|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02456 |
PLN02456 |
citrate synthase |
29-478 |
0e+00 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 783.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 29 AIEPWCTSAHITAAPHGSLKGNLKIVDERTGNEYQVPVSEHGTVKTVDLKKITTGKDDKGLNLYDPGYLNTAPVRSSISY 108
Cdd:PLN02456 1 AAAVSCTSSSLSRAAPGGGSGSLTIVDNRTGKDYESPLSELGPVQAERLKKIKAGKDDLGLKTVDPGYRNTAPVLSEISL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 109 IDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAM 188
Cdd:PLN02456 81 IDGDEGILRFRGYPIEELAEKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 189 SALSIFYPDANPSLMGLGVYKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVESMGDRSYKP 268
Cdd:PLN02456 161 MALSTFSPDANAYLRGQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 269 NPRLARVLDILFILQAEHEMNCSTAAARHL-SSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPEFIES 347
Cdd:PLN02456 241 DPRLARLLDLYFIIHADHEGGCSTAAARHLvGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 348 VKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFVKRKLYPNVDFYSGLINRAMG 427
Cdd:PLN02456 321 VKNSKKVLPGFGHRVYKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15231128 428 IPSSF----TAVSRIAGYLSHWRESLDDPDTKIMRPQQVYTGAGIRHYETVRERT 478
Cdd:PLN02456 401 FPEEFftvlFAVSRAAGYLSQWDEALGLPDERIMRPKQVYTGEWLRHYCPKAERT 455
|
|
| AthCS_per_like |
cd06115 |
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ... |
68-472 |
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: 720.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 68 EHGTVKTVDLKKITTGKDDKGLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQ 147
Cdd:cd06115 1 DHGTVKATDFKKIKAGKDDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 148 RQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFYPDANPSLMGLGVYKSKQVRDKQIVRVLGQAPT 227
Cdd:cd06115 81 SQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEANPALAGQDIYKNKQVRDKQIVRILGKAPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 228 IAAAAYLRKAGKPPVQPLSNLSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYT 307
Cdd:cd06115 161 IAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 308 AVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRD 387
Cdd:cd06115 241 AVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 388 PLVEVGDALEKAALSDEYFVKRKLYPNVDFYSGLINRAMGIPSSFT----AVSRIAGYLSHWRESLDDPDTKIMRPQQVY 463
Cdd:cd06115 321 PLIEIAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFpvlfAIPRMAGYLAHWRESLDDPDTKIMRPQQLY 400
|
....*....
gi 15231128 464 TGAGIRHYE 472
Cdd:cd06115 401 TGVWLRHYV 409
|
|
| EcCS_AthCS-per_like |
cd06107 |
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ... |
88-465 |
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: 592.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 88 GLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGV 167
Cdd:cd06107 1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 168 LDMIQSMPNDVHPVGALVTAMSALSIFYPDANPSLMGLGVYKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSN 247
Cdd:cd06107 81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHTGDLYQNNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 248 LSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEA 327
Cdd:cd06107 161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 328 TINMLSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFV 407
Cdd:cd06107 241 ALKMLREIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEDEYFV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231128 408 KRKLYPNVDFYSGLINRAMGIPSSF----TAVSRIAGYLSHWRESLDDPDTKIMRPQQVYTG 465
Cdd:cd06107 321 SRKLYPNVDFYSGFIYKALGFPPEFftvlFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
81-477 |
3.39e-179 |
|
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440141 [Multi-domain] Cd Length: 387 Bit Score: 506.94 E-value: 3.39e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 81 TTGKDDKGLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQN 160
Cdd:COG0372 2 SSEIDIRAKFTVDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 161 SAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFYPDANPslmglgvyKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKP 240
Cdd:COG0372 82 RELPEEVKEFLDGFPRDAHPMDVLRTAVSALGAFDPDADD--------IDPEARLEKAIRLIAKLPTIAAYAYRYRRGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 241 PVQPLSNLSYSENFLYMVesmgdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPL 320
Cdd:COG0372 154 PVYPDPDLSYAENFLYML-----FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 321 HGGAVEATINMLSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAA 400
Cdd:COG0372 229 HGGANEAVLEMLEEIGSPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 401 LSDEYFVKRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHYETVRE 476
Cdd:COG0372 309 LEDEYFIEKKLYPNVDFYSGIVYHALGIPTDmFTpifAISRVAGWIAHWLEQRA--DNRIIRPRQIYVGPEDRDYVPIEE 386
|
.
gi 15231128 477 R 477
Cdd:COG0372 387 R 387
|
|
| EcCS_like |
cd06114 |
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ... |
73-465 |
1.70e-175 |
|
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: 498.26 E-value: 1.70e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 73 KTVDLKKITTgkdDKGLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLAD 152
Cdd:cd06114 11 KVIDISSLRK---KTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQLQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 153 WEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFYPDAnpslmgLGVYKSKQvRDKQIVRVLGQAPTIAAAA 232
Cdd:cd06114 88 FREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDS------LDVNDPEQ-RELAAIRLIAKVPTIAAMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 233 YLRKAGKPPVQPLSNLSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGG 312
Cdd:cd06114 161 YRYSIGQPFIYPDNDLSYVENFLHMMFAVPYEPYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 313 VGAIYGPLHGGAVEATINMLSEIGTVENIPEFIESVKNKKR--RLSGFGHRIYKNYDPRGKVVKKLADEVFSILGR-DPL 389
Cdd:cd06114 241 IAALWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKDKNDpfRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKdDPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 390 VEVGDALEKAALSDEYFVKRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPDTKIMRPQQVYTG 465
Cdd:cd06114 321 LEIAMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEmFTvlfALGRTPGWIAQWREMHEDPELKIGRPRQLYTG 400
|
|
| gltA |
PRK05614 |
citrate synthase; |
69-466 |
2.05e-170 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 485.92 E-value: 2.05e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 69 HGTV--KTVDLKKITTgkdDKGLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPS 146
Cdd:PRK05614 23 KGTLgpDVIDIRKLYG---STGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQLAEKSDFLEVCYLLLYGELPT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 147 QRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFYPDAnpslmgLGVYKSKQvRDKQIVRVLGQAP 226
Cdd:PRK05614 100 AEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDS------LDINDPEH-REIAAIRLIAKMP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 227 TIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVY 306
Cdd:PRK05614 173 TLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTSTVRLAGSSGANPF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 307 TAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPEFIESVKNKKR--RLSGFGHRIYKNYDPRGKVVKKLADEVFSIL 384
Cdd:PRK05614 253 ACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNDgfRLMGFGHRVYKNYDPRAKIMRETCHEVLKEL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 385 G-RDPLVEVGDALEKAALSDEYFVKRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPDTKIMRP 459
Cdd:PRK05614 333 GlNDPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSmFTvifALARTVGWIAHWNEMHSDPEQKIGRP 412
|
....*..
gi 15231128 460 QQVYTGA 466
Cdd:PRK05614 413 RQLYTGY 419
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
94-463 |
9.01e-166 |
|
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: 471.70 E-value: 9.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 94 PGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQS 173
Cdd:cd06118 1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 174 MPNDVHPVGALVTAMSALSIFYPDANpslmglgvYKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSEN 253
Cdd:cd06118 81 LPKNAHPMDVLRTAVSALGSFDPFAR--------DKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 254 FLYMVESMgdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLS 333
Cdd:cd06118 153 FLYMLFGE-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 334 EIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFvkRKLYP 413
Cdd:cd06118 228 EIGTPENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVLGE--KGIYP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15231128 414 NVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPdTKIMRPQQVY 463
Cdd:cd06118 306 NVDFYSGVVYKALGFPTElFTplfAVSRAVGWLAHIIEYRENN-QRLIRPRAEY 358
|
|
| CaCS_like |
cd06116 |
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ... |
88-471 |
1.52e-165 |
|
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: 472.39 E-value: 1.52e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 88 GLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGV 167
Cdd:cd06116 1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 168 LDMIQSMPNDVHPVGALVTAMSALSIFYPDANPslmglgvYKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSN 247
Cdd:cd06116 81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKN-------IGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 248 LSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEA 327
Cdd:cd06116 154 LSYTGNFLSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 328 TINMLSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFV 407
Cdd:cd06116 234 VLRMLQQIGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDEYFI 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231128 408 KRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPDTKIMRPQQVYTGAGIRHY 471
Cdd:cd06116 314 SRKLYPNVDFYSGLIYQALGFPTEaFTvlfAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDY 381
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
95-459 |
2.04e-161 |
|
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: 460.82 E-value: 2.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 95 GYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSM 174
Cdd:pfam00285 1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 175 PNDVHPVGALVTAMSALSIFYPDAnpslmglgvYKSKQVRDKQIVR--VLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSE 252
Cdd:pfam00285 81 PRDAHPMAVLRAAVSALAAFDPEA---------ISDKADYWENALRddLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 253 NFLYMVesmgdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINML 332
Cdd:pfam00285 152 NFLYML-----FGYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEML 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 333 SEIGTVENIPEFIESVKNK-KRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFVKRKL 411
Cdd:pfam00285 227 EEIGSPDEVEEYIRKVLNKgKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEDLYFVEKNL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15231128 412 YPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLddPDTKIMRP 459
Cdd:pfam00285 307 YPNVDFYSGVLYHALGIPTDmFTplfAISRTAGWLAHWIEQL--ADNRIIRP 356
|
|
| cit_synth_I |
TIGR01798 |
citrate synthase I (hexameric type); This model describes one of several distinct but closely ... |
59-471 |
7.54e-147 |
|
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: 425.73 E-value: 7.54e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 59 GNEYQVPVSEhGTV--KTVDLKKITTgkdDKGLNLYDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVT 136
Cdd:TIGR01798 1 NKSVELPIYS-GTLgpDVIDIRKLYK---QTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 137 YLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFYPDAnpslmgLGVYKSKQvRDK 216
Cdd:TIGR01798 77 YLLLYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDA------LDINDPRH-REI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 217 QIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVESMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAAR 296
Cdd:TIGR01798 150 SAIRLIAKIPTLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 297 HLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPEFIESVKNKKR--RLSGFGHRIYKNYDPRGKVVK 374
Cdd:TIGR01798 230 LAGSSGANPFACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKDKNDpfRLMGFGHRVYKNYDPRAKVMR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 375 KLADEVFSILGR--DPLVEVGDALEKAALSDEYFVKRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRES 448
Cdd:TIGR01798 310 ETCHEVLKELGLhdDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSmFTvifALARTVGWISHWSEM 389
|
410 420
....*....|....*....|...
gi 15231128 449 LDDPDTKIMRPQQVYTGAGIRHY 471
Cdd:TIGR01798 390 ISDPGQKIGRPRQLYTGETQRDY 412
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
92-478 |
5.19e-132 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 386.62 E-value: 5.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 92 YDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMI 171
Cdd:PRK14036 4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 172 QSMPNDVHPVGALVTAMSALSIFYPDAnpslmglGVYKSKQVRDkQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYS 251
Cdd:PRK14036 84 KCFPETGHPMDALQASAAALGLFYSRR-------ALDDPEYIRD-AVVRLIAKIPTMVAAFQLIRKGNDPIQPRDDLDYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 252 ENFLYMvesMGDRsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINM 331
Cdd:PRK14036 156 ANFLYM---LTER--EPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 332 LSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAAlsDEYFVKRKL 411
Cdd:PRK14036 231 LEEIGSVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVA--EERLGPKGI 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231128 412 YPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHYETVRERT 478
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 ... |
92-471 |
4.84e-123 |
|
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: 363.67 E-value: 4.84e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 92 YDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMI 171
Cdd:cd06112 1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 172 QSMPNDVHPVGALVTAMSALSIFYPDANpSLMGLGVYKskqvrDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYS 251
Cdd:cd06112 81 KCFPETGHPMDMLQATVAALGMFYPKPE-VLKPNPDYI-----DAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 252 ENFLYMVesMGDrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINM 331
Cdd:cd06112 155 ENFLYML--FGE---EPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 332 LSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGR-DPLVEVGDALEKAALsdEYFVKRK 410
Cdd:cd06112 230 LEEIGSPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGElSKLYEIALEVERLCE--ELLGHKG 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231128 411 LYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHY 471
Cdd:cd06112 308 VYPNVDFYSGIVYKELGIPADlFTpifAVARVAGWLAHWKEQLG--DNRIFRPTQIYIGEIDRKY 370
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
104-477 |
4.29e-112 |
|
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: 335.49 E-value: 4.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGA 183
Cdd:TIGR01800 11 TALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHPMDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYPDANPSlmglgvyKSKQVRDKQIvRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVEsmGD 263
Cdd:TIGR01800 91 LRTAVSYLGALDPEKFGH-------TPEEARDIAI-RLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYMLH--GE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 264 rsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPE 343
Cdd:TIGR01800 161 ---EPTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 344 FIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSdeyfvKRKLYPNVDFYSGLIN 423
Cdd:TIGR01800 238 WIRKALENKERIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231128 424 RAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHYETVRER 477
Cdd:TIGR01800 313 YMMGIPTDlFTpifAMSRVTGWTAHIIEQVE--NNRLIRPRADYVGPEERKYVPIEER 368
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
103-465 |
2.78e-111 |
|
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: 333.09 E-value: 2.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 103 RSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVG 182
Cdd:cd06110 10 DSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 183 ALVTAMSALSIFYPDANPSLMGLGVYKSkqvrdkqiVRVLGQAPTIAAA-AYLRKaGKPPVQPLSNLSYSENFLYMVesm 261
Cdd:cd06110 90 VLRTAVSALALYDPEADDMSREANLRKA--------IRLIAKMPTIVAAfHRIRN-GLEPVAPDPDLSHAANFLYML--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 262 gdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENI 341
Cdd:cd06110 158 --TGEKPSEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 342 PEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSdeyfvKRKLYPNVDFYSGL 421
Cdd:cd06110 236 AAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRD-----EKGLNPNVDFYSAS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15231128 422 INRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPdtKIMRPQQVYTG 465
Cdd:cd06110 311 VYYMLGIPVDlFTpifAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
94-463 |
6.44e-107 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and form homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99855 [Multi-domain] Cd Length: 265 Bit Score: 318.49 E-value: 6.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 94 PGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSqrqladwefaisqnsavpqgvldmiqs 173
Cdd:cd06101 1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPS--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 174 mpndvhpvgalvtamsalsifypdanpslmglgvykskqvrdkqivrvlgqaptiaaaaylrkagkppvqplsnlsYSEN 253
Cdd:cd06101 54 ----------------------------------------------------------------------------YAEN 57
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 254 FLYMVESMgdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLS 333
Cdd:cd06101 58 FLYMLGGE-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLE 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 334 EIGTVENIPEFIESVK--NKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYFvkRKL 411
Cdd:cd06101 133 EIGTPKNEPAEAYIRKklNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYE--KKL 210
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231128 412 YPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPdTKIMRPQQVY 463
Cdd:cd06101 211 YPNVDFYSGVLYKAMGFPTElFTplfAVSRAVGWLAHLIEQREDG-QRIIRPRAEY 265
|
|
| Cit_synThplmales |
NF041157 |
citrate synthase; |
104-477 |
3.66e-99 |
|
citrate synthase;
Pssm-ID: 469069 Cd Length: 376 Bit Score: 302.70 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGA 183
Cdd:NF041157 15 TSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIRSLPRDSDALAM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYPdanpslmglgvYKSKQVRDK-QIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLymvESMG 262
Cdd:NF041157 95 METAFSALASIEN-----------YKWNKENDReKALKIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFL---RATF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 263 DRsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIP 342
Cdd:NF041157 161 GR--KPSEEEIKAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPDNVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 343 E-FIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALsdEYFVKRKLYPNVDFYSGL 421
Cdd:NF041157 239 KwFNENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPNTDFYSGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 422 INRAMGIP----SSFTAVSRIAGYLSHWRESLDDpDTKIMRPQQVYTGAGIRHYETVRER 477
Cdd:NF041157 317 VFYSLGFPvymfTSLFALSRVLGWLAHIIEYVEE-QHRLIRPRALYVGPEKRDFVPIDER 375
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
249-463 |
1.15e-90 |
|
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: 274.99 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 249 SYSENFLYMVESMgdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEAT 328
Cdd:cd06099 1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 329 INMLSEIGTVENIPEFIESVK--NKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDEYF 406
Cdd:cd06099 76 LKMLEEIGTPKNEPAEAYIRKklESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVLYE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231128 407 vkRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPdTKIMRPQQVY 463
Cdd:cd06099 156 --KKLYPNVDFYSGVLYKAMGFPTElFTplfAVARAVGWLAHLIEQLEDN-FKIIRPRSEY 213
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
102-465 |
5.98e-86 |
|
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: 267.63 E-value: 5.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 102 VRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMpNDVHPV 181
Cdd:cd06109 9 AETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPAL-AGLDPM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 182 GALVTAMSALsifyPDANpslmglgvykskqvRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVesm 261
Cdd:cd06109 88 DALRALLALL----PDSP--------------DLATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRML--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 262 gdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENI 341
Cdd:cd06109 147 --TGEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPENA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 342 PEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFsilGRDPLVEVGDALEKAALS--DEYFVKRKLYPNVDFYS 419
Cdd:cd06109 225 EAWLREALARGERLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEQAALAllREYKPGRPLETNVEFYT 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15231128 420 GLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTG 465
Cdd:cd06109 302 ALLLEALGLPREaFTptfAAGRTAGWTAHVLEQAR--TGRLIRPQSRYVG 349
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
104-477 |
1.72e-82 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 259.68 E-value: 1.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGA 183
Cdd:PRK14037 16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYpdanpslmglGVYKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLymvESMGD 263
Cdd:PRK14037 96 MEAAFAALASID----------KNFKWKENDKEKAISIIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFL---LASFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 264 RsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPE 343
Cdd:PRK14037 163 R--EPTAEEIKAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 344 -FIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSilgRDPLV----EVGDALEKaaLSDEYFVKRKLYPNVDFY 418
Cdd:PRK14037 241 wFNDKIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIE---RNSEAkkyfEIAQKLEE--LGIKQFGSKGIYPNTDFY 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231128 419 SGLINRAMGIP----SSFTAVSRIAGYLSHWRESLDDpDTKIMRPQQVYTGAGIRHYETVRER 477
Cdd:PRK14037 316 SGIVFYALGFPvymfTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEHREYVPIDKR 377
|
|
| DsCS_like |
cd06111 |
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ... |
104-469 |
5.67e-82 |
|
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: 258.11 E-value: 5.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGA 183
Cdd:cd06111 11 TAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYPDANPSlmglgvyKSKQVRDKQIvRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVesMGD 263
Cdd:cd06111 91 LRTAVSVLGAEDSETDDS-------SPDANLAKAI-RLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMC--FGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 264 rsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPE 343
Cdd:cd06111 161 ---VPSPEVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 344 FIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAAlsdeyFVKRKLYPNVDFYSGLIN 423
Cdd:cd06111 238 WMLDALARKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMYDALEDAM-----VAAKGIKPNLDFPAGPAY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15231128 424 RAMGIP-SSFT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIR 469
Cdd:cd06111 313 YLMGFDiDFFTpifVMARITGWTAHIMEQRA--DNALIRPLSEYNGPEQR 360
|
|
| PRK12349 |
PRK12349 |
citrate synthase; |
92-470 |
4.58e-80 |
|
citrate synthase;
Pssm-ID: 237069 [Multi-domain] Cd Length: 369 Bit Score: 253.49 E-value: 4.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 92 YDPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMI 171
Cdd:PRK12349 5 FSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVFNIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 172 QSMPNDVHPVGALVTAMSALSIFYPDANPslmglgvyKSKQVRDKQIVRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYS 251
Cdd:PRK12349 85 KALPKETHPMDGLRTGVSALAGYDNDIED--------RSLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 252 ENFLYMVESMgdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINM 331
Cdd:PRK12349 157 ANFLYMLTGK-----KPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMYM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 332 LSEIGTVENIPEFIESVKNKKRRLSGFGHRIY-KNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKaalsdeYFVKRK 410
Cdd:PRK12349 232 LLEAGTVEKFEELLQKKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEK------IMEKEK 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231128 411 -LYPNVDFYSGLINRAMGIPSS-FTAV---SRIAGYLSHWRESLDdpDTKIMRPQQVYTGAgiRH 470
Cdd:PRK12349 306 gLYPNLDYYAAPVYWMLGIPIQlYTPIffsSRTVGLCAHVIEQHA--NNRLFRPRVNYIGE--RH 366
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
104-477 |
7.53e-80 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 252.76 E-value: 7.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEgiLRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPND-VHPVG 182
Cdd:PRK14034 15 SSVSSIIDDT--LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDLKkVHPMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 183 ALVTAMSALSIFypDANPSLMglgvykSKQVRDKQIVRVLGQAPTIAAA-AYLRKaGKPPVQPLSNLSYSENFLYMVESM 261
Cdd:PRK14034 93 VLRTAISMLGLY--DEEAEIM------DEEANYRKAVRLQAKVPTIVAAfSRIRK-GLDPVEPRKDLSLAANFLYMLNGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 262 gdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENI 341
Cdd:PRK14034 164 -----EPDEVEVEAFNKALVLHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 342 PEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSDeyfvkRKLYPNVDFYSGL 421
Cdd:PRK14034 239 ESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKE-----KGLPPNVDFYSAS 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 422 INRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHYETVRER 477
Cdd:PRK14034 314 VYHCLGIDHDlFTpifAISRMSGWLAHILEQYE--NNRLIRPRADYVGPTHQVYVPIEER 371
|
|
| PRK14033 |
PRK14033 |
bifunctional 2-methylcitrate synthase/citrate synthase; |
104-470 |
2.00e-79 |
|
bifunctional 2-methylcitrate synthase/citrate synthase;
Pssm-ID: 237590 [Multi-domain] Cd Length: 375 Bit Score: 251.79 E-value: 2.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGA 183
Cdd:PRK14033 21 TAISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPTTCHPMDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYPDANPSlmglgvyKSKQVRDKQIvRVLGQAPTIAAAAYLRKAGKPPVQPLSNLSYSENFLYMVesMGD 263
Cdd:PRK14033 101 VRTAVSYLGAEDPEADDS-------SPEANLAKAL-RLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHMC--FGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 264 rsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPE 343
Cdd:PRK14033 171 ---VPEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 344 FIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAalsdeyFVKRK-LYPNVDFYSGLI 422
Cdd:PRK14033 248 WLRDALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKA------MAEATgIKPNLDFPAGPA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15231128 423 NRAMGIP-SSFT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRH 470
Cdd:PRK14033 322 YYLMGFDiDFFTpifVMSRITGWTAHIMEQRA--SNALIRPLSEYNGPEQRE 371
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
106-477 |
2.84e-75 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 240.82 E-value: 2.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 106 ISYIDGDEgiLRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLD--MIQSMPNdVHPVGA 183
Cdd:PRK14035 17 ISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQhfEEYSTDH-VHPMTA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFYPDANPslmglgvyKSKQVRDKQIVRVLGQAPTIAAA-AYLRKaGKPPVQPLSNLSYSENFLYMVesmg 262
Cdd:PRK14035 94 LRTSVSYLAHFDPDAEE--------ESDEARYERAIRIQAKVASLVTAfARVRQ-GKEPLKPRPDLSYAANFLYML---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 263 dRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIP 342
Cdd:PRK14035 161 -RGELPTDIEVEAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGDVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 343 EFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKaalsdeyFVKRK--LYPNVDFYSG 420
Cdd:PRK14035 240 AYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEK-------RMKEEkgLIPNVDFYSA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231128 421 LINRAMGIPSS-FT---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIRHYETVRER 477
Cdd:PRK14035 313 TVYHVMGIPHDlFTpifAVSRVAGWIAHILEQYK--DNRIMRPRAKYIGETNRKYIPIEER 371
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
104-465 |
7.41e-73 |
|
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: 234.51 E-value: 7.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 104 SSISYIdGDEGI-LRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVG 182
Cdd:cd06108 11 TAISTV-GKGGKgLTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 183 ALVTAMSALSIFYPDANPSlmglgvykskQVRDKQIvRVLGQAPTIAAAAYLRKAGKPPVQPLSN-LSYSENFLYMVesm 261
Cdd:cd06108 90 VMRTGCSMLGCLEPENEFS----------QQYEIAI-RLLAIFPSILLYWYHYSHSGKRIETETDeDSIAGHFLHLL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 262 gdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENI 341
Cdd:cd06108 156 --HGKKPGELEIKAMDVSLILYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 342 PEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKAALSdeyfvKRKLYPNVDFYSGL 421
Cdd:cd06108 234 EQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSAS 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15231128 422 INRAMGIPSS-FTAV---SRIAGYLSHWRESLDdpDTKIMRPQQVYTG 465
Cdd:cd06108 309 AYHFCGIPTElFTPIfvmSRVTGWAAHIMEQRA--NNRLIRPSADYIG 354
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
93-469 |
1.81e-59 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 199.03 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 93 DPGYLNTAPVRSSISYIDGDEGILRYRGYPVEELAEKSTYTEVTYLLIygnlpsqrqlaDWEFAISQNSAVPqgvldmiq 172
Cdd:PRK12350 2 VPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLV-----------DGRFGPGLPPAEP-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 173 sMPNDVHPVGALVTAMSALSIFYP-DANPSLMGLgvyKSKQVRDKqivrvLGQAPTIAAAAYLRKA--GKPPVQPLSNLS 249
Cdd:PRK12350 63 -FPLPVHLGDARVDVQAALAMLAPvWGFRPLLDI---DDLTARLD-----LARASVMALSAVAQSArgIGQPAVPQREID 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 250 YSENFLYMVesMGDRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATI 329
Cdd:PRK12350 134 HAATILERF--MGRWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 330 NMLSEIGTVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSilgrdPLVEVGDALEKAALSD--EYFV 407
Cdd:PRK12350 212 PMLDAVERTGDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRATAKRLGA-----PRYEVAEAVEQAALAElrERRP 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231128 408 KRKLYPNVDFYSGLINRAMGIP-SSFTAV---SRIAGYLSHWRESLDdpDTKIMRPQQVYTGAGIR 469
Cdd:PRK12350 287 DRPLETNVEFWAAVLLDFAGVPaHMFTAMftcGRTAGWSAHILEQKR--TGRLVRPSARYVGPAPR 350
|
|
| PRK14032 |
PRK14032 |
citrate synthase; Provisional |
112-477 |
6.01e-53 |
|
citrate synthase; Provisional
Pssm-ID: 184465 [Multi-domain] Cd Length: 447 Bit Score: 184.72 E-value: 6.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 112 DEGILRYRGYPVEELAEKST------YTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVL-DMIQSMP-NDVhpVGA 183
Cdd:PRK14032 64 DEGKLYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrDMILKAPsKDI--MNS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 184 LVTAMSALSIFypDANPSLMGLgvyksKQVRdKQIVRVLGQAPTIAAAAYLRKA----GKPPV--QPLSNLSYSENFLYM 257
Cdd:PRK14032 142 LARSVLALYSY--DDNPDDTSI-----DNVL-RQSISLIARFPTLAVYAYQAYRhyhdGKSLYihPPKPELSTAENILYM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 258 VEsmGDRSYKPNPrlARVLDILFILQAEHEM-NCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEI- 335
Cdd:PRK14032 214 LR--PDNKYTELE--ARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIk 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 336 ------GTVENIPEFIESVKNK-----KRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEKaaLSDE 404
Cdd:PRK14032 290 envkdwEDEDEIADYLTKILNKeafdkSGLIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEK--LAPE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 405 YFVK-RKLY----PNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDPDtKIMRPQQVYTGAGiRHYETVR 475
Cdd:PRK14032 368 LIAEeRGIYkgvsANVDFYSGFVYDMLGIPEElYTplfAIARIVGWSAHRIEELVNGG-KIIRPAYKSVLER-REYVPLE 445
|
..
gi 15231128 476 ER 477
Cdd:PRK14032 446 ER 447
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
112-459 |
1.16e-52 |
|
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: 182.85 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 112 DEGILRYRGYPVEELAEKST------YTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQG-VLDMIQSMPNdvhpvGAL 184
Cdd:cd06113 34 CPGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNfVEDVILKAPS-----KDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 185 VTAM--SALSIFYPDANPSlmglgvykskqvrDKQIVRVLGQA-------PTIAAAAY---LRKAGKPPV---QPLSNLS 249
Cdd:cd06113 109 MNKLqrSVLALYSYDDKPD-------------DISLENVLRQSiqliarlPTIAVYAYqakRHYYDGESLyihHPQPELS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 250 YSENFLYMVESmgDRSYkpNPRLARVLDILFILQAEHEM-NCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEAT 328
Cdd:cd06113 176 TAENILSMLRP--DKKY--TELEAKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 329 INMLSEI-------GTVENIPEFIESVKNKKRR-----LSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDAL 396
Cdd:cd06113 252 MEMLEDIkenvkdwTDEDEVRAYLRKILNKEAFdksglIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERI 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 397 EKAA---LSDEYFVKRKLYPNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESLDDpDTKIMRP 459
Cdd:cd06113 332 ERLApevIAEERGIGKTVCANVDFYSGFVYKMLGIPQElYTplfAVARIVGWCAHRIEELLN-SGRIIRP 400
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
116-465 |
8.21e-51 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 177.04 E-value: 8.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 116 LRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFY 195
Cdd:PRK12351 32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 196 P---DANPSlmglgvykskQVRDKqIVRVLGQAPTIAAAAYlrkagkppvqplsnlSYSEN----------------FLY 256
Cdd:PRK12351 112 PekeDHNFS----------GARDI-ADRLLASLGSILLYWY---------------HYSHNgrrievetdddsigghFLH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 257 MVEsmGDrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIG 336
Cdd:PRK12351 166 LLH--GK---KPSESWVKAMHTSLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 337 TVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVK----KLADEVfsilGRDPLVEVGDALEkAALSDEyfvkRKLY 412
Cdd:PRK12351 241 TPDEAEADIRRRVENKEVVIGFGHPVYTISDPRNKVIKevakKLSKEA----GDTKLYDIAERLE-TVMWEE----KKMF 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231128 413 PNVDFYSGLINRAMGIPSS-FT---AVSRIAGYLSHWRESldDPDTKIMRPQQVYTG 465
Cdd:PRK12351 312 PNLDWFSAVSYHMMGVPTAmFTplfVISRTTGWAAHVIEQ--RQDNKIIRPSANYTG 366
|
|
| Ec2MCS_like_1 |
cd06117 |
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ... |
116-465 |
1.38e-49 |
|
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: 173.49 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 116 LRYRGYPVEELAEKSTYTEVTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPNDVHPVGALVTAMSALSIFY 195
Cdd:cd06117 23 LHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRTGVSVLGCVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 196 PDANpslmGLGVYKSKQVRDkqivRVLGQAPTIAAAAYLRKAGKPPVQPLSNL-SYSENFLYMVESMgdrsyKPNPRLAR 274
Cdd:cd06117 103 PEKE----DHPVSGARDIAD----RLMASLGSILLYWYHYSHNGKRIEVETDDdSIGGHFLHLLHGE-----KPSESWEK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 275 VLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPEFIESVKNKKRR 354
Cdd:cd06117 170 AMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAEADIRRRVENKEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 355 LSGFGHRIYKNYDPRGKVVKKLADEVFSILGRDPLVEVGDALEkAALSDEyfvkRKLYPNVDFYSGLINRAMGIPSS-FT 433
Cdd:cd06117 250 VIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLE-TVMWEE----KKMFPNLDWFSAVSYHMMGVPTAmFT 324
|
330 340 350
....*....|....*....|....*....|....*
gi 15231128 434 ---AVSRIAGYLSHWRESLDdpDTKIMRPQQVYTG 465
Cdd:cd06117 325 plfVIARTTGWSAHIIEQRQ--DGKIIRPSANYTG 357
|
|
| PRK09569 |
PRK09569 |
citrate (Si)-synthase; |
45-465 |
5.88e-41 |
|
citrate (Si)-synthase;
Pssm-ID: 181961 Cd Length: 437 Bit Score: 151.83 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 45 GSLKGNLKIVDERTGNEYQVPVSEHGTVKtvdLKKITTGKDDKGLNLYDPGYlntapvrSSISYIDGDEGIlRYRGYPVE 124
Cdd:PRK09569 1 MQLKETLKQKIEEHRPRTTRLVKEFGSVV---IDEVTIEQCIGGARDIRSLV-------TDISYLDPQEGI-RFRGKTIP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 125 ELAEK---------STYTEVTYLLIYGNLPSQRQLADW--EFAISQNsaVPQGVLDMIQSMPNDVHPVGALVTAMSAL-- 191
Cdd:PRK09569 70 ETFEAlpkapgseyPTVESFWYFLLTGEVPTQEQVQEVvaEWKKRQN--VPQYVIDAIRALPRDSHPMVMLSVGILAMqr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 192 -SIFYPDANPSLMGLGVYKSKQVRDKQIvrVLGQAPTIAAAAYLRKA-GKPPVQPLSNLSYSENFLYMvesMGDrsykpN 269
Cdd:PRK09569 148 eSKFAKFYNEGKFNKMDAWEYMYEDASD--LVARIPVIAAYIYNLKYkGDKQIPSDPELDYGANFAHM---IGQ-----P 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 270 PRLARVLDILFILQAEHEMNCSTAAARHLSSSG-GDVYTAVSGGVGAIYGPLHGGA----VEATINMLSEIG----TVEN 340
Cdd:PRK09569 218 KPYKDVARMYFILHSDHESGNVSAHTTHLVASAlSDAYYSYSAGLNGLAGPLHGLAnqevLGWIQQFQEKLGgeepTKEQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 341 IPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEvfsILGRDPLVEVGDALEKAA--LSDEYFVKRKLYPNVDFY 418
Cdd:PRK09569 298 VEQALWDTLNAGQVIPGYGHAVLRKTDPRYTAQREFCLK---HLPDDPLFKLVAMIFEVApgVLTEHGKTKNPWPNVDAQ 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15231128 419 SGLINRAMGIPSS--FT---AVSRIAGYLSH--WRESLDDPdtkIMRPQQVYTG 465
Cdd:PRK09569 375 SGVIQWYYGVKEWdfYTvlfGVGRALGVMANitWDRGLGYA---IERPKSVTTE 425
|
|
| ScCS-like |
cd06103 |
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ... |
106-462 |
2.91e-37 |
|
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: 141.67 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 106 ISYIDGDEGIlRYRGYPVEELAEK--------STYTE-VTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPN 176
Cdd:cd06103 50 TSVLDPDEGI-RFRGKTIPECQELlpkadgggEPLPEgLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 177 DVHPVGALVTAMSAL---SIFypdanpslmgLGVYKSKQVRDKQI--------VRVLGQAPTIAAAAYLRKAGK--PPVQ 243
Cdd:cd06103 129 NLHPMTQLSAAILALqseSKF----------AKAYAEGKINKTTYweyvyedaMDLIAKLPVVAAKIYRRKYRKggEIGA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 244 PLSNLSYSENFLYMvesMGdrsyKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSG-GDVYTAVSGGVGAIYGPLHG 322
Cdd:cd06103 199 IDSKLDWSANFAHM---LG----YEDEEFTDLMRLYLTLHSDHEGGNVSAHTSHLVGSAlSDPYLSFSAALNGLAGPLHG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 323 GAVEA----TINMLSEIG---TVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLAdevFSILGRDPLVEVGDA 395
Cdd:cd06103 272 LANQEvlkwLLKMQKELGkdvSDEELEKYIWDTLNSGRVVPGYGHAVLRKTDPRFTCQREFA---LKHLPDDPLFKLVAQ 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231128 396 LEKAA---LSDEYFVKRKlYPNVDFYSGLINRAMGI--PSSFT---AVSRIAGYLSH--WRESLDDPdtkIMRPQQV 462
Cdd:cd06103 349 CYKIIpgvLKEHGKVKNP-YPNVDAHSGVLLQHYGMtePQYYTvlfGVSRALGVLAQlvWSRALGLP---IERPKSM 421
|
|
| citrate_synt_like_2 |
cd06102 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
264-465 |
5.65e-26 |
|
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: 106.96 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 264 RSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAIYGPLHGGAVEATINMLSEIGTVENIPE 343
Cdd:cd06102 89 RAWGLDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 344 FIESVKNKKRRLSGFGHRIYKNYDPRgkvvkklADEVFSILGRDPLVEVGDALEKAALSDEYFvkrKLYPNVDFYSGLIN 423
Cdd:cd06102 169 AVRERLRRGEALPGFGHPLYPDGDPR-------AAALLAALRPLGPAAPPAARALIEAARALT---GARPNIDFALAALT 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15231128 424 RAMGIP--SSFT--AVSRIAGYLSHWRESLDDPdtKIMRPQQVYTG 465
Cdd:cd06102 239 RALGLPagAAFAlfALGRSAGWIAHALEQRAQG--KLIRPRARYVG 282
|
|
| ScCit1-2_like |
cd06105 |
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ... |
107-470 |
6.94e-26 |
|
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.
Pssm-ID: 99858 Cd Length: 427 Bit Score: 109.38 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 107 SYIDGDEGIlRYRGYPVEELAE---KSTYTE------VTYLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPND 177
Cdd:cd06105 51 SVLDPEEGI-RFRGLSIPECQKllpKAPGGEeplpegLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 178 VHPVGALVTAMSAL---SIF---YPDanpslmglGVYKSK--QVRDKQIVRVLGQAPTIAAAAYLR--KAGK-PPVQPls 246
Cdd:cd06105 130 LHPMSQLSAAITALnseSKFakaYAE--------GIHKSKywEYVYEDSMDLIAKLPCVAAKIYRNlyRGGKiIAIDS-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 247 NLSYSENFLYMvesMGdrsYKpNPRLARVLDILFILQAEHEMNCSTAAARHLSSSG-GDVYTAVSGGVGAIYGPLHGGAV 325
Cdd:cd06105 200 NLDWSANFANM---LG---YT-DPQFTELMRLYLTIHSDHEGGNVSAHTTHLVGSAlSDPYLSFAAAMNGLAGPLHGLAN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 326 EATIN----MLSEIG---TVENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLA------DEVFSILGR------ 386
Cdd:cd06105 273 QEVLVwltkLQKEVGkdvSDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFAlkhlpnDPLFKLVSQlykivp 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 387 DPLVEVGDAlekaalsdeyfvkRKLYPNVDFYSGLINRAMGIP--SSFT---AVSRIAGYLSH--WRESLDDPdtkIMRP 459
Cdd:cd06105 353 PVLTEQGKA-------------KNPWPNVDAHSGVLLQYYGLTemNYYTvlfGVSRALGVLSQliWDRALGLP---LERP 416
|
410
....*....|.
gi 15231128 460 QQVYTGAGIRH 470
Cdd:cd06105 417 KSVSTDGLEKL 427
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
238-472 |
3.74e-24 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 101.49 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 238 GKPPVQPLSNLSYSENFLYMVesmgdRSYKPNPRLARVLDILFILQAEHEMNCSTAAARHLSSSGGDVYTAVSGGVGAiY 317
Cdd:PRK06224 25 GYDLEDLIGKLSFTDMIFLLL-----RGRLPTPNEARLLDAVLVALVDHGLTPSAAAARMTASGGESLQGAVAAGLLA-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 318 GPLHGGAVEATINMLSEI----GTVENIPEFIESV----KNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVfSILGRdpL 389
Cdd:PRK06224 99 GSVHGGAGEQAAELLQEIaaaaDAGADLDAAARAIvaeyRAAGKRVPGFGHPLHKPVDPRAPRLLALAREA-GVAGR--H 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 390 VEVGDALEKAALSDeyfVKRKLYPNVDFYSGLINRAMGIPSS----FTAVSRIAGYLSH-WRESLDDPDTKIMRPQQV-- 462
Cdd:PRK06224 176 CRLAEALEAALAAA---KGKPLPLNVDGAIAAILADLGFPPAlargLFVISRAAGLVAHvWEELQQPIGFRIWDPAEEav 252
|
250
....*....|.
gi 15231128 463 -YTGAGIRHYE 472
Cdd:PRK06224 253 eYTGPPPRELE 263
|
|
| ScCit3_like |
cd06106 |
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ... |
107-460 |
6.97e-23 |
|
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: 100.66 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 107 SYIDGDEGIlRYRGYPVEE----LAEKSTYTEVT-----YLLIYGNLPSQRQLADWEFAISQNSAVPQGVLDMIQSMPND 177
Cdd:cd06106 51 SVLDAEEGI-RFHGKTIPEcqkeLPKAPIGGEMLpesmlWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 178 VHPVGALVTAMSAL---SIFYPDANPslmglGVYKSKQVRD--KQIVRVLGQAPTIAAAAY--LRKAGKPPVQPLSNLSY 250
Cdd:cd06106 130 LHPMTQLSIGVAALnhdSKFAAAYEK-----GIKKTEYWEPtlEDSLNLIARLPALAARIYrnVYGEGHGLGKIDPEVDW 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 251 SENFLYMVeSMGDrsykpNPRLARVLDILFILQAEHEMNCSTAAARHLSSSG-GDVYTAVSGGVGAIYGPLHGGAVEATI 329
Cdd:cd06106 205 SYNFTSML-GYGD-----NLDFVDLLRLYIALHGDHEGGNVSAHTTHLVGSAlSDPYLSYSAGLMGLAGPLHGLAAQEVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 330 N----MLSEIGTV---ENIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVfSILGRDPLVEVGDALEKAA-- 400
Cdd:cd06106 279 RwileMQKNIGSKatdQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTR-PELENDPVVQLVQKLSEIApg 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231128 401 LSDEYFVKRKLYPNVDFYSGLINRAMGI--PSSFT---AVSRIAGYLSH--WRESLDDPdtkIMRPQ 460
Cdd:cd06106 358 VLTEHGKTKNPFPNVDAASGVLFYHYGIreFLYYTvifGVSRALGPLTQlvWDRILGLP---IERPK 421
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
267-447 |
1.18e-21 |
|
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 93.40 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 267 KPNPRLARVLDILFILQAEHEMN-CSTAAARHLSSSGG-DVYTAVSGGVGAIyGPLHGGAVEATINMLSEI-----GTVE 339
Cdd:cd06100 25 LPTPYEARLLEALLVALADHGPAtPSAHAARLTASAGPeDLQSAVAAGLLGI-GDRFGGAGEGAARLFKEAvdsgdALDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 340 NIPEFIESVKNKKRRLSGFGHRIYKNYDPRGKVVKKLADEVFSILgrdPLVEVGDALEKAALSDeyfvKRKLYP-NVDfy 418
Cdd:cd06100 104 AAAEFVAEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPAG---PHLDYALAVEKALTAA----KGKPLPlNVD-- 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231128 419 sGLINRA---MGIPSS----FTAVSRIAGYLSHWRE 447
Cdd:cd06100 175 -GAIAAIlldLGFPPGalrgLFVLGRSPGLIAHALE 209
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
270-416 |
4.94e-05 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 45.97 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231128 270 PRLA-RVLDILFILQAEHEMNCSTA-----AARhlssSGGDVYTAVSGGVGAIyGPLHGGAVEATINMLSEIGTVENIP- 342
Cdd:PLN02522 396 PRYCtKFIEMCIMLCADHGPCVSGAhntivTAR----AGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDAYDRGLTPy 470
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231128 343 EFIESVKNKKRRLSGFGHRIYK--NYDPRGKVVKKLADEVFsilgrdPLVEVgdaLEKAALSDEYFVKRK--LYPNVD 416
Cdd:PLN02522 471 EFVEGMKKKGIRVPGIGHRIKSrdNRDKRVELLQKYARTHF------PSVKY---MEYAVQVETYTLSKAnnLVLNVD 539
|
|
| |
