|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
32-603 |
0e+00 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 1337.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 32 SAPITTTSESTLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTF 111
Cdd:PLN02573 7 PATPVSSSDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 112 TVGGLSVLNAIAGAYSENLPVICIVGGPNSNDFGTNRILHHTIGLPDFSQELRCFQTVTCYQAVVNNLEDAHEQIDKAIA 191
Cdd:PLN02573 87 TVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAIS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 192 TALKESKPVYISISCNLAATPHPTFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLE 271
Cdd:PLN02573 167 TALKESKPVYISVSCNLAAIPHPTFSREPVPFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 272 LADASGYPLAVMPSTKGLVPENHPHFIGTYWGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIIVHPDR 351
Cdd:PLN02573 247 LADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 352 VVVANGPTFGCVLMSDFFRELAKRVKRNETAYENYERIFVPEGKPLKCKPGEPLRVNAMFQHIQKMLSSETAVIAETGDS 431
Cdd:PLN02573 327 VTIGNGPAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 432 WFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYT 511
Cdd:PLN02573 407 WFNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 512 IEVEIHDGPYNVIKNWNYTGLVDAIHNGEGKCWTTKVRYEEELVEAIKTATTEKKDSLCFIEVIVHKDDTSKELLEWGSR 591
Cdd:PLN02573 487 IEVEIHDGPYNVIKNWNYTGLVDAIHNGEGKCWTAKVRTEEELIEAIATATGEKKDCLCFIEVIVHKDDTSKELLEWGSR 566
|
570
....*....|..
gi 15240950 592 VSAANGRPPNPQ 603
Cdd:PLN02573 567 VSAANSRPPNPQ 578
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
42-591 |
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: 665.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNA 121
Cdd:COG3961 6 TVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAING 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 122 IAGAYSENLPVICIVGGPNSNDFGTNRILHHTIGLPDFSQELRCFQTVTCYQAVVNNlEDAHEQIDKAIATALKESKPVY 201
Cdd:COG3961 86 IAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVLTP-ENAAAEIDRVLAAALREKRPVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 202 ISISCNLAATPhptFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLA 281
Cdd:COG3961 165 IELPRDVADAP---IEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 282 VMPSTKGLVPENHPHFIGTYWGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIIVHPDRVVVAnGPTFG 361
Cdd:COG3961 242 TTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVG-GHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 362 CVLMSDFFRELAKRVKRNETAYEnYERIFVPEGKPlkcKPGEPLRVNAMFQHIQKMLSSETAVIAETGDSWFNCQKLKLP 441
Cdd:COG3961 321 GVSLADFLEALAELLKKRSAPLP-APAPPPPPPPA---APDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRLP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 442 KGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTIEVEIH--DG 519
Cdd:COG3961 397 EGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHgpDG 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240950 520 PYNVIKNWNYTGLVDAIHNGEGKCWttKVRYEEELVEAIKTAtTEKKDSLCFIEVIVHKDDTSKELLEWGSR 591
Cdd:COG3961 477 PYNDIANWDYAKLPEAFGGGNALGF--RVTTEGELEEALAAA-EANTDRLTLIEVVLDKMDAPPLLKRLGKA 545
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
45-206 |
8.80e-92 |
|
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: 279.76 E-value: 8.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 45 RHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAG 124
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 125 AYSENLPVICIVGGPNSNDFGTNRILHHTIGLPDFSQELRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKESKPVYISI 204
Cdd:cd07038 81 AYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEI 160
|
..
gi 15240950 205 SC 206
Cdd:cd07038 161 PR 162
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
404-586 |
1.01e-89 |
|
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: 275.18 E-value: 1.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 404 PLRVNAMFQHIQKMLSSETAVIAETGDSWFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSF 483
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 484 QVTAQDISTMIRNGQKAIIFLINNGGYTIEVEIHDG--PYNVIKNWNYTGLVDAIhNGEGKCWTTKVRYEEELVEAIKTA 561
Cdd:cd02005 81 QMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPeaSYNDIANWNYTKLPEVF-GGGGGGLSFRVKTEGELDEALKDA 159
|
170 180
....*....|....*....|....*
gi 15240950 562 tTEKKDSLCFIEVIVHKDDTSKELL 586
Cdd:cd02005 160 -LFNRDKLSLIEVILPKDDAPEALK 183
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
42-580 |
7.59e-75 |
|
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: 248.54 E-value: 7.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLN 120
Cdd:COG0028 4 TGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 121 AIAGAYSENLPVICIVGGPNSNDFGTNRIlhhtiglpdfsQEL---RCFQTVTCYQAVVNNLEDAHEQIDKAIATALKES 197
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGRGAF-----------QEVdqvGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 198 K-PVYISISCNLAATPhptFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADAS 276
Cdd:COG0028 153 PgPVVLDIPKDVQAAE---AEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 277 GYPLAVMPSTKGLVPENHPHFIGTyWGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIIVHPDRVVVAN 356
Cdd:COG0028 230 GAPVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 357 GPTFGCVLMSD---FFRELAKRVKRNETAYENY-ERIFVPEGKPLK--CKPGEPLRVNAMFQHIQKMLSSETAVIAETGD 430
Cdd:COG0028 309 NYPVDLPIVGDakaVLAALLEALEPRADDRAAWlARIAAWRAEYLAayAADDGPIKPQRVIAALREALPDDAIVVTDVGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 431 S--WFNcQKLKLPKGcgyefqMQY------GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAII 502
Cdd:COG0028 389 HqmWAA-RYLRFRRP------RRFltsgglGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 503 FLINNGGYTIEVEIHDGPYN------VIKNWNYTGLVDAIHngegkCWTTKVRYEEELVEAIKTATTEKKdsLCFIEVIV 576
Cdd:COG0028 462 VVLNNGGLGMVRQWQELFYGgrysgtDLPNPDFAKLAEAFG-----AKGERVETPEELEAALEEALASDG--PALIDVRV 534
|
....
gi 15240950 577 HKDD 580
Cdd:COG0028 535 DPEE 538
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
43-214 |
9.69e-39 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 140.06 E-value: 9.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 43 LGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSVLNA 121
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARaTGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 122 IAGAYSENLPVICIVGGPNSNDFGTnrilHHTIGLPDFSQELRCFqtvTCYQAVVNNLEDAHEQIDKAIATALKESK-PV 200
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGR----GALQQELDQLALFRPV---TKWAVRVTSADEIPEVLRRAFRAALSGRPgPV 153
|
170
....*....|....
gi 15240950 201 YISISCNLAATPHP 214
Cdd:pfam02776 154 YLEIPLDVLLEEVD 167
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
50-206 |
2.09e-32 |
|
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: 122.07 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 50 RLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAGAYSEN 129
Cdd:cd06586 6 VLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240950 130 LPVICIVGGPNSNDFGTnrilhhtiGLPDFSQELRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKESKPVYISISC 206
Cdd:cd06586 86 LPVVFLIGARGISAQAK--------QTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
49-204 |
1.48e-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: 119.94 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 49 RRLVQAGVTDVFSVPGDFNLTLLDHLiAEPELNNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSVLNAIAGAYS 127
Cdd:cd07035 5 EALKAEGVDHVFGVPGGAILPLLDAL-ARSGIRYILVRHEQGAVGMADGYARaTGKPGVVLVTSGPGLTNAVTGLANAYL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240950 128 ENLPVICIVGGPNSNDFGTNRilhhtigLPDFSQeLRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKESK-PVYISI 204
Cdd:cd07035 84 DSIPLLVITGQRPTAGEGRGA-------FQEIDQ-VALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPgPVALDL 153
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
42-580 |
2.86e-26 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 113.18 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHL-IAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVtftVGGLSVL 119
Cdd:PRK08266 5 TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALyKAGDRIRVIHTRHEQAAGYMAFGYARSTGrPGVCSV---VPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 120 NAIAG---AYSENLPVICIVGGPNSNDFGTNR-ILHHtigLPDFSQELRCFqtvTCYQAVVNNLEDAHEQIDKAIATALK 195
Cdd:PRK08266 82 NAGAAlltAYGCNSPVLCLTGQIPSALIGKGRgHLHE---MPDQLATLRSF---TKWAERIEHPSEAPALVAEAFQQMLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 196 -ESKPVYIsiscnlaATPHPTF-ARDPV-PFDLTPRMSNTMGLEAAVEATLEFLNKAVKPV-MVGGPklrVAKASEAFLE 271
Cdd:PRK08266 156 gRPRPVAL-------EMPWDVFgQRAPVaAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMiFVGGG---AAGAGEEIRE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 272 LADASGYPLAVMPSTKGLVPENHP---HFIGTYwgavstpfcsEIVESADAYIFAGPIFNDySSVGYSLLLKKEKAIIVH 348
Cdd:PRK08266 226 LAEMLQAPVVAFRSGRGIVSDRHPlglNFAAAY----------ELWPQTDVVIGIGSRLEL-PTFRWPWRPDGLKVIRID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 349 PD-RVVVANGPTFGCV---------LMSDFFRELAKRVKRNETAYENYERIFvpegkplkckpgeplrvnAMFQHIQKML 418
Cdd:PRK08266 295 IDpTEMRRLKPDVAIVadakagtaaLLDALSKAGSKRPSRRAELRELKAAAR------------------QRIQAVQPQA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 419 SSETAVIAETGD--------------SWFnCQKLKLPK---GCGYEfqmqyGSIGWSVGATLGYAQATPEKRVLSFIGDG 481
Cdd:PRK08266 357 SYLRAIREALPDdgifvdelsqvgfaSWF-AFPVYAPRtfvTCGYQ-----GTLGYGFPTALGAKVANPDRPVVSITGDG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 482 SFQVTAQDISTMIRNGQKAIIFLINNGGY----TIEVEIHDGPY--NVIKNWNYTGLVDAIhnGEGKCwttKVRYEEELV 555
Cdd:PRK08266 431 GFMFGVQELATAVQHNIGVVTVVFNNNAYgnvrRDQKRRFGGRVvaSDLVNPDFVKLAESF--GVAAF---RVDSPEELR 505
|
570 580
....*....|....*....|....*
gi 15240950 556 EAIKTATteKKDSLCFIEVIVHKDD 580
Cdd:PRK08266 506 AALEAAL--AHGGPVLIEVPVPRGS 528
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
239-354 |
2.16e-24 |
|
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: 98.79 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 239 VEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGtYWGAVSTPFCSEIVESAD 318
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 15240950 319 AYIFAGPIFNDYSSVGYSLLLKKEKAII-VHPDRVVV 354
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPDAKIIhIDIDPAEI 116
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
36-512 |
5.60e-24 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 106.11 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 36 TTTSESTLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVG 114
Cdd:PRK08199 3 STPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGrPGICFVTRGPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 115 GLsvlNAIAG---AYSENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQEL---RCFQTVTCYQAVVNNLEDAHEQIDK 188
Cdd:PRK08199 83 AT---NASIGvhtAFQDSTPMILFVG----------QVARDFREREAF-QEIdyrRMFGPMAKWVAEIDDAARIPELVSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 189 AIATALK-ESKPVYISISCN-LAATPHPTFARDPVPFDLTPRmsntmglEAAVEATLEFLNKAVKPVMVGGPKLRVAKAS 266
Cdd:PRK08199 149 AFHVATSgRPGPVVLALPEDvLSETAEVPDAPPYRRVAAAPG-------AADLARLAELLARAERPLVILGGSGWTEAAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 267 EAFLELADASGYPLAVMPSTKGLVPENHPHFIGTY-WGAvsTPFCSEIVESADAYIFAGPIFNDYSSVGYSLL---LKKE 342
Cdd:PRK08199 222 ADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDLgLGI--NPALAARIREADLVLAVGTRLGEVTTQGYTLLdipVPRQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 343 KAIIVHPD-----RV------VVANGPTFGCVLMSdffRELAKRVKRNE---TAYENYERifvpEGKPLKCkPGePLRVN 408
Cdd:PRK08199 300 TLVHVHPDaeelgRVyrpdlaIVADPAAFAAALAA---LEPPASPAWAEwtaAAHADYLA----WSAPLPG-PG-AVQLG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 409 AMFQHIQKMLSSETAVIAETGD--SW------FncqklklpkgcgYEFQMQY----GSIGWSVGATLGYAQATPEKRVLS 476
Cdd:PRK08199 371 EVMAWLRERLPADAIITNGAGNyaTWlhrffrF------------RRYRTQLaptsGSMGYGLPAAIAAKLLFPERTVVA 438
|
490 500 510
....*....|....*....|....*....|....*..
gi 15240950 477 FIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGY-TI 512
Cdd:PRK08199 439 FAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
42-580 |
2.26e-23 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 104.31 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPE-LNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVL 119
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDkIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 120 NAIAGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQEL---RCFQTVTCYQAVVNNLEDAHEQIDKAIATALKE 196
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGT-----------DFFQEVnleKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 197 SKPVYISISCNLAATPHPTFARDPVP-FDLTPRMSNTMGLEAAVEAtlefLNKAVKPVMVGGPKLRVAKasEAFLELADA 275
Cdd:PRK08611 154 KGVAVLTIPDDLPAQKIKDTTNKTVDtFRPTVPSPKPKDIKKAAKL----INKAKKPVILAGLGAKHAK--EELLAFAEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 276 SGYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGpifNDYSSVGYslLLKKEKAIIVHPD----- 350
Cdd:PRK08611 228 AKIPIIHTLPAKGIIPDDHPYSLGNL-GKIGTKPAYEAMQEADLLIMVG---TNYPYVDY--LPKKAKAIQIDTDpanig 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 -RVVVANGptfgcvLMSD---FFRELAKRVKRNEtayenyERIFVPEGKPLKCK-----------PGEPLRVNAMFQHIQ 415
Cdd:PRK08611 302 kRYPVNVG------LVGDakkALHQLTENIKHVE------DRRFLEACQENMAKwwkwmeedennASTPIKPERVMAAIQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 416 KMLSSETAVIAETGDS--WfNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTM 493
Cdd:PRK08611 370 KIADDDAVLSVDVGTVtvW-SARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 494 IRNGQKAIIFLINNGGYT-IEVEihdgpYNVIKNWNY-TGLVDAIH-----NGEGKCWTtkVRYEEELVEAIKTATTEKK 566
Cdd:PRK08611 449 VKYKLPIVVVVLNNQQLAfIKYE-----QQAAGELEYaIDLSDMDYakfaeACGGKGYR--VEKAEELDPAFEEALAQDK 521
|
570
....*....|....
gi 15240950 567 DslCFIEVIVHKDD 580
Cdd:PRK08611 522 P--VIIDVYVDPNA 533
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
95-579 |
4.90e-23 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 103.35 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 95 ADGYARS---RGVGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGpnsndfgTNRILHHTigLPDFSQeLRCFQTVTC 171
Cdd:PRK06154 70 ADGYARAtsgERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTG-------YPRGSTDV--APNFES-LRNYRHITK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 172 YQAVVNNLEDAHEQIDKAIaTALKESK--PVYISISCNLAATPHPTfardpVPFDLTP-RMSNTMGLEAAVEATLEFLNK 248
Cdd:PRK06154 140 WCEQVTLPDEVPELMRRAF-TRLRNGRpgPVVLELPVDVLAEELDE-----LPLDHRPsRRSRPGADPVEVVEAAALLLA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 249 AVKPVMVGGPKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGT---YWGAVSTPFCSEivesADAyIFAgp 325
Cdd:PRK06154 214 AERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSggrARPATVAHFLRE----ADV-LFG-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 326 IFNDYSSVGYSLLLKKEKAII------VHPDRVVVANGPTFG--CVLMSDFFRELAKRV-----KRNETAYENYE--RIF 390
Cdd:PRK06154 287 IGCSLTRSYYGLPMPEGKTIIhstlddADLNKDYPIDHGLVGdaALVLKQMIEELRRRVgpdrgRAQQVAAEIEAvrAAW 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 391 VPEGKPL---KCKPGEPLRVnamFQHIQKMLSSETAVIAETGDS-------WFNCQKLKLPKGCGYEFQMQYGsIGWSVG 460
Cdd:PRK06154 367 LAKWMPKltsDSTPINPYRV---VWELQHAVDIKTVIITHDAGSprdqlspFYVASRPGSYLGWGKTTQLGYG-LGLAMG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 461 ATLgyaqATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTIEVEIHDGPYNVIKNWNYTGLVDAIHNGE 540
Cdd:PRK06154 443 AKL----ARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFSMGGYDKVMPVSTTKYRATDISGDYAAIARAL 518
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15240950 541 GkCWTTKVRYEEELVEAIKTATTEKKDSL-CFIEVIVHKD 579
Cdd:PRK06154 519 G-GYGERVEDPEMLVPALLRALRKVKEGTpALLEVITSEE 557
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
32-575 |
6.32e-22 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 99.84 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 32 SAPiTTTSESTLGRHLSRRLVQAGVTDVF--SVPGDFnltlldHLIAEP-ELNNIGCCNELNAGYAADGYAR-SRGVGac 107
Cdd:PRK06112 6 SAP-GFTLNGTVAHAIARALKRHGVEQIFgqSLPSAL------FLAAEAiGIRQIAYRTENAGGAMADGYARvSGKVA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 108 VVTFTVGGLSVL--NAIAGAYSENLPVICIVGGPNSNDFGTNRI--LHHtIGLpdfsqelrcFQTVTCYQAVVNNLEDAH 183
Cdd:PRK06112 77 VVTAQNGPAATLlvAPLAEALKASVPIVALVQDVNRDQTDRNAFqeLDH-IAL---------FQSCTKWVRRVTVAERID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 184 EQIDKAIATALK-ESKPVYISISCNLAATPHPTFArdpvpfdltPRMSNTMG---------LEAAVEATLEFLNKAVKPV 253
Cdd:PRK06112 147 DYVDQAFTAATSgRPGPVVLLLPADLLTAAAAAPA---------APRSNSLGhfpldrtvpAPQRLAEAASLLAQAQRPV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 254 MVGGPKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGTYWGAV----STPFCSEIVESADAYIFAGPIFND 329
Cdd:PRK06112 218 VVAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGSLMgprsPGRHLRDLVREADVVLLVGTRTNQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 330 YSSVGYSLLlkKEKAIIVHPD-------------RVVVANGPTFGCVLMSDFFRELAKRVKRN---ETAYENYERIFVPE 393
Cdd:PRK06112 298 NGTDSWSLY--PEQAQYIHIDvdgeevgrnyealRLVGDARLTLAALTDALRGRDLAARAGRRaalEPAIAAGREAHRED 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 394 GKPLKCKPGEPLRVNAMFQHIQKMLSSETAVIAETGDS--WFnCQKLKLPKGcGYEFQMQYG--SIGWSVGATLGYAQAT 469
Cdd:PRK06112 376 SAPVALSDASPIRPERIMAELQAVLTGDTIVVADASYSsiWV-ANFLTARRA-GMRFLTPRGlaGLGWGVPMAIGAKVAR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 470 PEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNG--GYTIEVEihdgpynVIKNWNYTglvDAIHNGE------- 540
Cdd:PRK06112 454 PGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGFQKHAE-------TVKFGTHT---DACHFAAvdhaaia 523
|
570 580 590
....*....|....*....|....*....|....*..
gi 15240950 541 GKCWTTKVRYEE--ELVEAIKTAttEKKDSLCFIEVI 575
Cdd:PRK06112 524 RACGCDGVRVEDpaELAQALAAA--MAAPGPTLIEVI 558
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
49-507 |
2.00e-21 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 98.24 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 49 RRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGA-CVVTFTVGGLSVLNAIAGAYS 127
Cdd:PRK08155 21 RLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAvCMACSGPGATNLVTAIADARL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 128 ENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQELRCFQT---VTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYI 202
Cdd:PRK08155 101 DSIPLVCITGQVPASMIGT-----------DAFQEVDTYGIsipITKHNYLVRDIEELPQVISDAfrIAQSGRPG-PVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 203 SI-------SCNLAATPHPTFARDPVPFDltprmsntmglEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADA 275
Cdd:PRK08155 169 DIpkdvqtaVIELEALPAPAEKDAAPAFD-----------EESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 276 SGYPLAVMPSTKGLVPENHPHFIGT--YWGAVSTPFcseIVESADAYIFAGPIFNDySSVGyslllKKEK----AIIVHP 349
Cdd:PRK08155 238 AQLPTTMTLMALGMLPKAHPLSLGMlgMHGARSTNY---ILQEADLLIVLGARFDD-RAIG-----KTEQfcpnAKIIHV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 350 D----------RVVVANGPTFGCVLmsdffRELAKRVKRNETA-----YENYERIFvPEGKPlkcKPGEPLRVNAMFQHI 414
Cdd:PRK08155 309 DidraelgkikQPHVAIQADVDDVL-----AQLLPLVEAQPRAewhqlVADLQREF-PCPIP---KADDPLSHYGLINAV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 415 QKMLSSETAVIAETGDS--W------FNCQKLKLPKGcgyefqmQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVT 486
Cdd:PRK08155 380 AACVDDNAIITTDVGQHqmWtaqaypLNRPRQWLTSG-------GLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMN 452
|
490 500
....*....|....*....|.
gi 15240950 487 AQDISTMIRNGQKAIIFLINN 507
Cdd:PRK08155 453 IQEMATAAENQLDVKIILMNN 473
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
51-494 |
2.61e-21 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 97.99 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHLI---AEPELNNIGCCNELNAGYAADGYARSRGV-GACVVTFTVGGLSVLNAIAGAY 126
Cdd:PRK06456 12 LKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTTNLVTGLITAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 127 SENLPVICIVGGPNSNDFGTNRILH-HTIGLpdfsqelrcFQTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYIS 203
Cdd:PRK06456 92 WDSSPVIAITGQVPRSVMGKMAFQEaDAMGV---------FENVTKYVIGIKRIDEIPQWIKNAfyIATTGRPG-PVVID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 204 ISCNLAATPHPTFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLAVM 283
Cdd:PRK06456 162 IPRDIFYEKMEEIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 284 PSTKGLVPENHPHFIGT--YWGAVSTPFCSeiVESaDAYIFAGPIFNDYSSVGYSLLLKKEKAII------------VHP 349
Cdd:PRK06456 242 FPGKTAIPHDHPLYFGPmgYYGRAEASMAA--LES-DAMLVVGARFSDRTFTSYDEMVETRKKFImvnidptdgekaIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 350 DRVVVANGPTFGCVLMSDfFRELAKR------VKRNETAYENYERIFVPEGkPLKCKPGEPLRVnamfqhIQKMLSSETA 423
Cdd:PRK06456 319 DVGIYGNAKIILRELIKA-ITELGQKrdrsawLKRVKEYKEYYSQFYYTEE-NGKLKPWKIMKT------IRQALPRDAI 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240950 424 VIAETGDS-------WFNCQKLKLPKGCGyefqmqYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMI 494
Cdd:PRK06456 391 VTTGVGQHqmwaevfWEVLEPRTFLTSSG------MGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAV 462
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
37-576 |
7.47e-21 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 96.61 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 37 TTSEStlgrhLSRRLVQAGVTDVFSVPGDFNLTLLDhLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGG 115
Cdd:PRK07525 7 TPSEA-----FVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 116 LSVLNAIAGAYSENLPVICIvggpnsndfgTNRILHHTIGLPDFsQE---LRCFQTVTCYQAVVNNLEDAHEQIDKAIAT 192
Cdd:PRK07525 81 TNFVTAVATAYWAHTPVVLV----------TPQAGTKTIGQGGF-QEaeqMPMFEDMTKYQEEVRDPSRMAEVLNRVFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 193 ALKESKPVYISIscnlaatphptfARD----------PVPFDLtPRMSntmGLEAAVEATLEFLNKAVKPVMVGGPKLRV 262
Cdd:PRK07525 150 AKRESGPAQINI------------PRDyfygvidveiPQPVRL-ERGA---GGEQSLAEAAELLSEAKFPVILSGAGVVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 263 AKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGT--YWGAVSTpfcSEIVESADAYIFAGPIFNDYSSV-GYSL-L 338
Cdd:PRK07525 214 SDAIEECKALAERLDAPVACGYLHNDAFPGSHPLWVGPlgYNGSKAA---MELIAKADVVLALGTRLNPFGTLpQYGIdY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 339 LKKEKAII---VHPDRVVVANGPTFG-CVLMSDFFRELAKRVKR----NETAYENYERI--------------------- 389
Cdd:PRK07525 291 WPKDAKIIqvdINPDRIGLTKKVSVGiCGDAKAVARELLARLAErlagDAGREERKALIaaeksaweqelsswdhedddp 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 390 ---FVPEGKPLKCKPGEPLRVnamFQHIQK------MLSSETAVIAETGDSWfncqkLKLPKGCGYEFQMQYGSIGWSVG 460
Cdd:PRK07525 371 gtdWNEEARARKPDYMHPRQA---LREIQKalpedaIVSTDIGNNCSIANSY-----LRFEKGRKYLAPGSFGNCGYAFP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 461 ATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQK--AIIFliNNGGYTIE----VEIHDGPY---NVIKNWNYTG 531
Cdd:PRK07525 443 AIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPvtAVVF--RNYQWGAEkknqVDFYNNRFvgtELDNNVSYAG 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 15240950 532 LVDAIhNGEGkcwtTKVRYEEELVEAIKTATTEKKDSL-CFIEVIV 576
Cdd:PRK07525 521 IAEAM-GAEG----VVVDTQEELGPALKRAIDAQNEGKtTVIEIMC 561
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
409-576 |
6.60e-20 |
|
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: 87.31 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 409 AMFQHIQKMLSSETAVIAETGDS--WFNcQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVT 486
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSayWAY-RYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 487 AQDISTMIRNGQKAIIFLINNGGYTIEVEIHDGPYNV------IKNWNYTGLVDAIHngegkCWTTKVRYEEELVEAIKT 560
Cdd:cd00568 80 GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrvsgtdLSNPDFAALAEAYG-----AKGVRVEDPEDLEAALAE 154
|
170
....*....|....*.
gi 15240950 561 ATTEKKdsLCFIEVIV 576
Cdd:cd00568 155 ALAAGG--PALIEVKT 168
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
42-510 |
2.17e-19 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 91.57 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPeLNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLN 120
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSG-IRHVTPRHEQGAGFMADGYARVSGkPGVCFIITGPGMTNIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 121 AIAGAYSENLPVICIVGGPNSNDFGTNR-ILHHtigLPDfsqELRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKE-SK 198
Cdd:PRK07524 82 AMGQAYADSIPMLVISSVNRRASLGKGRgKLHE---LPD---QRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSArPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 199 PVYISISCNLAATP--HPTFARDPVPFDLTPRmsntmglEAAVEATLEFLNKAVKPVMV-GGPKLRvakASEAFLELADA 275
Cdd:PRK07524 156 PVHIEIPLDVLAAPadHLLPAPPTRPARPGPA-------PAALAQAAERLAAARRPLILaGGGALA---AAAALRALAER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 276 SGYPLAVMPSTKGLVPENHPHFIGtywGAVSTPFCSEIVESADAYIFAGPIF--NDYSSVGYSLLLKKEKAIIVHPDRVV 353
Cdd:PRK07524 226 LDAPVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELgeTDYDVYFDGGFPLPGELIRIDIDPDQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 354 VANGPTFGCVLMSDffrelakrvkrnetAYENYERIFV-PEGKPLKCKPGEPlRVNAMFQHIQKMLSSETA-------VI 425
Cdd:PRK07524 303 LARNYPPALALVGD--------------ARAALEALLArLPGQAAAADWGAA-RVAALRQALRAEWDPLTAaqvalldTI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 426 AET-------GDS------------------WFNCqklklPKGcgyefqmqYGSIGWSVGATLGYAQATPEKRVLSFIGD 480
Cdd:PRK07524 368 LAAlpdaifvGDStqpvyagnlyfdadaprrWFNA-----STG--------YGTLGYGLPAAIGAALGAPERPVVCLVGD 434
|
490 500 510
....*....|....*....|....*....|.
gi 15240950 481 GSFQVTAQDISTMiRNGQKAIIFLI-NNGGY 510
Cdd:PRK07524 435 GGLQFTLPELASA-VEADLPLIVLLwNNDGY 464
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
51-507 |
6.28e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 90.27 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSEN 129
Cdd:PRK07282 20 LRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVTSGPGATNAITGIADAMSDS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 130 LPVICIVGgpnsndfgtnRILHHTIGLPDFsQE---LRCFQTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYISI 204
Cdd:PRK07282 100 VPLLVFTG----------QVARAGIGKDAF-QEadiVGITMPITKYNYQIRETADIPRIITEAvhIATTGRPG-PVVIDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 205 SCNLAATpHPTFARDPvPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLAVMP 284
Cdd:PRK07282 168 PKDVSAL-ETDFIYDP-EVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 285 STKGLVPENHPHFIGTywGAVSTPFCSEI-VESADAYIFAGPIFNDySSVGYSLLLKKeKAIIVHPD-------RVVVAN 356
Cdd:PRK07282 246 LGQGTIATSHPLFLGM--GGMHGSYAANIaMTEADFMINIGSRFDD-RLTGNPKTFAK-NAKVAHIDidpaeigKIIKTD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 357 GPtfgcvLMSDFFRELAK-----RVKRN-----ETAYENYERIfvpegkPLKCKPGEPLRVNAMFQHIQKMLSSETAVIA 426
Cdd:PRK07282 322 IP-----VVGDAKKALQMllaepTVHNNtekwiEKVTKDKNRV------RSYDKKERVVQPQAVIERIGELTNGDAIVVT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 427 ETGDS--WF-------NCQKLKLPKGcgyefqmqYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDIStmIRNG 497
Cdd:PRK07282 391 DVGQHqmWAaqyypyqNERQLVTSGG--------LGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELA--ILNI 460
|
490
....*....|..
gi 15240950 498 QKAII--FLINN 507
Cdd:PRK07282 461 YKVPIkvVMLNN 472
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
44-507 |
1.54e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 89.43 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 44 GRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEpELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAI 122
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 123 AGAYSENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQE---LRCFQTVT--CYQavvnnLEDAhEQIDKAIATALKES 197
Cdd:PRK06276 83 ATAYADSSPVIALTG----------QVPTKLIGNDAF-QEidaLGIFMPITkhNFQ-----IKKP-EEIPEIFRAAFEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 198 K-----PVYISI-----SCNLAATPHPTFARDPVPfDLTPrmsNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASE 267
Cdd:PRK06276 146 KtgrpgPVHIDLpkdvqEGELDLEKYPIPAKIDLP-GYKP---TTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 268 AFLELADASGYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKaiIV 347
Cdd:PRK06276 222 ELIELSELVKIPVCTTLMGKGAFPEDHPLALGMV-GMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAK--II 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 348 HPD-------RVVVANGPTFG--CVLMSDFFRELAKRVKRNETAYENYERIFVPEGKPLKCKPGEPLRVNAMFQHIQKML 418
Cdd:PRK06276 299 HIDidpaeigKNVRVDVPIVGdaKNVLRDLLAELMKKEIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 419 S-----SETAVIAETGDS--W----FNCQKLK--LPKGcgyefqmQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQV 485
Cdd:PRK06276 379 ReidpsKNTIITTDVGQNqmWmahfFKTSAPRsfISSG-------GLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLM 451
|
490 500
....*....|....*....|..
gi 15240950 486 TAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK06276 452 NSQELATIAEYDIPVVICIFDN 473
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
38-508 |
2.58e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 88.68 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 38 TSESTLGRHLSRRLVQA----GVTDVFSVPGDFNLTLLDHLIaEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFT 112
Cdd:PRK06048 1 MTGSTEKMTGARAIIKClekeGVEVIFGYPGGAIIPVYDELY-DSDLRHILVRHEQAAAHAADGYARATGkVGVCVATSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 113 VGGLSVLNAIAGAYSENLPVICIVGGPNSNDFGTNRILHHTI-GLPdfsqelrcfQTVTCYQAVVNNLEDAHEQIDKA-- 189
Cdd:PRK06048 80 PGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADItGIT---------MPITKHNYLVQDAKDLPRIIKEAfh 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 190 IATALKESkPVYISISCNLAAtphptfarDPVPFDLTPRMS------NTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVA 263
Cdd:PRK06048 151 IASTGRPG-PVLIDLPKDVTT--------AEIDFDYPDKVElrgykpTYKGNPQQIKRAAELIMKAERPIIYAGGGVISS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 264 KASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGtYWGAVSTPFCSEIVESADAYIFAGPIFNDysSVGYSLLLKKEK 343
Cdd:PRK06048 222 NASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDD--RVTGKLASFAPN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 344 AIIVHPD-------RVVVANGPTFGCVlmSDFFRELAKRVKRNETAyENYERIFVPEGK-PLKCKPGEPLrvnAMFQHIQ 415
Cdd:PRK06048 299 AKIIHIDidpaeisKNVKVDVPIVGDA--KQVLKSLIKYVQYCDRK-EWLDKINQWKKEyPLKYKEREDV---IKPQYVI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 416 KMLSS---ETAVIAETGDS--WfNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDI 490
Cdd:PRK06048 373 EQIYElcpDAIIVTEVGQHqmW-AAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQEL 451
|
490
....*....|....*...
gi 15240950 491 STMIRNGQKAIIFLINNG 508
Cdd:PRK06048 452 ATAVQNDIPVIVAILNNG 469
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
51-576 |
7.86e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 87.08 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSEN 129
Cdd:PRK08527 13 LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATAYMDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 130 LPVICIVGG-PNSndfgtnrilhhTIGLPDFsQELRCF---QTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYIS 203
Cdd:PRK08527 93 IPLVLISGQvPNS-----------LIGTDAF-QEIDAVgisRPCVKHNYLVKSIEELPRILKEAfyIARSGRPG-PVHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 204 ISCNLAATpHPTFARdPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLAVM 283
Cdd:PRK08527 160 IPKDVTAT-LGEFEY-PKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 284 PSTKGLVPENHPHFIGTYwgAVSTPFCSEIVES-ADAYIFAGPIFNDYSSVGYSLLLKKEKaiIVHPD-------RVVVA 355
Cdd:PRK08527 238 LMARGVLRSDDPLLLGML--GMHGSYAANMAMSeCDLLISLGARFDDRVTGKLSEFAKHAK--IIHVDidpssisKIVNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 356 NGPTFGCVlmSDFFRELAKRVKR-NETAYENYERIF--VPEGKPLKCKPG-EPLRVNAMFQHIQKMLSSETAVIAETGDS 431
Cdd:PRK08527 314 DYPIVGDL--KNVLKEMLEELKEeNPTTYKEWREILkrYNELHPLSYEDSdEVLKPQWVIERVGELLGDDAIISTDVGQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 432 --W------FNCQKLKLPKGcgyefqmQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIF 503
Cdd:PRK08527 392 qmWvaqfypFNYPRQLATSG-------GLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 504 LINNGgytieveihdgpY-NVIKNW------------------NYTGLVDAIHnGEGKCWTTKvryeEELVEAIKTATte 564
Cdd:PRK08527 465 ILNNN------------FlGMVRQWqtffyeerysetdlstqpDFVKLAESFG-GIGFRVTTK----EEFDKALKEAL-- 525
|
570
....*....|..
gi 15240950 565 KKDSLCFIEVIV 576
Cdd:PRK08527 526 ESDKVALIDVKI 537
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
55-507 |
1.11e-17 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 86.51 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 55 GVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 133
Cdd:PRK06882 18 GVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGIATAYTDSVPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 134 CIVGGPNSNDFGTNRILH-HTIGLPdfsqelrcfQTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYISISCNLAA 210
Cdd:PRK06882 98 ILSGQVPSNLIGTDAFQEcDMLGIS---------RPVVKHSFIVKNAEDIPSTIKKAfyIASTGRPG-PVVIDIPKDMVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 211 TPHPTFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYPLAVMPSTKGLV 290
Cdd:PRK06882 168 PANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMGLGAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 291 PENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIIVHPD-----RVVVANGPTFGCV-- 363
Cdd:PRK06882 248 PSTDKQFLGML-GMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDptsisKNVPAYIPIVGSAkn 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 364 LMSDFFRELA-KRVKRNETAYENYERIfVPEGKPLKC----KPGEPLRVNAMFQHIQKMLSSETAVIAETGD-SWFNCQK 437
Cdd:PRK06882 327 VLEEFLSLLEeENLAKSQTDLTAWWQQ-INEWKAKKClefdRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQhQMFAALH 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 438 LKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK06882 406 YPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
42-212 |
1.59e-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: 80.29 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLN 120
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 121 AIAGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQE---LRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKES 197
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGT-----------DYFQEvdlLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR 149
|
170
....*....|....*
gi 15240950 198 KPVYISISCNLAATP 212
Cdd:cd07039 150 GVAVLILPGDVQDAP 164
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
13-579 |
2.01e-17 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 85.80 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 13 PTTGDIGSPPSNAVATIQDSAPITTTSESTLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAG 92
Cdd:PRK07789 3 PPTPAAAASAAPPPAAPAARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 93 YAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQELR-CFQT-- 168
Cdd:PRK07789 83 HAAEGYAQATGrVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGT-----------DAFQEADiVGITmp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 169 VTCYQAVVNNLEDaheqIDKAIATALKeskpvyisiscnLAATPHPtfarDPVPFDLT-------------PRMS----- 230
Cdd:PRK07789 152 ITKHNFLVTDADD----IPRVIAEAFH------------IASTGRP----GPVLVDIPkdalqaqttfswpPRMDlpgyr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 231 -NTMGLEAAVEATLEFLNKAVKPVM-VGGPKLRvAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGT--YWGAVS 306
Cdd:PRK07789 212 pVTKPHGKQIREAAKLIAAARRPVLyVGGGVIR-AEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 307 TpfcSEIVESADAYIFAGPIFNDysSVGYSLLLKKEKAIIVHPD-------RVVVANGPTFGCV------LMSDFFRELA 373
Cdd:PRK07789 291 A---VAALQRSDLLIALGARFDD--RVTGKLDSFAPDAKVIHADidpaeigKNRHADVPIVGDVkeviaeLIAALRAEHA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 374 KRVKRNETAYENYERIFVpEGKPLKCKPGE-----PLRV----------NAMF-----QHiqKMLSSEtAVIAETGDSWF 433
Cdd:PRK07789 366 AGGKPDLTAWWAYLDGWR-ETYPLGYDEPSdgslaPQYVierlgeiagpDAIYvagvgQH--QMWAAQ-FIDYEKPRTWL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 434 NCQKLklpkgcgyefqmqyGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTI- 512
Cdd:PRK07789 442 NSGGL--------------GTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMv 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 513 -------------EVEIHDGPYNVIknwNYTGLVDAIhngegKCWTTKVRYEEELVEAIKTAtTEKKDSLCFIEVIVHKD 579
Cdd:PRK07789 508 rqwqtlfyeerysNTDLHTHSHRIP---DFVKLAEAY-----GCVGLRCEREEDVDAVIEKA-RAINDRPVVIDFVVGKD 578
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
51-507 |
2.11e-16 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 82.24 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHLIAEPeLNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYSEN 129
Cdd:PRK08978 11 LRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGkVGVCIATSGPGATNLITGLADALLDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 130 LPVICIVGGPNSNDFGTnrilhhtiglpDFSQE-------LRCfqtvTCYQAVVNNLEDAHEQIDKAIATAlKESK--PV 200
Cdd:PRK08978 90 VPVVAITGQVSSPLIGT-----------DAFQEidvlglsLAC----TKHSFLVQSLEELPEIMAEAFEIA-SSGRpgPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 201 YISI--SCNLAAT---PHPTFARDPVPFDltprmsntmglEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADA 275
Cdd:PRK08978 154 LVDIpkDIQLAEGelePHLTTVENEPAFP-----------AAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 276 SGyplavMPST---KGL--VPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDysSVGYSLLLKKEKAIIVHPD 350
Cdd:PRK08978 223 TG-----MPAVatlKGLgaVEADHPYYLGML-GMHGTKAANLAVQECDLLIAVGARFDD--RVTGKLNTFAPHAKVIHLD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 ----------RVVVANG-------PTFGCVLMSDFFRELAKRVKR-NETAYENyerifvpegkplkckPGEPLRVNAMFQ 412
Cdd:PRK08978 295 idpaeinklrQAHVALQgdlnallPALQQPLNIDAWRQHCAQLRAeHAWRYDH---------------PGEAIYAPALLK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 413 HIQKMLSSETAVIAETGdswfncqklklpkgcgyEFQM---QY---------------GSIGWSVGATLGYAQATPEKRV 474
Cdd:PRK08978 360 QLSDRKPADTVVTTDVG-----------------QHQMwvaQHmrftrpenfitssglGTMGFGLPAAIGAQVARPDDTV 422
|
490 500 510
....*....|....*....|....*....|...
gi 15240950 475 LSFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK08978 423 ICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDN 455
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
32-508 |
5.58e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 81.17 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 32 SAPITTTSESTLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIaEPELNNIGCCNELNAGYAADGYARSRG-VGACVVT 110
Cdd:PRK06725 6 TYEKLQCEEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALY-ESGLKHILTRHEQAAIHAAEGYARASGkVGVVFAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 111 FTVGGLSVLNAIAGAYSENLPVICIVGgpnsndfgtnRILHHTIGLPDFSQE--LRCFQTVTCYQAVVNNLEDAHEQIDK 188
Cdd:PRK06725 85 SGPGATNLVTGLADAYMDSIPLVVITG----------QVATPLIGKDGFQEAdvVGITVPVTKHNYQVRDVNQLSRIVQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 189 AIATALK-ESKPVYISISCNLAATPHPTFARDPVP---FDLTPrMSNTMGLEAAVEAtlefLNKAVKPVMVGGPKLRVAK 264
Cdd:PRK06725 155 AFYIAESgRPGPVLIDIPKDVQNEKVTSFYNEVVEipgYKPEP-RPDSMKLREVAKA----ISKAKRPLLYIGGGVIHSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 265 ASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKA 344
Cdd:PRK06725 230 GSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGML-GMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 345 IIVHPD-----RVVVANGPTFGCV-------LMSDFFRELAKRVKRNETAYENYERIFvpEGKPLKCKPgeplrvnamfQ 412
Cdd:PRK06725 309 VHIDIDpsefhKNVAVEYPVVGDVkkalhmlLHMSIHTQTDEWLQKVKTWKEEYPLSY--KQKESELKP----------Q 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 413 HIQKMLSS----ETAVIAETGDS--WF-NCQKLKLPKGcgYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQV 485
Cdd:PRK06725 377 HVINLVSEltngEAIVTTEVGQHqmWAaHFYKAKNPRT--FLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQM 454
|
490 500
....*....|....*....|...
gi 15240950 486 TAQDISTMIRNGQKAIIFLINNG 508
Cdd:PRK06725 455 NIQELQTIAENNIPVKVFIINNK 477
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
49-507 |
1.66e-15 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 79.87 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 49 RRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYS 127
Cdd:PRK08979 12 RSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 128 ENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQE---LRCFQTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPVYI 202
Cdd:PRK08979 92 DSIPMVVLSGQVPSNLIGN-----------DAFQEcdmIGISRPVVKHSFLVKDAEDIPEIIKKAfyIASTGRPG-PVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 203 SI--SCNLAATPHPTfardPVPFDLTPRMSN--TMGLEAAVEATLEFLNKAVKPVM-VGGPKLrVAKASEAFLELADASG 277
Cdd:PRK08979 160 DLpkDCLNPAILHPY----EYPESIKMRSYNptTSGHKGQIKRGLQALLAAKKPVLyVGGGAI-ISGADKQILQLAEKLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 278 YPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGysllLKK--EKAIIVHPD----- 350
Cdd:PRK08979 235 LPVVSTLMGLGAFPGTHKNSLGML-GMHGRYEANMAMHNADLIFGIGVRFDDRTTNN----LEKycPNATILHIDidpss 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 --RVVVANGPTFGC---VL------------------MSDFFRELAKRVKRNETAYE-NYERIfvpegkplkcKPGEplr 406
Cdd:PRK08979 310 isKTVRVDIPIVGSadkVLdsmlalldesgetndeaaIASWWNEIEVWRSRNCLAYDkSSERI----------KPQQ--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 407 vnaMFQHIQKMLSSETAVIAETGD---------------SWFNCQKLklpkgcgyefqmqyGSIGWSVGATLGYAQATPE 471
Cdd:PRK08979 377 ---VIETLYKLTNGDAYVASDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAAMGVKFAMPD 439
|
490 500 510
....*....|....*....|....*....|....*.
gi 15240950 472 KRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK08979 440 ETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNN 475
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
452-574 |
5.75e-15 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 72.23 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 452 YGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTI----EVEIHDGPY-----N 522
Cdd:pfam02775 27 LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGYGMtrgqQTPFGGGRYsgpsgK 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15240950 523 VIKNWNYTGLVDAiHNGEGKCWTTKvryeEELVEAIKTAttEKKDSLCFIEV 574
Cdd:pfam02775 107 ILPPVDFAKLAEA-YGAKGARVESP----EELEEALKEA--LEHDGPALIDV 151
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
44-576 |
9.60e-15 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 77.09 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 44 GRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAI 122
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 123 AGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQE---LRCFQTVTCYQAVVNNLEDAHEQIDKA--IATALKES 197
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGE-----------DAFQEtdmVGISRPIVKHSFMVKHASEIPEIIKKAfyIAQSGRPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 198 kPVYISISCNlAATPHPTFARD-PVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADAS 276
Cdd:PRK06466 156 -PVVVDIPKD-MTNPAEKFEYEyPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 277 GYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKaiIVHPD------ 350
Cdd:PRK06466 234 NLPVTNTLMGLGGFPGTDRQFLGML-GMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAK--IIHIDidpasi 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 -RVVVANGPTFGCVL-----MSDFFRELAKRVKRNETA--------YENYERIFvpegkPLKCKPGEPLRVNAMFQHIQK 416
Cdd:PRK06466 311 sKTIKADIPIVGPVEsvlteMLAILKEIGEKPDKEALAawwkqideWRGRHGLF-----PYDKGDGGIIKPQQVVETLYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 417 MLSSETAVIAETGD-SWFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIR 495
Cdd:PRK06466 386 VTNGDAYVTSDVGQhQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 496 NGQKAIIFLINNGGYTIEVEIHDGPYNVIKNWNY-------TGLVDAI-HNGegkcwtTKVRYEEELVEAIKTAtTEKKD 567
Cdd:PRK06466 466 YGLPVKIINLNNGALGMVRQWQDMQYEGRHSHSYmeslpdfVKLAEAYgHVG------IRITDLKDLKPKLEEA-FAMKD 538
|
....*....
gi 15240950 568 SLCFIEVIV 576
Cdd:PRK06466 539 RLVFIDIYV 547
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
453-576 |
2.23e-14 |
|
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: 71.47 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 453 GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTI---EVEIHDGPYNVIKNWNY 529
Cdd:cd02002 49 GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGAlrsFLKRVGPEGPGENAPDG 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15240950 530 TGLVD------AIHNGEGkCWTTKVRYEEELVEAIKTATTEKKDSLcfIEVIV 576
Cdd:cd02002 129 LDLLDpgidfaAIAKAFG-VEAERVETPEELDEALREALAEGGPAL--IEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
404-576 |
2.40e-14 |
|
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: 71.41 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 404 PLRVnamFQHIQKMLSSETAVIAETGD------SWFNCQKLKLPKGCGYefqmqYGSIGWSVGATLGYAQATPEKRVLSF 477
Cdd:cd02004 1 PYRV---LHELQEALPDDAIIVSDGGNtmdwarYILRPRKPRHRLDAGT-----FGTLGVGLGYAIAAALARPDKRVVLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 478 IGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTIEVEIHDGPYNVIKN---WNYTGLVDAIHNGEGkCWTTKVRYEEEL 554
Cdd:cd02004 73 EGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPvttLLPDTRYDLVAEAFG-GKGELVTTPEEL 151
|
170 180
....*....|....*....|..
gi 15240950 555 VEAIKTAttEKKDSLCFIEVIV 576
Cdd:cd02004 152 KPALKRA--LASGKPALINVII 171
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
38-507 |
5.92e-14 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 74.74 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 38 TSESTLGRHLS------RRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVT 110
Cdd:PRK09107 2 AQKSHMPRQMTgaemvvQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 111 FTVGGLSVLNAIAGAYSENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQElrCfQTV------TCYQAVVNNLEDAHE 184
Cdd:PRK09107 82 SGPGATNAVTPLQDALMDSIPLVCITG----------QVPTHLIGSDAF-QE--C-DTVgitrpcTKHNWLVKDVNDLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 185 QIDKA--IATALKESkPVYISISCNL---AATPHPTfARDPVPFDLTPRMSNTMgleAAVEATLEFLNKAVKPVMV--GG 257
Cdd:PRK09107 148 VIHEAfhVATSGRPG-PVVVDIPKDVqfaTGTYTPP-QKAPVHVSYQPKVKGDA---EAITEAVELLANAKRPVIYsgGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 258 PKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFI------GTYWG-----------AVSTPFCSEIVESADAY 320
Cdd:PRK09107 223 VINSGPEASRLLRELVELTGFPITSTLMGLGAYPASGKNWLgmlgmhGTYEAnmamhdcdvmlCVGARFDDRITGRLDAF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 321 ifaGP------IFNDYSSVGYSllLKKEKAII-----VHPD--RVVVANGPTFGCVLMSDFFRELAKRVKRNETAYENYE 387
Cdd:PRK09107 303 ---SPnskkihIDIDPSSINKN--VRVDVPIIgdvghVLEDmlRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 388 RIFVPegkplkckpgeplrvnamfQH-IQKMLS----SETAVIAETGdswfncqklklpkgcgyEFQM---QY------- 452
Cdd:PRK09107 378 DVIMP-------------------QYaIQRLYEltkgRDTYITTEVG-----------------QHQMwaaQFfgfeepn 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240950 453 --------GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK09107 422 rwmtsgglGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
49-507 |
9.35e-14 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 74.10 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 49 RRLVQAGVTDVFSVPGDFNLTLLDhLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYS 127
Cdd:PRK06457 10 RVLEDNGIQRIYGIPGDSIDPLVD-AIRKSKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLNGLYDAKM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 128 ENLPVICIVGGPNSNdfgtnrILHHtiglpDFSQEL---RCFQTVTCYQAVVNNLEDAHEQIDKAIATALKESKPVYISI 204
Cdd:PRK06457 89 DHAPVIALTGQVESD------MIGH-----DYFQEVnltKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 205 SCNL---AATPHPTFARDPVPFDLTPRMSntmgleaaveATLEFLNKAVKPVMVGGPKLRvaKASEAFLELADASGYPLA 281
Cdd:PRK06457 158 PVDIlrkSSEYKGSKNTEVGKVKYSIDFS----------RAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPII 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 282 VMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFnDYSsvgySLLLKKEKAIIVHPD-----RVVVAN 356
Cdd:PRK06457 226 YTLNGKGILPDLDPKVMGGI-GLLGTKPSIEAMDKADLLIMLGTSF-PYV----NFLNKSAKVIQVDIDnsnigKRLDVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 357 GPTFGCVlmSDFFrelakRVKRNETAYENYERI------FVPEGKPLKCKPGEPLRVNAMFQHIQKMLSSETAVIAETGD 430
Cdd:PRK06457 300 LSYPIPV--AEFL-----NIDIEEKSDKFYEELkgkkedWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 431 S--WFNcQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKR-VLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PRK06457 373 VtmWTA-RHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNN 451
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
42-324 |
1.24e-13 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 73.49 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTFTvgGLSVLNA 121
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTST--GTGAGNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 122 iAGAYSENL----PVICIVGGPNSNDFGTNR-ILHHTiglPDfsqELRCFQTVTCYQAVVNNLEDAHEQIDKAIATALKE 196
Cdd:PRK07064 82 -AGALVEALtagtPLLHITGQIETPYLDQDLgYIHEA---PD---QLTMLRAVSKAAFRVRSAETALATIREAVRVALTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 197 -SKPVYISISCNL--AATPHPTFARdPVPFDLtPRMSntmglEAAVEATLEFLNKAVKPVM-VGGPKLRVAKASEAFLEL 272
Cdd:PRK07064 155 pTGPVSVEIPIDIqaAEIELPDDLA-PVHVAV-PEPD-----AAAVAELAERLAAARRPLLwLGGGARHAGAEVKRLVDL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15240950 273 adasGYPLAVMPSTKGLVPENHPHFIGTYWGavsTPFCSEIVESADAYIFAG 324
Cdd:PRK07064 228 ----GFGVVTSTQGRGVVPEDHPASLGAFNN---SAAVEALYKTCDLLLVVG 272
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
42-510 |
4.01e-13 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 71.95 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 42 TLGRHLSRRLVQAGVTDVFSVPGDfnltllDH--LIAE-----------PELnnIGCCNELNAGYAADGYARSRG-VGAC 107
Cdd:PRK08327 8 TAAELFLELLKELGVDYIFINSGT------DYppIIEAkararaagrplPEF--VICPHEIVAISMAHGYALVTGkPQAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 108 VVTFTVGGLSVLNAIAGAYSENLPVICIVG-GPNSND--FGT-NRILHhtiglpdFSQELRCfQTVTCYQAV-----VNN 178
Cdd:PRK08327 80 MVHVDVGTANALGGVHNAARSRIPVLVFAGrSPYTEEgeLGSrNTRIH-------WTQEMRD-QGGLVREYVkwdyeIRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 179 LEDAHEQIDKAIATALKESK-PVYISISCNLAATPHPTFARDPVPFdltPRMSNTMGLEAAVEATLEFLNKAVKPVMVGG 257
Cdd:PRK08327 152 GDQIGEVVARAIQIAMSEPKgPVYLTLPREVLAEEVPEVKADAGRQ---MAPAPPAPDPEDIARAAEMLAAAERPVIITW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 258 PKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGtywgavstPFCSEIVESADAYIFAGpifndySSVGY-- 335
Cdd:PRK08327 229 RAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLG--------PDPRADLAEADLVLVVD------SDVPWip 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 336 SLLLKKEKAIIVHpdrvvVANGPTFGCVLM-------------SDFFRELA----------KRVKRNETAYENYERIFVP 392
Cdd:PRK08327 295 KKIRPDADARVIQ-----IDVDPLKSRIPLwgfpcdlciqadtSTALDQLEerlkslasaeRRRARRRRAAVRELRIRQE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 393 EGK---PLKCKPGEPLRVNAMFQHIQKMLSSETAVIAETGdswFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQAT 469
Cdd:PRK08327 370 AAKraeIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYP---FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLAT 446
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15240950 470 PEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLI--NNGGY 510
Cdd:PRK08327 447 PDRLVIATVGDGSFIFGVPEAAHWVAERYGLPVLVVvfNNGGW 489
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
27-508 |
1.46e-12 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 70.22 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 27 ATIQDSAPITTTSESTLGRHLSRRLVQA-GVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-V 104
Cdd:PRK06965 6 AEFSTAESLSPPAADSIGAEILMKALAAeGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 105 GACVVTFTVGGLSVLNAIAGAYSENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQElrCfQTVTCYQAVVN------N 178
Cdd:PRK06965 86 GVALVTSGPGVTNAVTGIATAYMDSIPMVVISG----------QVPTAAIGQDAF-QE--C-DTVGITRPIVKhnflvkD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 179 LEDAHEQIDKAIATALK-ESKPVYISISCNLAATPHPTfardPVPFDLTPRMSN--TMGLEAAVEATLEFLNKAVKPVMV 255
Cdd:PRK06965 152 VRDLAETVKKAFYIARTgRPGPVVVDIPKDVSKTPCEY----EYPKSVEMRSYNpvTKGHSGQIRKAVSLLLSAKRPYIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 256 GGPKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGY 335
Cdd:PRK06965 228 TGGGVILANASRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGML-GMHGTYEANMAMQHCDVLIAIGARFDDRVIGNP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 336 SLLLKKEKAIIvHPD--------RVVVaNGPTFGCVlmSDFFRELAKRVKRNETAYEN------YERIfvpEG-KPLKC- 399
Cdd:PRK06965 307 AHFASRPRKII-HIDidpssiskRVKV-DIPIVGDV--KEVLKELIEQLQTAEHGPDAdalaqwWKQI---EGwRSRDCl 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 400 ---KPGEPLRVNAMFQHIQKMLSSETAVIAETGD---------------SWFNCQKLklpkgcgyefqmqyGSIGWSVGA 461
Cdd:PRK06965 380 kydRESEIIKPQYVVEKLWELTDGDAFVCSDVGQhqmwaaqfyrfneprRWINSGGL--------------GTMGVGLPY 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15240950 462 TLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNG 508
Cdd:PRK06965 446 AMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNR 492
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
49-507 |
1.61e-10 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 63.72 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 49 RRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAYS 127
Cdd:PRK07979 12 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 128 ENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQELRCF---QTVTCYQAVVNNLEDAHEQIDKAIATALK-ESKPVYIS 203
Cdd:PRK07979 92 DSIPLVVLSG----------QVATSLIGYDAF-QECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFWLAASgRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 204 ISCNLAatpHPTFARDPV-PFDLTPRMSN--TMGLEAAVEATLEFLNKAVKPVM-VGGPKLRvAKASEAFLELADASGYP 279
Cdd:PRK07979 161 LPKDIL---NPANKLPYVwPESVSMRSYNptTQGHKGQIKRALQTLVAAKKPVVyVGGGAIN-AACHQQLKELVEKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 280 LAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDYSSvgYSLLLKKEKAIIVHPD-------RV 352
Cdd:PRK07979 237 VVSSLMGLGAFPATHRQSLGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTT--NNLAKYCPNATVLHIDidptsisKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 353 VVANGPTFGCV--LMSDFFRELAKrvkrnETAYENYERI-----FVPEGKPLKC----KPGEPLRVNAMFQHIQKMLSSE 421
Cdd:PRK07979 314 VTADIPIVGDArqVLEQMLELLSQ-----ESAHQPLDEIrdwwqQIEQWRARQClkydTHSEKIKPQAVIETLWRLTKGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 422 TAVIAETGD---------------SWFNCQKLklpkgcgyefqmqyGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVT 486
Cdd:PRK07979 389 AYVTSDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMN 454
|
490 500
....*....|....*....|.
gi 15240950 487 AQDISTMIRNGQKAIIFLINN 507
Cdd:PRK07979 455 IQELSTALQYELPVLVLNLNN 475
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
51-507 |
2.34e-10 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 63.22 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQA----GVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGA 125
Cdd:PLN02470 19 LVEAlereGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGkVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 126 YSENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQE---LRCFQTVTCYQAVVNNLEDAHEQIDKA--IATALKESkPV 200
Cdd:PLN02470 99 LLDSVPLVAITG----------QVPRRMIGTDAF-QEtpiVEVTRSITKHNYLVMDVEDIPRVIREAffLASSGRPG-PV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 201 YISISCNLA---ATPHPTfardpVPFDLTPRMSNTMGL--EAAVEATLEFLNKAVKPVM-VGGPKLrvaKASEAFLELAD 274
Cdd:PLN02470 167 LVDIPKDIQqqlAVPNWN-----QPMKLPGYLSRLPKPpeKSQLEQIVRLISESKRPVVyVGGGCL---NSSEELREFVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 275 ASGYPLAVMPSTKGLVP---ENHPHFIGTYwGAVSTPFCseiVESADAYIFAGPIFNDysSVGYSLLLKKEKAIIVHPD- 350
Cdd:PLN02470 239 LTGIPVASTLMGLGAFPasdELSLQMLGMH-GTVYANYA---VDSADLLLAFGVRFDD--RVTGKLEAFASRASIVHIDi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 ---------------------------RVVVANGPTFGCVlmSDFFRELAKRVKRNETAYENYERIFVPegkplkckpge 403
Cdd:PLN02470 313 dpaeigknkqphvsvcadvklalqglnKLLEERKAKRPDF--SAWRAELDEQKEKFPLSYPTFGDAIPP----------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 404 plrvnamfQHIQKMLSSETA--VIAETGdswFNCQKLKLPKGCGYEFQMQY------GSIGWSVGATLGYAQATPEKRVL 475
Cdd:PLN02470 380 --------QYAIQVLDELTDgnAIISTG---VGQHQMWAAQWYKYKEPRRWltsgglGAMGFGLPAAIGAAAANPDAIVV 448
|
490 500 510
....*....|....*....|....*....|..
gi 15240950 476 SFIGDGSFQVTAQDISTMIRNGQKAIIFLINN 507
Cdd:PLN02470 449 DIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
51-508 |
3.90e-10 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 62.79 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHLIAEPE---LNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAY 126
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDELYAWEKkglIKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 127 SENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQELRCFQ---TVTCYQAVVNNLEDAHEQIDKAIATALK-ESKPVYI 202
Cdd:CHL00099 100 MDSVPLLVITGQVGRAFIGT-----------DAFQEVDIFGitlPIVKHSYVVRDARDISRIVAEAFYIAKHgRPGPVLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 203 SISCNLAATPHPTFarDPVPFDltpRMSNTMGLEAAVEATLEFLNKAVKPVM--------VGGPKLrVAKASEAFLELAD 274
Cdd:CHL00099 169 DIPKDVGLEKFDYY--PPEPGN---TIIKILGCRPIYKPTIKRIEQAAKLILqssqpllyVGGGAI-ISDAHQEITELAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 275 ASGYPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDysSVGYSLLLKKEKAIIVHP--DRV 352
Cdd:CHL00099 243 LYKIPVTTTLMGKGIFDEDHPLCLGML-GMHGTAYANFAVSECDLLIALGARFDD--RVTGKLDEFACNAQVIHIdiDPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 353 VVANGPTFGCVLMSD---FFRELAKRVKRNETAYEN------YERIfvpegkpLKCKPGEPLRVnamfQHIQKMLSSETa 423
Cdd:CHL00099 320 EIGKNRIPQVAIVGDvkkVLQELLELLKNSPNLLESeqtqawRERI-------NRWRKEYPLLI----PKPSTSLSPQE- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 424 VIAETG----DSWFN---------------CQKLKLPKGCGyefqmqYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQ 484
Cdd:CHL00099 388 VINEISqlapDAYFTtdvgqhqmwaaqflkCKPRKWLSSAG------LGTMGYGLPAAIGAQIAHPNELVICISGDASFQ 461
|
490 500
....*....|....*....|....
gi 15240950 485 VTAQDISTMIRNGQKAIIFLINNG 508
Cdd:CHL00099 462 MNLQELGTIAQYNLPIKIIIINNK 485
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
453-579 |
1.33e-09 |
|
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: 57.89 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 453 GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGgytieveiHDGpynVIKNW----- 527
Cdd:cd02015 50 GTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNG--------SLG---MVRQWqelfy 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240950 528 --NYTGLVDAIH----------NGEGKcwttKVRYEEELVEAIKTATTEKKdsLCFIEVIVHKD 579
Cdd:cd02015 119 egRYSHTTLDSNpdfvklaeayGIKGL----RVEKPEELEAALKEALASDG--PVLLDVLVDPE 176
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
445-510 |
1.40e-09 |
|
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: 58.09 E-value: 1.40e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240950 445 GYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGY 510
Cdd:cd02003 40 GYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
27-507 |
1.83e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 60.54 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 27 ATIQDSAPITTTSESTLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIaEPELNNIGCCNELNAGYAADGYARSRG-VG 105
Cdd:PRK07710 2 NVMRTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALY-DCGIPHILTRHEQGAIHAAEGYARISGkPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 106 ACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQE---LRCFQTVTCYQAVVNNLEDA 182
Cdd:PRK07710 81 VVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGS-----------DAFQEadiMGITMPVTKHNYQVRKASDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 183 HEQIDKA--IATALKESkPVYISISCNLAATpHPTFARDpVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKL 260
Cdd:PRK07710 150 PRIIKEAfhIATTGRPG-PVLIDIPKDMVVE-EGEFCYD-VQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 261 RVAKASEAFLELADASGYPLAVMPSTKGLVPENHPHFI------GTYWGAVSTPFCseivesaDAYIFAGPIFNDysSVG 334
Cdd:PRK07710 227 LHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLFLgmagmhGTYTANMALYEC-------DLLINIGARFDD--RVT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 335 YSLLLKKEKAIIVHPD---RVVVANGPTfGCVLMSDFFRELAKRVKRNETAYENYERI-FVPEGK---PLKCKP-GEPLR 406
Cdd:PRK07710 298 GNLAYFAKEATVAHIDidpAEIGKNVPT-EIPIVADAKQALQVLLQQEGKKENHHEWLsLLKNWKekyPLSYKRnSESIK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 407 VNAMFQHIQKMLSSETAVIAETGD-SWFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQV 485
Cdd:PRK07710 377 PQKAIEMLYEITKGEAIVTTDVGQhQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQM 456
|
490 500
....*....|....*....|...
gi 15240950 486 TAQDIStMIRNGQKAI-IFLINN 507
Cdd:PRK07710 457 TLQELS-VIKELSLPVkVVILNN 478
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
51-508 |
7.64e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 58.52 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPGDFNLTLLDHL-IAEPE--LNNIGCCNELNAGYAADGYARSRG-VGACVVTFTVGGLSVLNAIAGAY 126
Cdd:PRK07418 29 LKRHGVKHIFGYPGGAILPIYDELyKAEAEgwLKHILVRHEQGAAHAADGYARATGkVGVCFGTSGPGATNLVTGIATAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 127 SENLPVICIVGgpnsndfgtnRILHHTIGLPDFsQELRCFQT---VTCYQAVVNNLEDAHEQIDKA--IATALKESkPVY 201
Cdd:PRK07418 109 MDSVPMVVITG----------QVPRPAIGTDAF-QETDIFGItlpIVKHSYVVRDPSDMARIVAEAfhIASSGRPG-PVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 202 ISISCNLAatpHPTFARDPV-PFDLTPR--MSNTMGLEAAVEATLEFLNKAVKPVM-VGGPKLrVAKASEAFLELADASG 277
Cdd:PRK07418 177 IDIPKDVG---QEEFDYVPVePGSVKPPgyRPTVKGNPRQINAALKLIEEAERPLLyVGGGAI-SAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 278 YPLAVMPSTKGLVPENHPHFIGTYwGAVSTPFCSEIVESADAYIFAGPIFNDysSVGYSLLLKKEKAIIVHPD------- 350
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGML-GMHGTAYANFAVTECDLLIAVGARFDD--RVTGKLDEFASRAKVIHIDidpaevg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 351 RVVVANGPTFGCVLMSdfFRELAKRVKRNETAYEN---YERI-FVPEGKPLKCKPGE----PLRVNAMFQHiqkmLSSET 422
Cdd:PRK07418 330 KNRRPDVPIVGDVRKV--LVKLLERSLEPTTPPRTqawLERInRWKQDYPLVVPPYEgeiyPQEVLLAVRD----LAPDA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 423 AVIAETGdswfncqklklpkgcgyEFQM---QY--------------GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQV 485
Cdd:PRK07418 404 YYTTDVG-----------------QHQMwaaQFlrngprrwissaglGTMGFGMPAAMGVKVALPDEEVICIAGDASFLM 466
|
490 500
....*....|....*....|...
gi 15240950 486 TAQDISTMIRNGQKAIIFLINNG 508
Cdd:PRK07418 467 NIQELGTLAQYGINVKTVIINNG 489
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
33-296 |
2.20e-07 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 53.84 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 33 APITTTSESTLGRHLsrrLVQA----GVTDVFSVPGdFNLTLLDHLIAEPELNNIGCCNELNAGYAA--DGYARSRGvGA 106
Cdd:PRK09259 1 TAMSDQLQLTDGFHL---VIDAlklnGIDTIYGVVG-IPITDLARLAQAEGIRYIGFRHEQSAGNAAaaAGFLTQKP-GV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 107 CVVTFTVGGLSVLNAIAGAYSENLPVICIVGgpnSNDfgtnrilHHTIGLP--DFsQEL------RCFqtvtCYQAV-VN 177
Cdd:PRK09259 76 CLTVSAPGFLNGLTALANATTNCFPMIMISG---SSE-------REIVDLQqgDY-EELdqlnaaKPF----CKAAFrVN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 178 NLEDAHEQIDKAIATALkESKP--VYISISCNLAATPHPTFARDP---VPFDLTPRMsntMGLEAAVEATLEFLNKAVKP 252
Cdd:PRK09259 141 RAEDIGIGVARAIRTAV-SGRPggVYLDLPAKVLAQTMDADEALTslvKVVDPAPAQ---LPAPEAVDRALDLLKKAKRP 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15240950 253 VMVGGPKLRVAKASEAFLELADASGYPLAVMPSTKGLVPENHPH 296
Cdd:PRK09259 217 LIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQ 260
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
404-508 |
8.28e-07 |
|
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: 49.45 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 404 PLRVNAMFQHIQKMLSSETAVIAETGDS--WFNcQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQATPEKRVLSFIGDG 481
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVtvWAA-RHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDG 79
|
90 100
....*....|....*....|....*..
gi 15240950 482 SFQVTAQDISTMIRNGQKAIIFLINNG 508
Cdd:cd02014 80 GFAMLMGDLITAVKYNLPVIVVVFNNS 106
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
404-561 |
3.90e-06 |
|
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: 48.05 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 404 PLRVNAMFQHIQKMLSSETAVIAETGDSWF-NCQKLKLPK-----GCGyefqmQYGSIGWSVGATLGYAQATPEKRVLSF 477
Cdd:cd02006 7 PIKPQRVYEEMNKAFGRDVRYVTTIGLSQIaGAQMLHVYKprhwiNCG-----QAGPLGWTVPAALGVAAADPDRQVVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 478 IGDGSFQVTAQDISTMIRNGQKAIIFLINNG----------GYTIEVEIHDGpynvIKNWNYTGL----VDAIHNGEG-K 542
Cdd:cd02006 82 SGDYDFQFMIEELAVGAQHRIPYIHVLVNNAylglirqaqrAFDMDYQVNLA----FENINSSELggygVDHVKVAEGlG 157
|
170
....*....|....*....
gi 15240950 543 CWTTKVRYEEELVEAIKTA 561
Cdd:cd02006 158 CKAIRVTKPEELAAAFEQA 176
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
454-510 |
7.62e-06 |
|
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: 46.51 E-value: 7.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15240950 454 SIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGY 510
Cdd:cd02010 49 TMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGY 105
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
453-512 |
9.38e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 48.30 E-value: 9.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 453 GSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTMIRNGQKAIIFLINNGGYTI 512
Cdd:PRK07586 385 GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAI 444
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
41-300 |
1.75e-05 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 47.60 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 41 STLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLI-AEPELNNIGCCNELNAGYAADGYAR-SRGVGACVVTFTVGGLSV 118
Cdd:PRK08273 3 QTVADFILERLREWGVRRVFGYPGDGINGLLGALGrADDKPEFVQARHEEMAAFMAVAHAKfTGEVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 119 LNAIAGAYSENLPVICIVGGPNSNDFGTnrilhhtiglpDFSQEL---RCFQTVTC-YQAVVNNLEDAHEQIDKAIATAL 194
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGQQARAALGG-----------HYQQEVdlqSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 195 KESKPVYISISCNL--AATPHPTFARDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKLRvaKASEAFLEL 272
Cdd:PRK08273 152 AERTVTAVILPNDVqeLEYEPPPHAHGTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEVIAV 229
|
250 260
....*....|....*....|....*...
gi 15240950 273 ADASGYPLAVMPSTKGLVPENHPHFIGT 300
Cdd:PRK08273 230 AERLGAGVAKALLGKAALPDDLPWVTGS 257
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
51-510 |
1.85e-04 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 44.46 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 51 LVQAGVTDVFSVPG---D--FNlTLLDhliAEPELnnIGCCNELNAGYAADGYARSRG-VGACVVTftvGGLSVLNAIAG 124
Cdd:PRK08617 15 LINQGVKYVFGIPGakiDrvFD-ALED---SGPEL--IVTRHEQNAAFMAAAIGRLTGkPGVVLVT---SGPGVSNLATG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 125 ---AYSENLPVICIVGGPNSNDFGtnRILHHTIGlpdfSQELrcFQTVTCYQAVVNNLEDAHEQIDKAIATAlKESKP-- 199
Cdd:PRK08617 86 lvtATAEGDPVVAIGGQVKRADRL--KRTHQSMD----NVAL--FRPITKYSAEVQDPDNLSEVLANAFRAA-ESGRPga 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 200 VYISISCNLAATPHPTFARDPVPfdlTPRMSNTMglEAAVEATLEFLNKAVKPVMVGGPKLRVAKASEAFLELADASGYP 279
Cdd:PRK08617 157 AFVSLPQDVVDAPVTSKAIAPLS---KPKLGPAS--PEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 280 LAVMPSTKGLVPENH-PHFIGTYwGAVSTPFCSEIVESADAYIFAGpifndYSSVGY--SLLLKKEKAIIVH-------- 348
Cdd:PRK08617 232 VVETFQAAGVISRELeDHFFGRV-GLFRNQPGDELLKKADLVITIG-----YDPIEYepRNWNSEGDATIIHidvlpaei 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 349 -----PDRVVVAN--------GPTFGCVLMSDFFRELAKRVKRNETayENYERIFVPEGKPLkckpgEPLRVnamFQHIQ 415
Cdd:PRK08617 306 dnyyqPERELIGDiaatldllAEKLDGLSLSPQSLEILEELRAQLE--ELAERPARLEEGAV-----HPLRI---IRALQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 416 KMLSSETAVIAETGdS---W-------FNCQKLKLPKGcgyefqMQygSIG----WSVGATLgyaqATPEKRVLSFIGDG 481
Cdd:PRK08617 376 DIVTDDTTVTVDVG-ShyiWmaryfrsYEPRHLLFSNG------MQ--TLGvalpWAIAAAL----VRPGKKVVSVSGDG 442
|
490 500 510
....*....|....*....|....*....|
gi 15240950 482 SFQVTAQDISTMIRNGQKaIIFLI-NNGGY 510
Cdd:PRK08617 443 GFLFSAMELETAVRLKLN-IVHIIwNDGHY 471
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
418-512 |
5.55e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 41.36 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 418 LSSETAVIAETG----DSWFNCQKlklPKgcgyEFQMqYGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTM 493
Cdd:PRK06163 26 LKDEEAVIGGIGntnfDLWAAGQR---PQ----NFYM-LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTI 97
|
90 100
....*....|....*....|
gi 15240950 494 I-RNGQKAIIFLINNGGYTI 512
Cdd:PRK06163 98 AaLAPKNLTIIVMDNGVYQI 117
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
443-582 |
6.12e-04 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 41.14 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 443 GCGYEFQMQyGSIGWSVGATLGYAQATPEKRVLSFIGDGSFQVTAQDISTmirNGQKA----IIFLINNGgytieveIHD 518
Cdd:cd03371 39 GHAQDFLTV-GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLAT---IGGLApanlIHIVLNNG-------AHD 107
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 519 ---GPYNVIKNWNYTGLVDAihngegkCWTTKVRYE---EELVEAIKTATTEkkDSLCFIEVIVHKDDTS 582
Cdd:cd03371 108 svgGQPTVSFDVSLPAIAKA-------CGYRAVYEVpslEELVAALAKALAA--DGPAFIEVKVRPGSRS 168
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| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
45-133 |
3.61e-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: 38.63 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 45 RHLSRRLVQAGVTDVFSVPGDFN--LTLLdhLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTfTvGGLSVLN-- 120
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSapLALA--AAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVC-T-SGTAVANll 76
|
90
....*....|....
gi 15240950 121 -AIAGAYSENLPVI 133
Cdd:cd07037 77 pAVVEAYYSGVPLL 90
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| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
41-279 |
3.68e-03 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 40.36 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 41 STLGRHLSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGA-CVVTFTVGGLSVL 119
Cdd:PRK09124 3 QTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAvCAGSCGPGNLHLI 82
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 120 NAIAGAYSENLPVICIVGG-PNSNdfgtnrilhhtIGLPDFS----QELrcFQTVTCYQAVVNNLEDAHEQIDKAIATAL 194
Cdd:PRK09124 83 NGLFDCHRNHVPVLAIAAHiPSSE-----------IGSGYFQethpQEL--FRECSHYCELVSNPEQLPRVLAIAMRKAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 195 KESKPVYISISCNLAATPHPtfaRDPVPFDLTPRMSNTMGLEAAVEATLEFLNKAVKPVMVGGPKlrVAKASEAFLELAD 274
Cdd:PRK09124 150 LNRGVAVVVLPGDVALKPAP---ERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSG--CAGAHDELVALAE 224
|
....*
gi 15240950 275 ASGYP 279
Cdd:PRK09124 225 TLKAP 229
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| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
47-137 |
5.91e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 39.44 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240950 47 LSRRLVQAGVTDVFSVPGDFNLTLLDHLIAEPELNNIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSvlNAIAgay 126
Cdd:PRK07586 7 LVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLA--NGLA--- 81
|
90
....*....|....*....
gi 15240950 127 seNL--------PVICIVG 137
Cdd:PRK07586 82 --NLhnarrartPIVNIVG 98
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