVYKNYDPRAKVIKKLADEVFSIVGRDP---LIEVAVALEKAA 403
Cdd:cd06113 259 KENVKDWtdEDEVRAYLRKIlnkeafdksgliYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEefaLYERIERLAPEV 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 404 LSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDpDTRIMRPqqAYTGV 473
Cdd:cd06113 339 IAEERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEELLN-SGRIIRP--AYKYV 405
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
69-472 |
5.02e-54 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 188.04 E-value: 5.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 69 VSEHGTVKavdLKKITTGKDDKGLKLYDPGYlntapvrSSICYIDGDEGIlRYRGYPIEEL---------AESSTFIEVA 139
Cdd:PRK09569 22 VKEFGSVV---IDEVTIEQCIGGARDIRSLV-------TDISYLDPQEGI-RFRGKTIPETfealpkapgSEYPTVESFW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 140 YLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDAHPMGVLVSAMSAL---SIFHPDANPA-LSGQDIYKSKQ 215
Cdd:PRK09569 91 YFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMqreSKFAKFYNEGkFNKMDAWEYMY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 216 vrdKQIVRILGKAPTIAAAAY-LRTAGRPPVLPSANLSYSENFLYMLDSmgnrsykpNPRLARVLDILFILHAEHEMNCS 294
Cdd:PRK09569 171 ---EDASDLVARIPVIAAYIYnLKYKGDKQIPSDPELDYGANFAHMIGQ--------PKPYKDVARMYFILHSDHESGNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 295 TAAARHLASSGV-DVYTACAGAVGALYGPLHGGANEAVL----KMLAEIG----TAENIPDFIEGVKNRKRKMSGFGHRV 365
Cdd:PRK09569 240 SAHTTHLVASALsDAYYSYSAGLNGLAGPLHGLANQEVLgwiqQFQEKLGgeepTKEQVEQALWDTLNAGQVIPGYGHAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 366 YKNYDPRAKVIKKLADEVFSivgRDPLIEVAVALEKAA--LSDEYFVKRKLYPNVDFYSGLIYRAMGFP-PEFFTVLFAV 442
Cdd:PRK09569 320 LRKTDPRYTAQREFCLKHLP---DDPLFKLVAMIFEVApgVLTEHGKTKNPWPNVDAQSGVIQWYYGVKeWDFYTVLFGV 396
|
410 420 430
....*....|....*....|....*....|..
gi 15231130 443 PRMAGYLSH--WRESLDDPdtrIMRPQQAYTG 472
Cdd:PRK09569 397 GRALGVMANitWDRGLGYA---IERPKSVTTE 425
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
111-466 |
1.41e-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: 156.69 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 111 YIDGDEGIlRYRGYPIEELAE--------SSTFIE-VAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSMPHDA 181
Cdd:cd06103 52 VLDPDEGI-RFRGKTIPECQEllpkadggGEPLPEgLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 182 HPMGVLVSAMSAL---SIFhpdanpalsgQDIYKSKQVRDKQI--------VRILGKAPTIAAAAYLRTAGRPPVLPSAN 250
Cdd:cd06103 131 HPMTQLSAAILALqseSKF----------AKAYAEGKINKTTYweyvyedaMDLIAKLPVVAAKIYRRKYRKGGEIGAID 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 251 LS--YSENFLYMldsMGNrsykPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGV-DVYTACAGAVGALYGPLHGGA 327
Cdd:cd06103 201 SKldWSANFAHM---LGY----EDEEFTDLMRLYLTLHSDHEGGNVSAHTSHLVGSALsDPYLSFSAALNGLAGPLHGLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 328 NEAVL----KMLAEIG---TAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFsivGRDPLIEVAVALE 400
Cdd:cd06103 274 NQEVLkwllKMQKELGkdvSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFALKHL---PDDPLFKLVAQCY 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231130 401 KAA---LSDEYFVKRKlYPNVDFYSGLIYRAMGFP-PEFFTVLFAVPRMAGYLSH--WRESLDDPdtrIMRP 466
Cdd:cd06103 351 KIIpgvLKEHGKVKNP-YPNVDAHSGVLLQHYGMTePQYYTVLFGVSRALGVLAQlvWSRALGLP---IERP 418
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
112-477 |
4.42e-39 |
|
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: 147.13 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 112 IDGDEGIlRYRGYPI--------------EELAESstfieVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSM 177
Cdd:cd06105 53 LDPEEGI-RFRGLSIpecqkllpkapggeEPLPEG-----LFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 178 PHDAHPMGVLVSAMSALsifHPDANPALSGQD-IYKSK--QVRDKQIVRILGKAPTIAAAAYLRTAGRPPVLP-SANLSY 253
Cdd:cd06105 127 PTNLHPMSQLSAAITAL---NSESKFAKAYAEgIHKSKywEYVYEDSMDLIAKLPCVAAKIYRNLYRGGKIIAiDSNLDW 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 254 SENFLYMLdsmgnrSYKpNPRLARVLDILFILHAEHEMNCSTAAARHLASSGV-DVYTACAGAVGALYGPLHGGANEAVL 332
Cdd:cd06105 204 SANFANML------GYT-DPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSALsDPYLSFAAAMNGLAGPLHGLANQEVL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 333 ----KMLAEIG---TAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLA------DEVFSIVGRdpLIEVA--V 397
Cdd:cd06105 277 vwltKLQKEVGkdvSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlpnDPLFKLVSQ--LYKIVppV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 398 ALEKAALSDEyfvkrklYPNVDFYSGLIYRAMGFPPE-FFTVLFAVPRMAGYLSH--WRESLDDPdtrIMRPQQAYTGVW 474
Cdd:cd06105 355 LTEQGKAKNP-------WPNVDAHSGVLLQYYGLTEMnYYTVLFGVSRALGVLSQliWDRALGLP---LERPKSVSTDGL 424
|
...
gi 15231130 475 MRH 477
Cdd:cd06105 425 EKL 427
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
112-467 |
6.22e-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: 130.32 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 112 IDGDEGIlRYRGYPIEE--------------LAESstfieVAYLLMYGNLPSQSQLADWEFTVSQHSAVPQGVLDIIQSM 177
Cdd:cd06106 53 LDAEEGI-RFHGKTIPEcqkelpkapiggemLPES-----MLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 178 PHDAHPMGVLVSAMSALSifHPDANPALSGQDIYKSKQVRD--KQIVRILGKAPTIAAAAYLRTAGRPPVLP--SANLSY 253
Cdd:cd06106 127 PKTLHPMTQLSIGVAALN--HDSKFAAAYEKGIKKTEYWEPtlEDSLNLIARLPALAARIYRNVYGEGHGLGkiDPEVDW 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 254 SENFLYMLdSMGNrsykpNPRLARVLDILFILHAEHEMNCSTAAARHLASSGV-DVYTACAGAVGALYGPLHGGANEAVL 332
Cdd:cd06106 205 SYNFTSML-GYGD-----NLDFVDLLRLYIALHGDHEGGNVSAHTTHLVGSALsDPYLSYSAGLMGLAGPLHGLAAQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 333 K----MLAEIG---TAENIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLA--------DEVFSIVGRdpLIEVAV 397
Cdd:cd06106 279 RwileMQKNIGskaTDQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAqtrpelenDPVVQLVQK--LSEIAP 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231130 398 ALEKaalsdEYFVKRKLYPNVDFYSGLIYRAMGF-PPEFFTVLFAVPRMAGYLSH--WRESLDDPdtrIMRPQ 467
Cdd:cd06106 357 GVLT-----EHGKTKNPFPNVDAASGVLFYHYGIrEFLYYTVIFGVSRALGPLTQlvWDRILGLP---IERPK 421
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
250-459 |
1.33e-30 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 119.59 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 250 NLSYSENFLYMLdsmgnRSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALyGPLHGGANE 329
Cdd:PRK06224 34 KLSFTDMIFLLL-----RGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLAL-GSVHGGAGE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 330 AVLKMLAEI-----------GTAENIpdfIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVfSIVGRdpLIEVAVA 398
Cdd:PRK06224 108 QAAELLQEIaaaadagadldAAARAI---VAEYRAAGKRVPGFGHPLHKPVDPRAPRLLALAREA-GVAGR--HCRLAEA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231130 399 LEKAALSDeyfVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDP 459
Cdd:PRK06224 182 LEAALAAA---KGKPLPLNVDGAIAAILADLGFPPALARGLFVISRAAGLVAHVWEELQQP 239
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
267-472 |
7.77e-29 |
|
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: 115.44 E-value: 7.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 267 RSYKPNPRLARVLDILFILHAEHEMNCSTAAARHLASSGVDVYTACAGAVGALYGPLHGGANEAVLKMLAEIGTAENIPD 346
Cdd:cd06102 89 RAWGLDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 347 FIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVGR--DPLIEVAVALEKAAlsdeyfvkrklyPNVDFYSGL 424
Cdd:cd06102 169 AVRERLRRGEALPGFGHPLYPDGDPRAAALLAALRPLGPAAPPaaRALIEAARALTGAR------------PNIDFALAA 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231130 425 IYRAMGFPPEFFTVLFAVPRMAGYLSHWRESLDDPdtRIMRPQQAYTG 472
Cdd:cd06102 237 LTRALGLPAGAAFALFALGRSAGWIAHALEQRAQG--KLIRPRARYVG 282
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
270-454 |
4.45e-27 |
|
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 108.81 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 270 KPNPRLARVLDILFILHAEHEMN-CSTAAARHLASSGVDVyTACAGAVGAL-YGPLHGGANEAVLKMLAEI-----GTAE 342
Cdd:cd06100 25 LPTPYEARLLEALLVALADHGPAtPSAHAARLTASAGPED-LQSAVAAGLLgIGDRFGGAGEGAARLFKEAvdsgdALDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 343 NIPDFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIKKLADEVFSIVgrdPLIEVAVALEKAALSDeyfvKRKLYP-NVDFY 421
Cdd:cd06100 104 AAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPAG---PHLDYALAVEKALTAA----KGKPLPlNVDGA 176
|
170 180 190
....*....|....*....|....*....|...
gi 15231130 422 SGLIYRAMGFPPEFFTVLFAVPRMAGYLSHWRE 454
Cdd:cd06100 177 IAAILLDLGFPPGALRGLFVLGRSPGLIAHALE 209
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
273-419 |
1.57e-04 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 44.43 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231130 273 PRLA-RVLDILFILHAEHEMNCSTAAARHLAS-SGVDVYTACAGAVGALyGPLHGGANEAVLKMLAEIGTAENIP-DFIE 349
Cdd:PLN02522 396 PRYCtKFIEMCIMLCADHGPCVSGAHNTIVTArAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPyEFVE 474
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231130 350 GVKNRKRKMSGFGHRVYK--NYDPRAKVIKKLADEVFSIVgrdPLIEVAVALEKAALSDeyfvKRKLYPNVD 419
Cdd:PLN02522 475 GMKKKGIRVPGIGHRIKSrdNRDKRVELLQKYARTHFPSV---KYMEYAVQVETYTLSK----ANNLVLNVD 539
|
|
| |
