|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
26-591 |
0e+00 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 1315.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 26 SPDATLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLS 105
Cdd:PLN02573 13 SSDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 106 VLNAIAGAYSENLPVICIVGGPNTNDFGTNRILHHTIGLFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTALAES 185
Cdd:PLN02573 93 VLNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKES 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 KPVYISISCNLPGIPHPTFMRDPIPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADASG 265
Cdd:PLN02573 173 KPVYISVSCNLAAIPHPTFSREPVPFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 266 YALAVMPSAKGLVPEHHPHFIGTYWGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKITNG 345
Cdd:PLN02573 253 YPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 346 PTFGCVLMKDFLKELAKKVKKNTTAYENYRRIFITDGQPPKCKPNEPLRVNIMFQHIQKMLSADTAVIAETGDSWFNCQK 425
Cdd:PLN02573 333 PAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFNCQK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 426 LKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTIEVEIH 505
Cdd:PLN02573 413 LKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIH 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 506 DGPYNIIKNWNYTALVDAIHNGEGKCWTTKVRTEEELIEAIKKATGDKSDSLCFIEVIVHKDDTSKELLEWGSRVCSANS 585
Cdd:PLN02573 493 DGPYNVIKNWNYTGLVDAIHNGEGKCWTAKVRTEEELIEAIATATGEKKDCLCFIEVIVHKDDTSKELLEWGSRVSAANS 572
|
....*.
gi 2047937441 586 RPPNLQ 591
Cdd:PLN02573 573 RPPNPQ 578
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
30-579 |
0e+00 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 656.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNA 109
Cdd:COG3961 6 TVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAING 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 110 IAGAYSENLPVICIVGGPNTNDFGTNRILHHTIGLFDFSQELRCFQTVTCFQAVINNmEEAHAQIDKAISTALAESKPVY 189
Cdd:COG3961 86 IAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVLTP-ENAAAEIDRVLAAALREKRPVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 190 ISISCNLPGIPhptFMRDPIPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADASGYALA 269
Cdd:COG3961 165 IELPRDVADAP---IEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 270 VMPSAKGLVPEHHPHFIGTYWGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKItNGPTFG 349
Cdd:COG3961 242 TTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRV-GGHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 350 CVLMKDFLKELAKKVKKNTTAYENYRRIFitdgQPPKCKPNEPLRVNIMFQHIQKMLSADTAVIAETGDSWFNCQKLKLP 429
Cdd:COG3961 321 GVSLADFLEALAELLKKRSAPLPAPAPPP----PPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRLP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 430 NGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTIEVEIH--DG 507
Cdd:COG3961 397 EGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHgpDG 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047937441 508 PYNIIKNWNYTALVDAIHNGEGKCWttKVRTEEELIEAIKKATGDKsDSLCFIEVIVHKDDTSKELLEWGSR 579
Cdd:COG3961 477 PYNDIANWDYAKLPEAFGGGNALGF--RVTTEGELEEALAAAEANT-DRLTLIEVVLDKMDAPPLLKRLGKA 545
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
33-194 |
1.23e-91 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 278.99 E-value: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 33 RHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAG 112
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 113 AYSENLPVICIVGGPNTNDFGTNRILHHTIGLFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTALAESKPVYISI 192
Cdd:cd07038 81 AYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEI 160
|
..
gi 2047937441 193 SC 194
Cdd:cd07038 161 PR 162
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
392-574 |
1.16e-87 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 269.40 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 392 PLRVNIMFQHIQKMLSADTAVIAETGDSWFNCQKLKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSF 471
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 472 QVTAQDVSTMIRCEQKTIIFLINNGGYTIEVEIHDG--PYNIIKNWNYTALVDAIhNGEGKCWTTKVRTEEELIEAIKKA 549
Cdd:cd02005 81 QMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPeaSYNDIANWNYTKLPEVF-GGGGGGLSFRVKTEGELDEALKDA 159
|
170 180
....*....|....*....|....*
gi 2047937441 550 TgDKSDSLCFIEVIVHKDDTSKELL 574
Cdd:cd02005 160 L-FNRDKLSLIEVILPKDDAPEALK 183
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
30-568 |
2.49e-68 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 231.20 E-value: 2.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLN 108
Cdd:COG0028 4 TGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 109 AIAGAYSENLPVICIVGGPNTNDFGTNRIlhhtiglfdfsQEL---RCFQTVTCFQAVINNMEEAHAQIDKAISTALAES 185
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGRGAF-----------QEVdqvGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 K-PVYISiscnlpgIPHPTFMR----DPIPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVEL 260
Cdd:COG0028 153 PgPVVLD-------IPKDVQAAeaeeEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 261 ADASGYALAVMPSAKGLVPEHHPHFIGTyWGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRV 340
Cdd:COG0028 226 AERLGAPVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 341 KITNGPTFGCVL---MKDFLKELAKKVKKNTTAY-----------ENYRRIFITDGQPPKckpnePLRVnimFQHIQKML 406
Cdd:COG0028 305 EIGKNYPVDLPIvgdAKAVLAALLEALEPRADDRaawlariaawrAEYLAAYAADDGPIK-----PQRV---IAALREAL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 407 SADTAVIAETGDS--WFNcQKLKL--------PNGcgyefqmqYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQ 476
Cdd:COG0028 377 PDDAIVVTDVGQHqmWAA-RYLRFrrprrfltSGG--------LGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 477 DVSTMIRCEQKTIIFLINNGGYTIEVEIHDGPYN------IIKNWNYTALVDAIHngegkCWTTKVRTEEELIEAIKKAT 550
Cdd:COG0028 448 ELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGgrysgtDLPNPDFAKLAEAFG-----AKGERVETPEELEAALEEAL 522
|
570
....*....|....*...
gi 2047937441 551 gdKSDSLCFIEVIVHKDD 568
Cdd:COG0028 523 --ASDGPALIDVRVDPEE 538
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
31-192 |
7.84e-38 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 137.37 E-value: 7.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 31 LGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSVLNA 109
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARaTGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 110 IAGAYSENLPVICIVGGPNTNDFGTnrilHHTIGLFDFSQELRCFqtvTCFQAVINNMEEAHAQIDKAISTALAESK-PV 188
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGR----GALQQELDQLALFRPV---TKWAVRVTSADEIPEVLRRAFRAALSGRPgPV 153
|
....
gi 2047937441 189 YISI 192
Cdd:pfam02776 154 YLEI 157
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
35-194 |
2.85e-36 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 132.85 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 35 LARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAGAY 114
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 115 SENLPVICIVGGPNTNDFGTnrilhhtiGLFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTALAESKPVYISISC 194
Cdd:cd06586 83 AEHLPVVFLIGARGISAQAK--------QTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
35-192 |
1.58e-31 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 119.56 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 35 LARRLVQIGVSDVFTVPGDFNLTLLDHLiAEPGLTNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSVLNAIAGA 113
Cdd:cd07035 3 LVEALKAEGVDHVFGVPGGAILPLLDAL-ARSGIRYILVRHEQGAVGMADGYARaTGKPGVVLVTSGPGLTNAVTGLANA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 114 YSENLPVICIVGGPNTNDFGTNRilhhtigLFDFSQeLRCFQTVTCFQAVINNMEEAHAQIDKAISTALAESK-PVYISI 192
Cdd:cd07035 82 YLDSIPLLVITGQRPTAGEGRGA-------FQEIDQ-VALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPgPVALDL 153
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
30-568 |
8.28e-26 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 111.63 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEP-GLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVL 107
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQdKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 108 NAIAGAYSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQEL---RCFQTVTCFQAVINNMEEAHAQIDKAISTALAE 184
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGT-----------DFFQEVnleKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 185 SKPVYISISCNLPGIPHPTFMRDPIPFSISPRLSNKmglEAAVEATAAFLNKAVKPVMVGGPKLRVAKatDALVELADAS 264
Cdd:PRK08611 154 KGVAVLTIPDDLPAQKIKDTTNKTVDTFRPTVPSPK---PKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 265 GYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGpifNDYSSVGYslLLKKEKAIIVEPDRVKItn 344
Cdd:PRK08611 229 KIPIIHTLPAKGIIPDDHPYSLGNL-GKIGTKPAYEAMQEADLLIMVG---TNYPYVDY--LPKKAKAIQIDTDPANI-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 345 GPTF----GCVL-MKDFLKELAKKVKKNttayENyrRIFITDGQPPKCKPNE-----------PLRVNIMFQHIQKmLSA 408
Cdd:PRK08611 301 GKRYpvnvGLVGdAKKALHQLTENIKHV----ED--RRFLEACQENMAKWWKwmeedennastPIKPERVMAAIQK-IAD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 409 DTAVIA---ETGDSW----FNCQklklPN------------GCGYEfqmqyGSIgwsvGATLGYaqsvPSKRVIACIGDG 469
Cdd:PRK08611 374 DDAVLSvdvGTVTVWsaryLNLG----TNqkfiisswlgtmGCGLP-----GAI----AAKIAF----PDRQAIAICGDG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 470 SFQVTAQDVSTMIRCEQKTIIFLINNGGYT-IEVEIHDG---PYNI-IKNWNYTALVDAIhNGEGkcwtTKVRTEEELIE 544
Cdd:PRK08611 437 GFSMVMQDFVTAVKYKLPIVVVVLNNQQLAfIKYEQQAAgelEYAIdLSDMDYAKFAEAC-GGKG----YRVEKAEELDP 511
|
570 580
....*....|....*....|....
gi 2047937441 545 AIKKATgdKSDSLCFIEVIVHKDD 568
Cdd:PRK08611 512 AFEEAL--AQDKPVIIDVYVDPNA 533
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
30-568 |
1.67e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 107.40 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTN-IGCCNELNAGYAADGYARSRG-VGACVVtftVGGLSVL 107
Cdd:PRK08266 5 TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRvIHTRHEQAAGYMAFGYARSTGrPGVCSV---VPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 108 NAIAG---AYSENLPVICIVGgpntndfgtnRILHHTIG-----LFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAIS 179
Cdd:PRK08266 82 NAGAAlltAYGCNSPVLCLTG----------QIPSALIGkgrghLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 180 TALA-ESKPVYISiscnlpgIPHPTFMR-----DPIPFSISPRLsnkMGLEAAVEATAAFLNKAVKPV-MVGGPklrVAK 252
Cdd:PRK08266 152 QMLSgRPRPVALE-------MPWDVFGQrapvaAAPPLRPAPPP---APDPDAIAAAAALIAAAKNPMiFVGGG---AAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 253 ATDALVELADASGYALAVMPSAKGLVPEHHP---HFIGTYwgavstafcgEIVESADAYLFAGPIFNDySSVGYSLLLKK 329
Cdd:PRK08266 219 AGEEIRELAEMLQAPVVAFRSGRGIVSDRHPlglNFAAAY----------ELWPQTDVVIGIGSRLEL-PTFRWPWRPDG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 330 EKAIIVEPDRVKITN-GPTFGCVL-MKDFLKELAKKVKKNTTAYENYRRIF----------ITDGQPPKckpnEPLRVni 397
Cdd:PRK08266 288 LKVIRIDIDPTEMRRlKPDVAIVAdAKAGTAALLDALSKAGSKRPSRRAELrelkaaarqrIQAVQPQA----SYLRA-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 398 mfqhIQKMLSADTAVIAETGD----SWFnCQKLKLPN---GCGYEfqmqyGSIGWSVGATLGYAQSVPSKRVIACIGDGS 470
Cdd:PRK08266 362 ----IREALPDDGIFVDELSQvgfaSWF-AFPVYAPRtfvTCGYQ-----GTLGYGFPTALGAKVANPDRPVVSITGDGG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 471 FQVTAQDVSTMIRCEQKTIIFLINNGGY----TIEVEIHDGPY--NIIKNWNYTALVDAIhnGEGKCwttKVRTEEELIE 544
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAYgnvrRDQKRRFGGRVvaSDLVNPDFVKLAESF--GVAAF---RVDSPEELRA 506
|
570 580
....*....|....*....|....
gi 2047937441 545 AIKKATGDKSDSLcfIEVIVHKDD 568
Cdd:PRK08266 507 ALEAALAHGGPVL--IEVPVPRGS 528
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
227-360 |
1.87e-23 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 96.09 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 227 VEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADASGYALAVMPSAKGLVPEHHPHFIGtYWGAVSTAFCGEIVESAD 306
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 307 AYLFAGPIFNDYSSVGYSLLLKKEKAII-VEPDRVKI-----TNGPTFGCVlmKDFLKEL 360
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPDAKIIhIDIDPAEIgknypVDVPIVGDA--KETLEAL 137
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
39-564 |
1.18e-21 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 98.92 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 39 LVQIGVSDVFTVPGDFNLTLLDhLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSEN 117
Cdd:PRK07525 16 LQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYWAH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 118 LPVICIvggpnTNDFGTNrilhhTIGLFDFsQE---LRCFQTVTCFQAVINNMEEAHAQIDKAISTALAESKPVYIsisc 194
Cdd:PRK07525 95 TPVVLV-----TPQAGTK-----TIGQGGF-QEaeqMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQI---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 195 NLP----------GIPHPtfmrdpipfsisPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADAS 264
Cdd:PRK07525 160 NIPrdyfygvidvEIPQP------------VRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 265 GYALAVMPSAKGLVPEHHPHFIGT--YWGavSTAfCGEIVESADAYLFAGPIFNDYSSV-GYSL-LLKKEKAII---VEP 337
Cdd:PRK07525 228 DAPVACGYLHNDAFPGSHPLWVGPlgYNG--SKA-AMELIAKADVVLALGTRLNPFGTLpQYGIdYWPKDAKIIqvdINP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 338 DRVKITNGPTFG-CVLMKDFLKELAKKVKKNTTAYENY--RRIFITDGQ---------------PPKCKPNEPLRV---N 396
Cdd:PRK07525 305 DRIGLTKKVSVGiCGDAKAVARELLARLAERLAGDAGReeRKALIAAEKsaweqelsswdheddDPGTDWNEEARArkpD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 397 IM-----FQHIQK------MLSADTAVIAETGDSWfncqkLKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIAC 465
Cdd:PRK07525 385 YMhprqaLREIQKalpedaIVSTDIGNNCSIANSY-----LRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 466 IGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTIE----VEIHDGPY---NIIKNWNYTALVDAIhNGEGkcwtTKVRT 538
Cdd:PRK07525 460 AGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEkknqVDFYNNRFvgtELDNNVSYAGIAEAM-GAEG----VVVDT 534
|
570 580
....*....|....*....|....*..
gi 2047937441 539 EEELIEAIKKATGDKSDSL-CFIEVIV 564
Cdd:PRK07525 535 QEELGPALKRAIDAQNEGKtTVIEIMC 561
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
21-563 |
5.62e-20 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 93.67 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 21 TNDAVSPDATLGRHLARRLVQIGVSDVF--TVPGDFnltlldHLIAEP-GLTNIGCCNELNAGYAADGYAR-SRGVGacV 96
Cdd:PRK06112 6 SAPGFTLNGTVAHAIARALKRHGVEQIFgqSLPSAL------FLAAEAiGIRQIAYRTENAGGAMADGYARvSGKVA--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 97 VTFTVGGLSVL--NAIAGAYSENLPVICIVGGPNTNDFGTNRI--LHHtIGLfdfsqelrcFQTVTCFQAVINNMEEAHA 172
Cdd:PRK06112 78 VTAQNGPAATLlvAPLAEALKASVPIVALVQDVNRDQTDRNAFqeLDH-IAL---------FQSCTKWVRRVTVAERIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 173 QIDKAISTALA-ESKPVYISISCNLpgiphptfMRDPIPFSISPRlSNKMG---------LEAAVEATAAFLNKAVKPVM 242
Cdd:PRK06112 148 YVDQAFTAATSgRPGPVVLLLPADL--------LTAAAAAPAAPR-SNSLGhfpldrtvpAPQRLAEAASLLAQAQRPVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 243 VGGPKLRVAKATDALVELADASGYALAVMPSAKGLVPEHHPHFIGTYWGAV----STAFCGEIVESADAYLFAGPIFNDY 318
Cdd:PRK06112 219 VAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGSLMgprsPGRHLRDLVREADVVLLVGTRTNQN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 319 SSVGYSLLLKKEKAIIVEPDRVKItnGPTFGCV-----------LMKDFLKELAKKVKKNTTA-----YENYRRIFITDG 382
Cdd:PRK06112 299 GTDSWSLYPEQAQYIHIDVDGEEV--GRNYEALrlvgdarltlaALTDALRGRDLAARAGRRAalepaIAAGREAHREDS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 383 QPPKCKPNEPLRVNIMFQHIQKMLSADTAVIAETGDS--WFnCQKLKLPNGcGYEFQMQYG--SIGWSVGATLGYAQSVP 458
Cdd:PRK06112 377 APVALSDASPIRPERIMAELQAVLTGDTIVVADASYSsiWV-ANFLTARRA-GMRFLTPRGlaGLGWGVPMAIGAKVARP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 459 SKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNG--GYTIEVEihdgpynIIKNWNYTalvDAIHNGE-------G 529
Cdd:PRK06112 455 GAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGFQKHAE-------TVKFGTHT---DACHFAAvdhaaiaR 524
|
570 580 590
....*....|....*....|....*....|....*.
gi 2047937441 530 KCWTTKVRTEE--ELIEAIKKATGDKSDSLcfIEVI 563
Cdd:PRK06112 525 ACGCDGVRVEDpaELAQALAAAMAAPGPTL--IEVI 558
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
33-495 |
2.58e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 91.44 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 33 RHLARRLVQIGVSDVFTVPGDFNLTLLDHLI---AEPGLTNIGCCNELNAGYAADGYARSRGV-GACVVTFTVGGLSVLN 108
Cdd:PRK06456 6 RILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTTNLVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 109 AIAGAYSENLPVICIVGGPNTNDFGTNRilhhtiglFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTA-LAESKP 187
Cdd:PRK06456 86 GLITAYWDSSPVIAITGQVPRSVMGKMA--------FQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIAtTGRPGP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 188 VYISISCNLPGI-------PHPTFMRDPIPFsisPRLSNKMGLEAAVEataaFLNKAVKPVMVGGPKLRVAKATDALVEL 260
Cdd:PRK06456 158 VVIDIPRDIFYEkmeeikwPEKPLVKGYRDF---PTRIDRLALKKAAE----ILINAERPIILVGTGVVWSNATPEVLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 261 ADASGYALAVMPSAKGLVPEHHPHFIGT--YWGAVSTAFCGeiVESaDAYLFAGPIFNDYSSVGYSLLLKKEKAII---V 335
Cdd:PRK06456 231 AELLHIPIVSTFPGKTAIPHDHPLYFGPmgYYGRAEASMAA--LES-DAMLVVGARFSDRTFTSYDEMVETRKKFImvnI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 336 EPDRVKITNGPTFGCV-----LMKDFLK---ELAKKVK-----KNTTAYENYRRIFITDGQPPKCKPNEPLRVnimfqhI 402
Cdd:PRK06456 308 DPTDGEKAIKVDVGIYgnakiILRELIKaitELGQKRDrsawlKRVKEYKEYYSQFYYTEENGKLKPWKIMKT------I 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 403 QKMLSADTAVIAETGDS-------WFNCQKLKLPNGCGyefqmqYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTA 475
Cdd:PRK06456 382 RQALPRDAIVTTGVGQHqmwaevfWEVLEPRTFLTSSG------MGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTG 455
|
490 500
....*....|....*....|
gi 2047937441 476 QDVSTMIRcEQKTIIFLINN 495
Cdd:PRK06456 456 TNLATAVD-EHIPVISVIFD 474
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
402-564 |
2.69e-18 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 82.30 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 402 IQKMLSADTAVIAETGDS--WFNcQKLKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVS 479
Cdd:cd00568 6 LRAALPEDAIVVNDAGNSayWAY-RYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQELA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 480 TMIRCEQKTIIFLINNGGYTIEVEIHDGPYNI------IKNWNYTALVDAIHngegkCWTTKVRTEEELIEAIKKAtgDK 553
Cdd:cd00568 85 TAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrvsgtdLSNPDFAALAEAYG-----AKGVRVEDPEDLEAALAEA--LA 157
|
170
....*....|.
gi 2047937441 554 SDSLCFIEVIV 564
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
15-567 |
4.30e-18 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 87.95 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 15 DSGTSVTNDAVSPDAT---LGRHLARRLVQIGVSDVFTVPGDfnlTLLDHlIAEPGLTNIGCCNELNAGYAADGYARS-- 89
Cdd:PRK06154 3 DGTHALPNAHLPAEAKtmkVAEAVAEILKEEGVELLFGFPVN---ELFDA-AAAAGIRPVIARTERVAVHMADGYARAts 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 90 -RGVGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGpntndfgTNRILHHTIGLFDfsqELRCFQTVTCFQAVINNME 168
Cdd:PRK06154 79 gERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTG-------YPRGSTDVAPNFE---SLRNYRHITKWCEQVTLPD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 169 EAHAQIDKAISTAL-AESKPVYISISCNLPGIPhptFMRDPIPFSISPRLSNKMGlEAAVEATAAFLNKAVKPVMVGGPK 247
Cdd:PRK06154 149 EVPELMRRAFTRLRnGRPGPVVLELPVDVLAEE---LDELPLDHRPSRRSRPGAD-PVEVVEAAALLLAAERPVIYAGQG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 248 LRVAKATDALVELADASGYALAVMPSAKGLVPEHHPHFIGT---YWGAVSTAFcgeiVESADAyLFAgpIFNDYSSVGYS 324
Cdd:PRK06154 225 VLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSggrARPATVAHF----LREADV-LFG--IGCSLTRSYYG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 325 LLLKKEKAII---VEPDRVKITNGPTFGCV-----LMKDFLKELAKKVKKNT-------TAYENYRRIFITDGQP---PK 386
Cdd:PRK06154 298 LPMPEGKTIIhstLDDADLNKDYPIDHGLVgdaalVLKQMIEELRRRVGPDRgraqqvaAEIEAVRAAWLAKWMPkltSD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 387 CKPNEPLRVnimFQHIQKMLSADTAVIAETGDS-------WFNCQKLKLPNGCGYEFQMQYGsIGWSVGATLgyaqSVPS 459
Cdd:PRK06154 378 STPINPYRV---VWELQHAVDIKTVIITHDAGSprdqlspFYVASRPGSYLGWGKTTQLGYG-LGLAMGAKL----ARPD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 460 KRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTIEVEIHDGPYNIIKNWNYTALVDAIHNGEGkCWTTKVRTE 539
Cdd:PRK06154 450 ALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFSMGGYDKVMPVSTTKYRATDISGDYAAIARALG-GYGERVEDP 528
|
570 580 590
....*....|....*....|....*....|
gi 2047937441 540 EELIEAIKKATgDKSDS--LCFIEVIVHKD 567
Cdd:PRK06154 529 EMLVPALLRAL-RKVKEgtPALLEVITSEE 557
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
30-500 |
2.42e-17 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 85.31 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLsvlN 108
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGrPGICFVTRGPGAT---N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 109 AIAG---AYSENLPVICIVGGPNtNDFgtnrilhhtiglfdfsQELRCFQTVTcFQAVINNMEEAHAQIDKA------IS 179
Cdd:PRK08199 86 ASIGvhtAFQDSTPMILFVGQVA-RDF----------------REREAFQEID-YRRMFGPMAKWVAEIDDAaripelVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 180 TALAESK-----PVYISiscnLP-----GIPHPTFMRDPIPFSISPRlsnkmglEAAVEATAAFLNKAVKPVMVGGPKLR 249
Cdd:PRK08199 148 RAFHVATsgrpgPVVLA----LPedvlsETAEVPDAPPYRRVAAAPG-------AADLARLAELLARAERPLVILGGSGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 250 VAKATDALVELADAsgYALAVMPSAK--GLVPEHHPHFIGTY-WGAvsTAFCGEIVESADAYLFAGPIFNDYSSVGYSLL 326
Cdd:PRK08199 217 TEAAVADLRAFAER--WGLPVACAFRrqDLFDNRHPNYAGDLgLGI--NPALAARIREADLVLAVGTRLGEVTTQGYTLL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 327 ---LKKEKAIIVEPD-----RVKitnGPTFG-CVLMKDFLKELAKKVKKNTTAY----ENYRRIFITDGQPPKCkpnePL 393
Cdd:PRK08199 293 dipVPRQTLVHVHPDaeelgRVY---RPDLAiVADPAAFAAALAALEPPASPAWaewtAAAHADYLAWSAPLPG----PG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 394 RVN---IMfQHIQKMLSADtAVIAetgdswfncqklklpNGCG------------YEFQMQY----GSIGWSVGATLGYA 454
Cdd:PRK08199 366 AVQlgeVM-AWLRERLPAD-AIIT---------------NGAGnyatwlhrffrfRRYRTQLaptsGSMGYGLPAAIAAK 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2047937441 455 QSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGY-TI 500
Cdd:PRK08199 429 LLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
30-200 |
2.90e-17 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 79.52 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLN 108
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 109 AIAGAYSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQE---LRCFQTVTCFQAVINNMEEAHAQIDKAISTALAES 185
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGT-----------DYFQEvdlLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR 149
|
170
....*....|....*
gi 2047937441 186 KPVYISISCNLPGIP 200
Cdd:cd07039 150 GVAVLILPGDVQDAP 164
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
29-498 |
6.38e-17 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 83.87 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 29 ATLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLiAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVL 107
Cdd:PRK07524 2 TTCGEALVRLLEAYGVETVFGIPGVHTVELYRGL-AGSGIRHVTPRHEQGAGFMADGYARVSGkPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 108 NAIAGAYSENLPVICIVGGPNTNDFGTNRILHHtiglfdfsqELR----CFQTVTCFQAVINNMEEAHAQIDKAIstALA 183
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSVNRRASLGKGRGKLH---------ELPdqraMVAGVAAFSHTLMSAEDLPEVLARAF--AVF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 184 ES---KPVYISISCNLPGIPHPtFMRDPIPFSISPRLSNKmgleAAVEATAAFLNKAVKPVMV-GGPKLRVAKATDALVE 259
Cdd:PRK07524 150 DSarpRPVHIEIPLDVLAAPAD-HLLPAPPTRPARPGPAP----AALAQAAERLAAARRPLILaGGGALAAAAALRALAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 260 LADASgYALAVmpSAKGLVPEHHPHFIGtywGAVSTAFCGEIVESADAYLFAGPIF--NDYSSVGYSLLLKKEKAIIVEP 337
Cdd:PRK07524 225 RLDAP-VALTI--NAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELgeTDYDVYFDGGFPLPGELIRIDI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 338 DRVKITNGPTFGCVLMKD-------FLKELAKKVKKNTTAYENYR--RIFITDGQPPKCKPNEPLrvnimFQHIQKMLSA 408
Cdd:PRK07524 299 DPDQLARNYPPALALVGDaraaleaLLARLPGQAAAADWGAARVAalRQALRAEWDPLTAAQVAL-----LDTILAALPD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 409 DTAViaetGDS------------------WFNCqklklPNGcgyefqmqYGSIGWSVGATLGYAQSVPSKRVIACIGDGS 470
Cdd:PRK07524 374 AIFV----GDStqpvyagnlyfdadaprrWFNA-----STG--------YGTLGYGLPAAIGAALGAPERPVVCLVGDGG 436
|
490 500
....*....|....*....|....*....
gi 2047937441 471 FQVTAQDVSTMIRcEQKTIIFLI-NNGGY 498
Cdd:PRK07524 437 LQFTLPELASAVE-ADLPLIVLLwNNDGY 464
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
39-564 |
1.38e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 82.84 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 39 LVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSEN 117
Cdd:PRK08527 13 LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATAYMDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 118 LPVICIVGGPNTNDFGTnrilhhtiglfDFSQELR-------CFQ---TVTCFQAVINNMEEA------------HAQID 175
Cdd:PRK08527 93 IPLVLISGQVPNSLIGT-----------DAFQEIDavgisrpCVKhnyLVKSIEELPRILKEAfyiarsgrpgpvHIDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 176 KAISTALAESK-PVYISISCNLPGIPhptfmrdpipfsisprlSNKMGLEAAVEAtaafLNKAVKPVMVGGPKLRVAKAT 254
Cdd:PRK08527 162 KDVTATLGEFEyPKEISLKTYKPTYK-----------------GNSRQIKKAAEA----IKEAKKPLFYLGGGAILSNAS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 255 DALVELADASG-------YALAVM----PSAKGLVPEHhphfiGTYwgAVSTAfcgeiVESADAYLFAGPIFNDYSSVGY 323
Cdd:PRK08527 221 EEIRELVKKTGipavetlMARGVLrsddPLLLGMLGMH-----GSY--AANMA-----MSECDLLISLGARFDDRVTGKL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 324 SLLLKKEKAIIVEPDRVKI-----TNGPTFGCVlmKDFLKELAKKVKK-NTTAYENYRRIF--ITDGQPPKCK-PNEPLR 394
Cdd:PRK08527 289 SEFAKHAKIIHVDIDPSSIskivnADYPIVGDL--KNVLKEMLEELKEeNPTTYKEWREILkrYNELHPLSYEdSDEVLK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 395 VNIMFQHIQKMLSADTAVIAETGDS--W------FNCQKLKLPNGcgyefqmQYGSIGWSVGATLGYAQSVPSKRVIACI 466
Cdd:PRK08527 367 PQWVIERVGELLGDDAIISTDVGQHqmWvaqfypFNYPRQLATSG-------GLGTMGYGLPAALGAKLAVPDKVVINFT 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 467 GDGSFQVTAQDVSTMIRCEQKTIIFLINNgGY--------TIEVEIHDGPYNIIKNWNYTALVDAIHnGEGkcwtTKVRT 538
Cdd:PRK08527 440 GDGSILMNIQELMTAVEYKIPVINIILNN-NFlgmvrqwqTFFYEERYSETDLSTQPDFVKLAESFG-GIG----FRVTT 513
|
570 580
....*....|....*....|....*.
gi 2047937441 539 EEELIEAIKKATgdKSDSLCFIEVIV 564
Cdd:PRK08527 514 KEEFDKALKEAL--ESDKVALIDVKI 537
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
43-568 |
5.53e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 80.97 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 43 GVSDVFTVPGDFNLTLLDHLIaEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 121
Cdd:PRK06048 22 GVEVIFGYPGGAIIPVYDELY-DSDLRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGATNLVTGIATAYMDSVPIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 122 CIVGGPNTNDFGTnrilhhtiglfDFSQELR---CFQTVTCFQAVINNMEEAHAQIDKAISTA-LAESKPVYIsiscNLP 197
Cdd:PRK06048 101 ALTGQVPRSMIGN-----------DAFQEADitgITMPITKHNYLVQDAKDLPRIIKEAFHIAsTGRPGPVLI----DLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 198 giphPTFMRDPIPFSISPRLSNK------MGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADASGYALAVM 271
Cdd:PRK06048 166 ----KDVTTAEIDFDYPDKVELRgykptyKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 272 PSAKGLVPEHHPHFIGtYWGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKITNG-----P 346
Cdd:PRK06048 242 LMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNvkvdvP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 347 TFGCVlmKDFLKELAKKVK-KNTTAYENY----RRIFitdgqPPKCKPNEPLrvnIMFQHIQKMLS---ADTAVIAETGD 418
Cdd:PRK06048 321 IVGDA--KQVLKSLIKYVQyCDRKEWLDKinqwKKEY-----PLKYKEREDV---IKPQYVIEQIYelcPDAIIVTEVGQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 419 S--WfNCQKLKlpngcgYEFQMQY------GSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTII 490
Cdd:PRK06048 391 HqmW-AAQYFK------YKYPRTFitsgglGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 491 FLINNGGYTIEVEIHDGPYNiiKNWNYTAL---VDAIHNGEG-KCWTTKVRTEEELIEAIKKATGdkSDSLCFIEVIVHK 566
Cdd:PRK06048 464 AILNNGYLGMVRQWQELFYD--KRYSHTCIkgsVDFVKLAEAyGALGLRVEKPSEVRPAIEEAVA--SDRPVVIDFIVEC 539
|
..
gi 2047937441 567 DD 568
Cdd:PRK06048 540 EE 541
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
30-510 |
6.99e-16 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 80.80 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTvgGLSVLNA 109
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTST--GTGAGNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 110 iAGAYSENL----PVICIVGGPNTNDFGTNRILHHtiglfDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTAL-AE 184
Cdd:PRK07064 82 -AGALVEALtagtPLLHITGQIETPYLDQDLGYIH-----EAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALtAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 185 SKPVYISISCNLPG--IPHPTFMRdPIPFSiSPRLSnkmglEAAVEATAAFLNKAVKPVM-VGGPKLRVAKATDALVELa 261
Cdd:PRK07064 156 TGPVSVEIPIDIQAaeIELPDDLA-PVHVA-VPEPD-----AAAVAELAERLAAARRPLLwLGGGARHAGAEVKRLVDL- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 262 dasGYALAVMPSAKGLVPEHHPHFIGTYWGAVSTAfcgEIVESADAYLFAGPIFNDYSSVGYSLLLkkekaiivePD-RV 340
Cdd:PRK07064 228 ---GFGVVTSTQGRGVVPEDHPASLGAFNNSAAVE---ALYKTCDLLLVVGSRLRGNETLKYSLAL---------PRpLI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 341 KITNGPT----------FGCVLMKDFLKELAKKVKKNTTAYENyrriFITDGQPPKCKPNEPLRVNI-----MFQHIQKM 405
Cdd:PRK07064 293 RVDADAAadgrgypndlFVHGDAARVLARLADRLEGRLSVDPA----FAADLRAAREAAVADLRKGLgpyakLVDALRAA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 406 LSADTAV---IAETGDSWFNcqklklpngcgYEFQMQY---------GSIGWSVGATLGYAQSVPSKRVIACIGDGSFQV 473
Cdd:PRK07064 369 LPRDGNWvrdVTISNSTWGN-----------RLLPIFEpranvhalgGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLML 437
|
490 500 510
....*....|....*....|....*....|....*..
gi 2047937441 474 TAQDVSTMIRCEQKTIIFLINNGGYTIEVEIHDGPYN 510
Cdd:PRK07064 438 NLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYG 474
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
32-495 |
7.01e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 80.95 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 32 GRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEpGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAI 110
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 111 AGAYSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQE---LRCFQTVTCFQAVINNMEEAHAQIDKAISTA-LAESK 186
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGN-----------DAFQEidaLGIFMPITKHNFQIKKPEEIPEIFRAAFEIAkTGRPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 187 PVYISISCNLPGIPHPTFmRDPIPFSIS-PRLS-NKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADAS 264
Cdd:PRK06276 152 PVHIDLPKDVQEGELDLE-KYPIPAKIDlPGYKpTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 265 GYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKI-- 342
Cdd:PRK06276 231 KIPVCTTLMGKGAFPEDHPLALGMV-GMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIgk 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 343 ---TNGPTFG--CVLMKDFLKELAKKVKKNTTAY----ENYRRIFIT----DGQPpkCKPNEPLRVnIMFQHIQKMLSAD 409
Cdd:PRK06276 310 nvrVDVPIVGdaKNVLRDLLAELMKKEIKNKSEWlervKKLKKESIPrmdfDDKP--IKPQRVIKE-LMEVLREIDPSKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 410 TAVIAETGDS--W----FNCQKLK--LPNGcgyefqmQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTM 481
Cdd:PRK06276 387 TIITTDVGQNqmWmahfFKTSAPRsfISSG-------GLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATI 459
|
490
....*....|....
gi 2047937441 482 IRCEQKTIIFLINN 495
Cdd:PRK06276 460 AEYDIPVVICIFDN 473
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
43-498 |
1.96e-14 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 76.02 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 43 GVSDVFTVPGDFNLTLLDHLiAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 121
Cdd:PRK08322 15 GVEYIFGIPGEENLDLLEAL-RDSSIKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVAYAQLGGMPMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 122 CIVGgpntnDFGTNRIlhHtIGLFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTALAEsKP--VYISISCNLPGI 199
Cdd:PRK08322 94 AITG-----QKPIKRS--K-QGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEE-RPgaVHLELPEDIAAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 200 PHPTfmrDPIPFSISPRlsnKMGLEAAVEATAAFLNKAVKPV-MVGGPKLRvAKATDALVELADASGYALAVMPSAKGLV 278
Cdd:PRK08322 165 ETDG---KPLPRSYSRR---PYASPKAIERAAEAIQAAKNPLiLIGAGANR-KTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 279 PEHHPHFIGTywgavsTAF-------CGeiVESADAylfagpIFNdyssVGYSLLLKK--------EKAII------VEP 337
Cdd:PRK08322 238 PETHPLSLGT------AGLsqgdyvhCA--IEHADL------IIN----VGHDVIEKPpffmnpngDKKVIhinflpAEV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 338 DRVKItngPTFGCV-----LMKDFLKELAKKVKKNTTAYENYRRIF---ITDGQ-----PPKckpnePLRVnimFQHIQK 404
Cdd:PRK08322 300 DPVYF---PQVEVVgdianSLWQLKERLADQPHWDFPRFLKIREAIeahLEEGAdddrfPMK-----PQRI---VADLRK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 405 MLSADTAVIAETG--DSWF----NCQKlklPNGC----GYefqmqygsigwsvgATLGYAqsVPS----------KRVIA 464
Cdd:PRK08322 369 VMPDDDIVILDNGayKIWFarnyRAYE---PNTClldnAL--------------ATMGAG--LPSaiaaklvhpdRKVLA 429
|
490 500 510
....*....|....*....|....*....|....
gi 2047937441 465 CIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGY 498
Cdd:PRK08322 430 VCGDGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
33-287 |
3.07e-14 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 75.69 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 33 RHLARRLVQIGVSDVFTVPGDFNLTLLDHLIaEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIA 111
Cdd:PRK08978 5 QWVVHALRAQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGkVGVCIATSGPGATNLITGLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 112 GAYSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQELRCF-QTVTC----FqaVINNMEEAHAQIDKAIstALAESK 186
Cdd:PRK08978 84 DALLDSVPVVAITGQVSSPLIGT-----------DAFQEIDVLgLSLACtkhsF--LVQSLEELPEIMAEAF--EIASSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 187 ---PVYISIS-----CNLPGIPHPTFMRDPIPFSisprlsnkmglEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALV 258
Cdd:PRK08978 149 rpgPVLVDIPkdiqlAEGELEPHLTTVENEPAFP-----------AAELEQARALLAQAKKPVLYVGGGVGMAGAVPALR 217
|
250 260 270
....*....|....*....|....*....|....
gi 2047937441 259 ELADASGyalavMPSA---KGL--VPEHHPHFIG 287
Cdd:PRK08978 218 EFLAATG-----MPAVatlKGLgaVEADHPYYLG 246
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
43-564 |
1.07e-13 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 73.79 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 43 GVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 121
Cdd:PRK06882 18 GVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGIATAYTDSVPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 122 CIVGGPNTNDFGTNRilhhtiglFDFSQELRCFQTVTCFQAVINNMEEAHAQIDKAISTA-LAESKPVYISISCNLPGIP 200
Cdd:PRK06882 98 ILSGQVPSNLIGTDA--------FQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIAsTGRPGPVVIDIPKDMVNPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 201 HPTFMRDPIPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALVELADAsgYALAVMPSAKGL--V 278
Cdd:PRK06882 170 NKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQK--LNLPVTSSLMGLgaY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 279 PEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKITNG-----PTFGCV-- 351
Cdd:PRK06882 248 PSTDKQFLGML-GMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNvpayiPIVGSAkn 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 352 LMKDFLKELAKK-VKKNTTAYENYRRIfITDGQPPKC----KPNEPLRVNIMFQHIQKMLSADTAVIAETGD-------- 418
Cdd:PRK06882 327 VLEEFLSLLEEEnLAKSQTDLTAWWQQ-INEWKAKKClefdRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQhqmfaalh 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 419 -------SWFNCQKLklpngcgyefqmqyGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIF 491
Cdd:PRK06882 406 ypfdkprRWINSGGA--------------GTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047937441 492 LINNGGYTIEVEIHDGPYNIIKNWNY-TALVDAIHNGEGKCWT-TKVRTEEELIEAIKKATGDKsDSLCFIEVIV 564
Cdd:PRK06882 472 SLNNRFLGMVKQWQDLIYSGRHSQVYmNSLPDFAKLAEAYGHVgIQIDTPDELEEKLTQAFSIK-DKLVFVDVNV 545
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
392-564 |
1.21e-13 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 69.10 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 392 PLRVnimFQHIQKMLSADTAVIAETGD------SWFNCQKLKLPNGCGYefqmqYGSIGWSVGATLGYAQSVPSKRVIAC 465
Cdd:cd02004 1 PYRV---LHELQEALPDDAIIVSDGGNtmdwarYILRPRKPRHRLDAGT-----FGTLGVGLGYAIAAALARPDKRVVLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 466 IGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTIEVeiHDGPYNIIKNWNYTALV-----DAIHNGEGkCWTTKVRTEE 540
Cdd:cd02004 73 EGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGL--DGQQLSYGLGLPVTTLLpdtryDLVAEAFG-GKGELVTTPE 149
|
170 180
....*....|....*....|....
gi 2047937441 541 ELIEAIKKATgdKSDSLCFIEVIV 564
Cdd:cd02004 150 ELKPALKRAL--ASGKPALINVII 171
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
37-317 |
1.48e-13 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 73.59 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 37 RRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGA-CVVTFTVGGLSVLNAIAGAYS 115
Cdd:PRK08155 21 RLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAvCMACSGPGATNLVTAIADARL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 116 ENLPVICIVGGPNTNDFGTNrilhhtiglfdfsqelrCFQTVTCFQAVI-----NNMEEAHAQIDKAISTA--LAES--- 185
Cdd:PRK08155 101 DSIPLVCITGQVPASMIGTD-----------------AFQEVDTYGISIpitkhNYLVRDIEELPQVISDAfrIAQSgrp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 KPVYISI-------SCNLPGIPHPtFMRDPIPfSISPrlsnkmgleAAVEATAAFLNKAVKPVMVGGPKLRVAKATDALV 258
Cdd:PRK08155 164 GPVWIDIpkdvqtaVIELEALPAP-AEKDAAP-AFDE---------ESIRDAAAMINAAKRPVLYLGGGVINSGAPARAR 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047937441 259 ELADASGYALAVMPSAKGLVPEHHPHFIGT--YWGAVSTAFcgeIVESADAYLFAGPIFND 317
Cdd:PRK08155 233 ELAEKAQLPTTMTLMALGMLPKAHPLSLGMlgMHGARSTNY---ILQEADLLIVLGARFDD 290
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
168-564 |
1.59e-13 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 73.07 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 168 EEAHAQ-----IDKAISTALAESK-PVYISIscnlpgiPHPTFMRDPIPfsISPR-LSNKMGLE-AAVEATAAFLNKAVK 239
Cdd:PRK07092 138 EPARAEdvpaaIARAYHIAMQPPRgPVFVSI-------PYDDWDQPAEP--LPARtVSSAVRPDpAALARLGDALDAARR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 240 PVMVGGPKLRVAKATDALVELADASGYALAVMP-SAKGLVPEHHPHFIGtywgaVSTAFCGEIVESADAY----LFAGPI 314
Cdd:PRK07092 209 PALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPmSGRCSFPEDHPLFAG-----FLPASREKISALLDGHdlvlVIGAPV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 315 FNdYSSVGYSLLLKKEKAIIvepdrvKITNGPT------FGCVL---MKDFLKELAKKVKKNTTAYENYRRIFitdgqPP 385
Cdd:PRK07092 284 FT-YHVEGPGPHLPEGAELV------QLTDDPGeaawapMGDAIvgdIRLALRDLLALLPPSARPAPPARPMP-----PP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 386 KCKPNEPLRVNIMFQHIQKMLSADTAVIAE----TGDSWfncQKLKLPnGCGYEFQMQYGSIGWSVGATLGYAQSVPSKR 461
Cdd:PRK07092 352 APAPGEPLSVAFVLQTLAALRPADAIVVEEapstRPAMQ---EHLPMR-RQGSFYTMASGGLGYGLPAAVGVALAQPGRR 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 462 VIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGY--------TIEVEIHDGpyniiknwnyTALVD----AIHNGEG 529
Cdd:PRK07092 428 VIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYgalrwfapVFGVRDVPG----------LDLPGldfvALARGYG 497
|
410 420 430
....*....|....*....|....*....|....*
gi 2047937441 530 kCWTTKVRTEEELIEAIKKATGDKSDSLcfIEVIV 564
Cdd:PRK07092 498 -CEAVRVSDAAELADALARALAADGPVL--VEVEV 529
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
440-562 |
3.52e-13 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 67.23 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 440 YGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTI----EVEIHDGPY-----N 510
Cdd:pfam02775 27 LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGYGMtrgqQTPFGGGRYsgpsgK 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2047937441 511 IIKNWNYTALVDAIHngegkCWTTKVRTEEELIEAIKKATgdKSDSLCFIEV 562
Cdd:pfam02775 107 ILPPVDFAKLAEAYG-----AKGARVESPEELEEALKEAL--EHDGPALIDV 151
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
35-567 |
1.18e-12 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 70.78 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 35 LARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGA 113
Cdd:PRK07789 37 VVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrVGVCMATSGPGATNLVTPIADA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 114 YSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQELR-CFQT--VTCFQAVINNMEEahaqidkaISTALAESkpVYI 190
Cdd:PRK07789 117 NMDSVPVVAITGQVGRGLIGT-----------DAFQEADiVGITmpITKHNFLVTDADD--------IPRVIAEA--FHI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 191 SIScnlpGIPHP-------TFMRDPIPFSISPRLS------NKMGLEAAVEATAAFLNKAVKPVM-VGGPKLRvAKATDA 256
Cdd:PRK07789 176 AST----GRPGPvlvdipkDALQAQTTFSWPPRMDlpgyrpVTKPHGKQIREAAKLIAAARRPVLyVGGGVIR-AEASAE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 257 LVELADASGYALAVMPSAKGLVPEHHPHFIGT--YWGAVS--TAfcgeiVESADAYLFAGPIFNDYSSVGYSLLLKKEKA 332
Cdd:PRK07789 251 LRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTVAavAA-----LQRSDLLIALGARFDDRVTGKLDSFAPDAKV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 333 IIVEPDRVKITNG-----PTFGCVlmKDFLKELAKKVKK--------NTTAY----ENYRRIFITDGQPPKCKPNEPLRV 395
Cdd:PRK07789 326 IHADIDPAEIGKNrhadvPIVGDV--KEVIAELIAALRAehaaggkpDLTAWwaylDGWRETYPLGYDEPSDGSLAPQYV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 396 nimFQHIQKMLSADTAVIAETG---------------DSWFNCQKLklpngcgyefqmqyGSIGWSVGATLGYAQSVPSK 460
Cdd:PRK07789 404 ---IERLGEIAGPDAIYVAGVGqhqmwaaqfidyekpRTWLNSGGL--------------GTMGYAVPAAMGAKVGRPDK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 461 RVIACIGDGSFQVTAQDVSTmirCEQKTI---IFLINNGGYTI--------------EVEIHDGPYNIIknwNYTALVDA 523
Cdd:PRK07789 467 EVWAIDGDGCFQMTNQELAT---CAIEGIpikVALINNGNLGMvrqwqtlfyeerysNTDLHTHSHRIP---DFVKLAEA 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2047937441 524 IhngegKCWTTKVRTEEELIEAIKKATgDKSDSLCFIEVIVHKD 567
Cdd:PRK07789 541 Y-----GCVGLRCEREEDVDAVIEKAR-AINDRPVVIDFVVGKD 578
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
30-498 |
1.74e-12 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 70.03 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPG-DF--------NLTLLDHLIAEPgltnIGCCNELNAGYAADGYARSRG-VGACVVTF 99
Cdd:PRK08327 8 TAAELFLELLKELGVDYIFINSGtDYppiieakaRARAAGRPLPEF----VICPHEIVAISMAHGYALVTGkPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 100 TVGGLSVLNAIAGAYSENLPVICIVG-GPNTND--FGT-NRILHHTIGLFDFSQELRcfqtvtcfQAV-----INNMEEA 170
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGrSPYTEEgeLGSrNTRIHWTQEMRDQGGLVR--------EYVkwdyeIRRGDQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 171 HAQIDKAISTALAESK-PVYISI----SCNlpgiphpTFMRDPIPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGG 245
Cdd:PRK08327 156 GEVVARAIQIAMSEPKgPVYLTLprevLAE-------EVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 246 PKLRVAKATDALVELADAsgYALAVMPSAKGLV--PEHHPHFIGtywgavstAFCGEIVESADAYLFAGpifndySSVGY 323
Cdd:PRK08327 229 RAGRTAEGFASLRRLAEE--LAIPVVEYAGEVVnyPSDHPLHLG--------PDPRADLAEADLVLVVD------SDVPW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 324 SLLLKKEKA----IIVEPDRVKiTNGP--TFGC------------VLMKDFLKELAK-----------KVKKNTTAYENY 374
Cdd:PRK08327 293 IPKKIRPDAdarvIQIDVDPLK-SRIPlwGFPCdlciqadtstalDQLEERLKSLASaerrrarrrraAVRELRIRQEAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 375 RRifitdGQPPKCKPNEPLRVNIMFQHIQKMLSADTAVIAETGdswFNCQKLKLpNGCGYEFQM-QYGSIGWSVGATLGY 453
Cdd:PRK08327 372 KR-----AEIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYP---FVPRQARL-NKPGSYFGDgSAGGLGWALGAALGA 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2047937441 454 AQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLI--NNGGY 498
Cdd:PRK08327 443 KLATPDRLVIATVGDGSFIFGVPEAAHWVAERYGLPVLVVvfNNGGW 489
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
18-496 |
2.50e-12 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 69.45 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 18 TSVTNDAVSPDATLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACV 96
Cdd:PRK06965 10 TAESLSPPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 97 VTFTVGGLSVLNAIAGAYSENLPVICIVGGPNTndfgtnrilhHTIGLfDFSQElrCfQTVTCFQAVINnmeeaHAQIDK 176
Cdd:PRK06965 90 VTSGPGVTNAVTGIATAYMDSIPMVVISGQVPT----------AAIGQ-DAFQE--C-DTVGITRPIVK-----HNFLVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 177 AI-STALAESKPVYISIScnlpGIPHPTFMRDP-----------IPFSISPRLSN--KMGLEAAVEATAAFLNKAVKPVM 242
Cdd:PRK06965 151 DVrDLAETVKKAFYIART----GRPGPVVVDIPkdvsktpceyeYPKSVEMRSYNpvTKGHSGQIRKAVSLLLSAKRPYI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 243 VGGPKLRVAKATDALVELADASGYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVG 322
Cdd:PRK06965 227 YTGGGVILANASRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGML-GMHGTYEANMAMQHCDVLIAIGARFDDRVIGN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 323 YSLLLKKEKAII---VEPD----RVKItNGPTFGCVlmKDFLKELAKKVKKNTT------------AYENYRRI--FITD 381
Cdd:PRK06965 306 PAHFASRPRKIIhidIDPSsiskRVKV-DIPIVGDV--KEVLKELIEQLQTAEHgpdadalaqwwkQIEGWRSRdcLKYD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 382 GQPPKCKPneplrvNIMFQHIQKMLSADTAVIAETGD---------------SWFNCQKLklpngcgyefqmqyGSIGWS 446
Cdd:PRK06965 383 RESEIIKP------QYVVEKLWELTDGDAFVCSDVGQhqmwaaqfyrfneprRWINSGGL--------------GTMGVG 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2047937441 447 VGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNG 496
Cdd:PRK06965 443 LPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNR 492
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
29-495 |
1.12e-11 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 67.55 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 29 ATLGRHLARRLVQIGVSDVFTVPGDFNLTLLDhLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVL 107
Cdd:PRK06457 2 PSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVD-AIRKSKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 108 NAIAGAYSENLPVICIVGGPNTNdfgtnrILHHtiglfDFSQEL---RCFQTVTCFQAVINNMEEAHAQIDKAISTALAE 184
Cdd:PRK06457 81 NGLYDAKMDHAPVIALTGQVESD------MIGH-----DYFQEVnltKLFDDVAVFNQILINPENAEYIIRRAIREAISK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 185 SKPVYIsiscNLP-GIPHPTFMRDPIPFSISPRLSNKMGLEAAVEataaFLNKAVKPVMVGGPKLRvaKATDALVELADA 263
Cdd:PRK06457 150 RGVAHI----NLPvDILRKSSEYKGSKNTEVGKVKYSIDFSRAKE----LIKESEKPVLLIGGGTR--GLGKEINRFAEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 264 SGYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFnDYSsvgySLLLKKEKAIIVEPD----- 338
Cdd:PRK06457 220 IGAPIIYTLNGKGILPDLDPKVMGGI-GLLGTKPSIEAMDKADLLIMLGTSF-PYV----NFLNKSAKVIQVDIDnsnig 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 339 -RVKItngpTFGCVL-MKDFLK-ELAKKVKKNTTAYENYRRIFITDGQPPKCKPNEPLRVNIMFQHIQKMLSADTAVIAE 415
Cdd:PRK06457 294 kRLDV----DLSYPIpVAEFLNiDIEEKSDKFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 416 TGDS--WFNcQKLKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKR-VIACIGDGSFQVTAQDVSTMIRCEQKTIIFL 492
Cdd:PRK06457 370 TGNVtmWTA-RHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIII 448
|
...
gi 2047937441 493 INN 495
Cdd:PRK06457 449 YNN 451
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
35-495 |
1.22e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 67.54 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 35 LARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGA 113
Cdd:PRK08979 10 IVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 114 YSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQE---LRCFQTVTCFQAVINNMEEAHAQIDKAISTA-LAESKPVY 189
Cdd:PRK08979 90 YMDSIPMVVLSGQVPSNLIGN-----------DAFQEcdmIGISRPVVKHSFLVKDAEDIPEIIKKAFYIAsTGRPGPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 190 ISI--SCNLPGIPHPTfmrdPIPFSISPRLSN----------KMGLEAAVEATaaflnkavKPVM-VGGPKLrVAKATDA 256
Cdd:PRK08979 159 IDLpkDCLNPAILHPY----EYPESIKMRSYNpttsghkgqiKRGLQALLAAK--------KPVLyVGGGAI-ISGADKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 257 LVELADASGyaLAVMPSAKGL--VPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAII 334
Cdd:PRK08979 226 ILQLAEKLN--LPVVSTLMGLgaFPGTHKNSLGML-GMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 335 VEPDRVKITNG-----PTFGCV--LMKDFLKELAKKVKKNTTAYENY----------RRIFITDGQPPKCKPNEplrvni 397
Cdd:PRK08979 303 IDIDPSSISKTvrvdiPIVGSAdkVLDSMLALLDESGETNDEAAIASwwneievwrsRNCLAYDKSSERIKPQQ------ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 398 MFQHIQKMLSADTAVIAETGD---------------SWFNCQKLklpngcgyefqmqyGSIGWSVGATLGYAQSVPSKRV 462
Cdd:PRK08979 377 VIETLYKLTNGDAYVASDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAAMGVKFAMPDETV 442
|
490 500 510
....*....|....*....|....*....|...
gi 2047937441 463 IACIGDGSFQVTAQDVSTMIRCEQKTIIFLINN 495
Cdd:PRK08979 443 VCVTGDGSIQMNIQELSTALQYDIPVKIINLNN 475
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
441-564 |
1.95e-11 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 63.00 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 441 GSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRcEQ---KTIIFliNNGGYTI-EVEI-HDGPYNIIKN- 514
Cdd:cd02002 49 GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAAR-YGlpvTVVIL--NNRGYGAlRSFLkRVGPEGPGENa 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2047937441 515 WNYTALVD------AIHNGEGkCWTTKVRTEEELIEAIKKATGDKSDSLcfIEVIV 564
Cdd:cd02002 126 PDGLDLLDpgidfaAIAKAFG-VEAERVETPEELDEALREALAEGGPAL--IEVVV 178
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
32-564 |
2.33e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 66.31 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 32 GRHLARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAI 110
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 111 AGAYSENLPVICIVGgpntndfgtnRILHHTIGLfDFSQE---LRCFQTVTCFQAVINNMEEAHAQIDKAIStaLAES-- 185
Cdd:PRK06466 87 ATAYMDSIPMVVLSG----------QVPSTLIGE-DAFQEtdmVGISRPIVKHSFMVKHASEIPEIIKKAFY--IAQSgr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 -KPVYISISCNLpGIPHPTF---------MRdpipfSISPRLSNKMG-LEAAVEataaFLNKAVKPVMVGGPKLRVAKAT 254
Cdd:PRK06466 154 pGPVVVDIPKDM-TNPAEKFeyeypkkvkLR-----SYSPAVRGHSGqIRKAVE----MLLAAKRPVIYSGGGVVLGNAS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 255 DALVELADASGYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAII 334
Cdd:PRK06466 224 ALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGML-GMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 335 VEPDRVKITNG-----PTFGCVL-----MKDFLKELAKKVKKNTTA--------YENYRRIFITD-GQPPKCKPNEplrv 395
Cdd:PRK06466 303 IDIDPASISKTikadiPIVGPVEsvlteMLAILKEIGEKPDKEALAawwkqideWRGRHGLFPYDkGDGGIIKPQQ---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 396 niMFQHIQKMLSADTAVIAETGD-SWFNCQ--KLKLP----NGCGyefqmqYGSIGWSVGATLGYAQSVPSKRVIACIGD 468
Cdd:PRK06466 379 --VVETLYEVTNGDAYVTSDVGQhQMFAAQyyKFNKPnrwiNSGG------LGTMGFGLPAAMGVKLAFPDQDVACVTGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 469 GSFQVTAQDVSTmirCEQKTI---IFLINNGGYTIEVEIHDGPYNIIKNWNY-------TALVDAI-HNGegkcwtTKVR 537
Cdd:PRK06466 451 GSIQMNIQELST---CLQYGLpvkIINLNNGALGMVRQWQDMQYEGRHSHSYmeslpdfVKLAEAYgHVG------IRIT 521
|
570 580
....*....|....*....|....*..
gi 2047937441 538 TEEELIEAIKKATGDKsDSLCFIEVIV 564
Cdd:PRK06466 522 DLKDLKPKLEEAFAMK-DRLVFIDIYV 547
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
39-496 |
8.46e-11 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 64.72 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 39 LVQIGVSDVFTVPGDFNLTLLDHLIA--EPGL-TNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAY 114
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDELYAweKKGLiKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 115 SENLPVICIVGGPNTNDFGTNrilhhtiglfdfsqelrCFQTVTCFQAVINNMEEAHAQID-KAISTALAES-------- 185
Cdd:CHL00099 100 MDSVPLLVITGQVGRAFIGTD-----------------AFQEVDIFGITLPIVKHSYVVRDaRDISRIVAEAfyiakhgr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 -KPVYISISCNL--------PGIPHPTFMRDP-IPFSISPRLSNkmgleaaVEATAAFLNKAVKPVM-VGGPKLrVAKAT 254
Cdd:CHL00099 163 pGPVLIDIPKDVglekfdyyPPEPGNTIIKILgCRPIYKPTIKR-------IEQAAKLILQSSQPLLyVGGGAI-ISDAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 255 DALVELADASGYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAII 334
Cdd:CHL00099 235 QEITELAELYKIPVTTTLMGKGIFDEDHPLCLGML-GMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 335 VEPDRVKITNG--PTFGCVL-MKDFLKELAKKVKKNTTAYEN------YRRIfitdgqpPKCKPNEPLRVnimfQHIQKM 405
Cdd:CHL00099 314 IDIDPAEIGKNriPQVAIVGdVKKVLQELLELLKNSPNLLESeqtqawRERI-------NRWRKEYPLLI----PKPSTS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 406 LSADTaVIAETG----DSWFN---------------CQKLKLPNGCGyefqmqYGSIGWSVGATLGYAQSVPSKRVIaCI 466
Cdd:CHL00099 383 LSPQE-VINEISqlapDAYFTtdvgqhqmwaaqflkCKPRKWLSSAG------LGTMGYGLPAAIGAQIAHPNELVI-CI 454
|
490 500 510
....*....|....*....|....*....|.
gi 2047937441 467 -GDGSFQVTAQDVSTMIRCEQKTIIFLINNG 496
Cdd:CHL00099 455 sGDASFQMNLQELGTIAQYNLPIKIIIINNK 485
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
37-495 |
1.68e-10 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 63.96 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 37 RRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYS 115
Cdd:PRK09107 19 QALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNAVTPLQDALM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 116 ENLPVICIVGGPNTNDFGTNRILH-HTIGLfdfsqelrcfqTVTCFQA--VINNMEEAHAQIDKAISTALA-ESKPVYIS 191
Cdd:PRK09107 99 DSIPLVCITGQVPTHLIGSDAFQEcDTVGI-----------TRPCTKHnwLVKDVNDLARVIHEAFHVATSgRPGPVVVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 192 ISCNL---PGIPHPTfMRDPIPFSISPRLSNKMgleAAVEATAAFLNKAVKPVMV--GGPKLRVAKATDALVELADASGY 266
Cdd:PRK09107 168 IPKDVqfaTGTYTPP-QKAPVHVSYQPKVKGDA---EAITEAVELLANAKRPVIYsgGGVINSGPEASRLLRELVELTGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 267 ALAVMPSAKGLVPEHHPHFI------GTYWGAVSTAFCgeivesaDAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPD-- 338
Cdd:PRK09107 244 PITSTLMGLGAYPASGKNWLgmlgmhGTYEANMAMHDC-------DVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDps 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 339 ------RVKITNGPTFGCVL--MKDFLKELAKKVKKNTTA-----YENYRRIfitdgQPPKCKPNEPLrvnIMFQH-IQK 404
Cdd:PRK09107 317 sinknvRVDVPIIGDVGHVLedMLRLWKARGKKPDKEALAdwwgqIARWRAR-----NSLAYTPSDDV---IMPQYaIQR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 405 MLSA----DTAVIAETGdswfncqklklpngcgyEFQM---QY---------------GSIGWSVGATLGYAQSVPSKRV 462
Cdd:PRK09107 389 LYELtkgrDTYITTEVG-----------------QHQMwaaQFfgfeepnrwmtsgglGTMGYGLPAALGVQIAHPDALV 451
|
490 500 510
....*....|....*....|....*....|...
gi 2047937441 463 IACIGDGSFQVTAQDVSTMIRCEQKTIIFLINN 495
Cdd:PRK09107 452 IDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
43-495 |
1.80e-10 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 63.60 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 43 GVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 121
Cdd:PLN02470 27 GVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGkVGVCIATSGPGATNLVTGLADALLDSVPLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 122 CIVGGPNTNDFGTnrilhhtiglfDFSQE---LRCFQTVTCFQAVINNMEEahaqIDKAISTA--LAES---KPVYISIS 193
Cdd:PLN02470 107 AITGQVPRRMIGT-----------DAFQEtpiVEVTRSITKHNYLVMDVED----IPRVIREAffLASSgrpGPVLVDIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 194 CNLP---GIPH-PTFMRDPIPFSISPRLSNKMGLEAAVEAtaafLNKAVKPVM-VGGPKLrvaKATDALVELADASGYAL 268
Cdd:PLN02470 172 KDIQqqlAVPNwNQPMKLPGYLSRLPKPPEKSQLEQIVRL----ISESKRPVVyVGGGCL---NSSEELREFVELTGIPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 269 AVMPSAKGLVP---EHHPHFIGTYwGAVSTAFCgeiVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKITNG 345
Cdd:PLN02470 245 ASTLMGLGAFPasdELSLQMLGMH-GTVYANYA---VDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 346 PTFGCVLMKDF---LKELAKKVKKNTTAYENYRR-IFITDGQppkcKPNEPLRVN-----IMFQHIQKMLSADTA--VIA 414
Cdd:PLN02470 321 KQPHVSVCADVklaLQGLNKLLEERKAKRPDFSAwRAELDEQ----KEKFPLSYPtfgdaIPPQYAIQVLDELTDgnAII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 415 ETG--------DSWFNCQKLK--LPNGcgyefqmQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTmIRC 484
Cdd:PLN02470 397 STGvgqhqmwaAQWYKYKEPRrwLTSG-------GLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELAT-IHV 468
|
490
....*....|..
gi 2047937441 485 EQKTI-IFLINN 495
Cdd:PLN02470 469 ENLPVkIMVLNN 480
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
441-567 |
2.32e-08 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 54.04 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 441 GSIGWSVGATLGYAQSVPSKRVIaCI-GDGSFQVTAQDVSTMIRCEQKTIIFLINNGgytieveiHDGpynIIKNW---- 515
Cdd:cd02015 50 GTMGFGLPAAIGAKVARPDKTVI-CIdGDGSFQMNIQELATAAQYNLPVKIVILNNG--------SLG---MVRQWqelf 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047937441 516 --------------NYTALVDAiHNGEGKcwttKVRTEEELIEAIKKATgdKSDSLCFIEVIVHKD 567
Cdd:cd02015 118 yegryshttldsnpDFVKLAEA-YGIKGL----RVEKPEELEAALKEAL--ASDGPVLLDVLVDPE 176
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
30-330 |
4.21e-08 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 56.07 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHLARRLVQIGVSDVFTVPGDFNLTLLDHLI-AEPGLTNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSVL 107
Cdd:PRK08273 4 TVADFILERLREWGVRRVFGYPGDGINGLLGALGrADDKPEFVQARHEEMAAFMAVAHAKfTGEVGVCLATSGPGAIHLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 108 NAIAGAYSENLPVICIVGGPNTNDFGTnrilhhtiglfDFSQEL---RCFQTVTC-FQAVINNMEEAHAQIDKAISTALA 183
Cdd:PRK08273 84 NGLYDAKLDHVPVVAIVGQQARAALGG-----------HYQQEVdlqSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 184 ESKPVYISISCNLPGIPHPtfmrDP------IPFSISPRLSNKMGLEAAVEATAAFLNKAVKPVMVGGPKLRvaKATDAL 257
Cdd:PRK08273 153 ERTVTAVILPNDVQELEYE----PPphahgtVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047937441 258 VELADASGYALAVMPSAKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGpifndySSVGYSLLLKKE 330
Cdd:PRK08273 227 IAVAERLGAGVAKALLGKAALPDDLPWVTGSI-GLLGTKPSYELMRECDTLLMVG------SSFPYSEFLPKE 292
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
43-472 |
1.65e-07 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 54.22 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 43 GVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSR--GVGACVVTftvGGLSVLNAIAGAYS---EN 117
Cdd:PRK11269 18 GVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATagNIGVCIGT---SGPAGTDMITGLYSasaDS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 118 LPVICIVG-GPNTNdfgtnriLHhtiglfdfsQElrcfqtvtCFQAVinNME--------------EAhAQIDKAISTA- 181
Cdd:PRK11269 95 IPILCITGqAPRAR-------LH---------KE--------DFQAV--DIEsiakpvtkwavtvrEP-ALVPRVFQQAf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 182 -LAESK---PVYIS--ISCNLPGIPHPTFMRDPIPFSiSPRLSnkmglEAAVEATAAFLNKAVKPVMVGGPKLRVAKATD 255
Cdd:PRK11269 148 hLMRSGrpgPVLIDlpFDVQVAEIEFDPDTYEPLPVY-KPAAT-----RAQIEKALEMLNAAERPLIVAGGGVINADASD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 256 ALVELADASGyaLAVMPS--AKGLVPEHHPHFIGTYWGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAI 333
Cdd:PRK11269 222 LLVEFAELTG--VPVIPTlmGWGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 334 IV--EPDRVKITNGPTFGCV----LMKDFLKELAKKVKKNTTAYEnyRRIFITDGQPPK----------CKPNEPLRVni 397
Cdd:PRK11269 300 HVdiEPTQIGRVFGPDLGIVsdakAALELLVEVAREWKAAGRLPD--RSAWVADCQERKrtllrkthfdNVPIKPQRV-- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 398 mFQHIQKMLSADTAVIAETGDS---------------WFNCQklklpngcgyefqmQYGSIGWSVGATLGYAQSVPSKRV 462
Cdd:PRK11269 376 -YEEMNKAFGRDTCYVSTIGLSqiaaaqflhvykprhWINCG--------------QAGPLGWTIPAALGVRAADPDRNV 440
|
490
....*....|
gi 2047937441 463 IACIGDGSFQ 472
Cdd:PRK11269 441 VALSGDYDFQ 450
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
433-562 |
2.94e-07 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 51.15 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 433 GYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGYTI------------ 500
Cdd:cd02003 40 GYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCinnlqestgsgs 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047937441 501 ---EVEIHDgpyNIIKNWNYTAL-VDAIHNGEGK-CWTTKVRTEEELIEAIKKAtgDKSDSLCFIEV 562
Cdd:cd02003 120 fgtEFRDRD---QESGQLDGALLpVDFAANARSLgARVEKVKTIEELKAALAKA--KASDRTTVIVI 181
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
37-495 |
7.65e-07 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 52.16 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 37 RRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYS 115
Cdd:PRK07979 12 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 116 ENLPVICIVGGPNTNDFGtnrilhhtiglFDFSQELRCF---QTVTCFQAVINNMEEAHAQIDKAISTAlAESKPVYISI 192
Cdd:PRK07979 92 DSIPLVVLSGQVATSLIG-----------YDAFQECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFWLA-ASGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 193 scNLP-GIPHPTF-MRDPIPFSISPRLSNKM--GLEAAVEATAAFLNKAVKPVM-VGGPKLRvAKATDALVELADAsgYA 267
Cdd:PRK07979 160 --DLPkDILNPANkLPYVWPESVSMRSYNPTtqGHKGQIKRALQTLVAAKKPVVyVGGGAIN-AACHQQLKELVEK--LN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 268 LAVMPSAKGL--VPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVEPDRVKITNG 345
Cdd:PRK07979 235 LPVVSSLMGLgaFPATHRQSLGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 346 -----PTFG-----CVLMKDFLKELAKK-----VKKNTTAYENY--RRIFITDGQPPKCKPNEPLRVnimfqhIQKMLSA 408
Cdd:PRK07979 314 vtadiPIVGdarqvLEQMLELLSQESAHqpldeIRDWWQQIEQWraRQCLKYDTHSEKIKPQAVIET------LWRLTKG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 409 DTAVIAETGD---------------SWFNCQKLklpngcgyefqmqyGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQV 473
Cdd:PRK07979 388 DAYVTSDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 453
|
490 500
....*....|....*....|..
gi 2047937441 474 TAQDVSTMIRCEQKTIIFLINN 495
Cdd:PRK07979 454 NIQELSTALQYELPVLVLNLNN 475
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
39-496 |
6.90e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 48.89 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 39 LVQIGVSDVFTVPGDFNLTLLDHL-IAEPG--LTNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAY 114
Cdd:PRK07418 29 LKRHGVKHIFGYPGGAILPIYDELyKAEAEgwLKHILVRHEQGAAHAADGYARATGkVGVCFGTSGPGATNLVTGIATAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 115 SENLPVICI---VGGPN--TNDFGTNRILHHTIGLFDFSQELRcfqtvtcfqavinnmeeAHAQIDKAISTA--LAES-- 185
Cdd:PRK07418 109 MDSVPMVVItgqVPRPAigTDAFQETDIFGITLPIVKHSYVVR-----------------DPSDMARIVAEAfhIASSgr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 186 -KPVYISI-------SCN----LPGIPHPTFMRDPIPfsisprlsnkmGLEAAVEATAAFLNKAVKPVM-VGGPKLrVAK 252
Cdd:PRK07418 172 pGPVLIDIpkdvgqeEFDyvpvEPGSVKPPGYRPTVK-----------GNPRQINAALKLIEEAERPLLyVGGGAI-SAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 253 ATDALVELADAsgYALAVMPS--AKGLVPEHHPHFIGTYwGAVSTAFCGEIVESADAYLFAGPIFNDYSSVGYSLLLKKE 330
Cdd:PRK07418 240 AHAELKELAER--FQIPVTTTlmGKGAFDEHHPLSVGML-GMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 331 KAIIVE--PDRVKITNGPT------FGCVLMKDFLKELAKKVKKNTTAYENyrRIfitdgqpPKCKPNEPLRVnimfQHI 402
Cdd:PRK07418 317 KVIHIDidPAEVGKNRRPDvpivgdVRKVLVKLLERSLEPTTPPRTQAWLE--RI-------NRWKQDYPLVV----PPY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 403 QKMLSADTaVIAETGDswfncqklKLPNgcGY------EFQM---QY--------------GSIGWSVGATLGYAQSVPS 459
Cdd:PRK07418 384 EGEIYPQE-VLLAVRD--------LAPD--AYyttdvgQHQMwaaQFlrngprrwissaglGTMGFGMPAAMGVKVALPD 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 2047937441 460 KRVIaCI-GDGSFQVTAQDVSTMIRCEQKTIIFLINNG 496
Cdd:PRK07418 453 EEVI-CIaGDASFLMNIQELGTLAQYGINVKTVIINNG 489
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
389-549 |
1.69e-05 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 46.12 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 389 PNEPLRVnimFQHIQKMLSADTAVIAETGDS---------------WFNCQklklpngcgyefqmQYGSIGWSVGATLGY 453
Cdd:cd02006 7 PIKPQRV---YEEMNKAFGRDVRYVTTIGLSqiagaqmlhvykprhWINCG--------------QAGPLGWTVPAALGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 454 AQSVPSKRVIACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNG----------GYTIEVEIHDGPYNIIKNWNYTALVDA 523
Cdd:cd02006 70 AAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAylglirqaqrAFDMDYQVNLAFENINSSELGGYGVDH 149
|
170 180
....*....|....*....|....*..
gi 2047937441 524 IHNGEG-KCWTTKVRTEEELIEAIKKA 549
Cdd:cd02006 150 VKVAEGlGCKAIRVTKPEELAAAFEQA 176
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
392-498 |
1.80e-05 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 45.36 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 392 PLRVnimFQHIQKMLSADTAVIAETG--DSWFN----CQKlklPNGCGYEFQMQYGSIG--WSVGATLGYaqsvPSKRVI 463
Cdd:cd02010 1 PQRI---VHDLRAVMGDDDIVLLDVGahKIWMAryyrTYA---PNTCLISNGLATMGVAlpGAIGAKLVY----PDRKVV 70
|
90 100 110
....*....|....*....|....*....|....*
gi 2047937441 464 ACIGDGSFQVTAQDVSTMIRCEQKTIIFLINNGGY 498
Cdd:cd02010 71 AVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGY 105
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
392-568 |
2.12e-05 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 45.21 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 392 PLRVNIMFQHIQKMLSADTAVIAETGDS--WFNcQKLKLPNGCGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDG 469
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVtvWAA-RHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 470 SFQVTAQDVSTMIRCEQKTIIFLINNG--GYtIEVEIHDGPYNII----KNWNYTALVDAIHngeGKCWTtkVRTEEELI 543
Cdd:cd02014 80 GFAMLMGDLITAVKYNLPVIVVVFNNSdlGF-IKWEQEVMGQPEFgvdlPNPDFAKIAEAMG---IKGIR--VEDPDELE 153
|
170 180
....*....|....*....|....*
gi 2047937441 544 EAIKKATgdKSDSLCFIEVIVHKDD 568
Cdd:cd02014 154 AALDEAL--AADGPVVIDVVTDPNE 176
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
441-500 |
2.58e-05 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 47.15 E-value: 2.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047937441 441 GSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRcEQ---KTIIFliNNGGYTI 500
Cdd:PRK07586 385 GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQAR-ENldvTTVIF--ANRAYAI 444
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-500 |
2.66e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 42.51 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 406 LSADTAVIAETG----DSWFNCQKLKlpngcgyEFQMqYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTM 481
Cdd:PRK06163 26 LKDEEAVIGGIGntnfDLWAAGQRPQ-------NFYM-LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTI 97
|
90 100
....*....|....*....|
gi 2047937441 482 IRCEQKTIIFLI-NNGGYTI 500
Cdd:PRK06163 98 AALAPKNLTIIVmDNGVYQI 117
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
405-564 |
5.21e-04 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 41.34 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 405 MLSADTAVIAETGDSWFNCQKLKlpngcGYEFQMQYGSIGWSVGATLGYAQSVPSKRVIACIGDGSFQVTAQDVSTMIRC 484
Cdd:cd02013 22 IVSTDIGNICSVANSYLRFEKPR-----SFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMMEIMTAVRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 485 EQKTIIFLINNGGYTIE----VEIHDGPY--NIIKNWNYTALVDAIhNGEGkcwtTKVRTEEELIEAIKKATGD-KSDSL 557
Cdd:cd02013 97 KLPVTAVVFRNRQWGAEkknqVDFYNNRFvgTELESESFAKIAEAC-GAKG----ITVDKPEDVGPALQKAIAMmAEGKT 171
|
....*..
gi 2047937441 558 CFIEVIV 564
Cdd:cd02013 172 TVIEIVC 178
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
30-284 |
6.39e-04 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 42.67 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 30 TLGRHL-ARRLVQIGVSDVFTVPGdFNLTLLDHLIAEPGLTNIGCCNELNAGYAA--DGYARSRGvGACVVTFTVGGLSV 106
Cdd:PRK09259 10 TDGFHLvIDALKLNGIDTIYGVVG-IPITDLARLAQAEGIRYIGFRHEQSAGNAAaaAGFLTQKP-GVCLTVSAPGFLNG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 107 LNAIAGAYSENLPVICIVGGpntndfgTNRilhHTIglfDFSQ----EL------RCFqtvtCFQAV-INNMEEAHAQID 175
Cdd:PRK09259 88 LTALANATTNCFPMIMISGS-------SER---EIV---DLQQgdyeELdqlnaaKPF----CKAAFrVNRAEDIGIGVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 176 KAISTALAeSKP--VYISISCNLPG------IPHPTFMR--DPIPFSISPRlsnkmgleAAVEATAAFLNKAVKPVMVGG 245
Cdd:PRK09259 151 RAIRTAVS-GRPggVYLDLPAKVLAqtmdadEALTSLVKvvDPAPAQLPAP--------EAVDRALDLLKKAKRPLIILG 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 2047937441 246 PKLRVAKATDALVELADASGYALAVMPSAKGLVPEHHPH 284
Cdd:PRK09259 222 KGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQ 260
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
33-121 |
2.40e-03 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 39.02 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 33 RHLARRLVQIGVSDVFTVPGDFN--LTLLdhLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTfTvGGLSVLN-- 108
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSapLALA--AAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVC-T-SGTAVANll 76
|
90
....*....|....
gi 2047937441 109 -AIAGAYSENLPVI 121
Cdd:cd07037 77 pAVVEAYYSGVPLL 90
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
35-125 |
6.72e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 39.44 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047937441 35 LARRLVQIGVSDVFTVPGDFNLTLLDHLIAEPGLTNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSvlNAIAgay 114
Cdd:PRK07586 7 LVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLA--NGLA--- 81
|
90
....*....|....*....
gi 2047937441 115 seNL--------PVICIVG 125
Cdd:PRK07586 82 --NLhnarrartPIVNIVG 98
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|
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