|
Name |
Accession |
Description |
Interval |
E-value |
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
16-608 |
1.39e-156 |
|
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: 487.74 E-value: 1.39e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 16 IQYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAH 95
Cdd:COG3961 8 GDYLLDRLAE-LGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGhphqTLLYSSF---FKEISGSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:COG3961 87 AGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLG----DGDFDHFlrmFEEVTVAQAVLTPENAAAEIDRVLAAALREKRP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 173 VYIALPQDLVEMPLKKEGLS---RPLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG3961 163 VYIELPRDVADAPIEPPEAPlplPPPASDPAALAAA----VAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 250 WPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG3961 238 IPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 330 TFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYFWPRVEKWLREDDVLCVEAGTSSFGAAD 409
Cdd:COG3961 318 IYPGVSLADFLEALAELLKKRSAPLPAPAPPPPPPP-----AAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 410 VRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeeeeTVASNGDG-ADENggdgeakgrRRVICVVGD 488
Cdd:COG3961 393 LRLPEGATFIAQPLWGSIGYT----------------------------LPAALGAAlAAPD---------RRVILLVGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 489 GALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTgWDYSSTLSYFGsasssspdssASSVSTHVLN 568
Cdd:COG3961 436 GAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIAN-WDYAKLPEAFG----------GGNALGFRVT 504
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 813212725 569 TESEFDEFLTTeANADPGNLRFVIVRFEDLDAPRMLKMMA 608
Cdd:COG3961 505 TEGELEEALAA-AEANTDRLTLIEVVLDKMDAPPLLKRLG 543
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
17-178 |
1.81e-70 |
|
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: 233.16 E-value: 1.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHA 96
Cdd:cd07038 1 EYLLERLKQ-LGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 97 GAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPHqtllYSSF---FKEIS-GSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:cd07038 80 GAYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGD----FDVFlkmFEEITcAAARLTDPENAAEEIDRVLRTALRESRP 155
|
....*.
gi 813212725 173 VYIALP 178
Cdd:cd07038 156 VYIEIP 161
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
18-541 |
6.54e-65 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 231.90 E-value: 6.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 18 YLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHAG 97
Cdd:PLN02573 21 HLARRLVE-IGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSVLNAIAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 98 AYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPH--QTLlysSFFKEISGSMLVVSETTRA-EEIDRALEIGVRRCLPVY 174
Cdd:PLN02573 100 AYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDfsQEL---RCFQTVTCYQAVINNLEDAhELIDTAISTALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 175 IALPQDLVEMPlkKEGLSR--------PLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIAD----AGASRDNIS--AEV 240
Cdd:PLN02573 177 ISVSCNLAAIP--HPTFSRepvpffltPRLSNKMSLEAA----VEAAAEFLNKAVKPVLVGGpklrVAKACKAFVelADA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 241 SNlisslptWPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELH 320
Cdd:PLN02573 251 SG-------YPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 321 ATWTSV-DGSTFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPLPtIRPASDKFVRHAYFWPRVEKWLREDDVLCVE 399
Cdd:PLN02573 324 PDRVTIgNGPAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEP-LKSEPGEPLRVNVLFKHIQKMLSGDTAVIAE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 400 AGTSSFGAADVRLPRGATMLSQWLWASIGFSVgatvgaavaaaegfqentkkrkaeeeetvasngdGAdeNGGDGEAKGR 479
Cdd:PLN02573 403 TGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSV----------------------------------GA--TLGYAQAAPD 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813212725 480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRgiTREYNAINTgWDYS 541
Cdd:PLN02573 447 KRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIH--DGPYNVIKN-WNYT 505
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
378-605 |
8.38e-52 |
|
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: 180.42 E-value: 8.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 378 RHAYFWPRVEKWLREDDVLCVEAGTSSFGAADVRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeee 457
Cdd:cd02005 3 TQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYS--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 458 eTVASNGDGAdenggdgeAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTg 537
Cdd:cd02005 56 -VPAALGAAL--------AAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIAN- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813212725 538 WDYSSTLSYFGsasssspdsSASSVSTHVLNTESEFDEFLtTEANADPGNLRFVIVRFEDLDAPRMLK 605
Cdd:cd02005 126 WNYTKLPEVFG---------GGGGGLSFRVKTEGELDEAL-KDALFNRDKLSLIEVILPKDDAPEALK 183
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
17-518 |
2.90e-49 |
|
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: 184.98 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:COG0028 7 DALVEALEA-EGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVTGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGLPSTSQLSSseilhhslgHPHQTLLYSSFFKEISG-SMLVvsetTRAEEIDRALEIGVR-----R 169
Cdd:COG0028 86 ADAYMDSVPVLAITGQVPTSLIGR---------GAFQEVDQVGLFRPITKwSYLV----TDPEDLPEVLRRAFRiatsgR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 170 CLPVYIALPQDLVEMPLKKEGLSRPLvKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG0028 153 PGPVVLDIPKDVQAAEAEEEPAPPEL-RGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLG- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 250 WPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG0028 231 APVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 330 TFPGVGM----KSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIR--PASDKFVRHAYFWPRVEKWLREDDVLCVEAGTS 403
Cdd:COG0028 310 YPVDLPIvgdaKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAayAADDGPIKPQRVIAALREALPDDAIVVTDVGQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 404 SFGAAD-VRLPRGATMLSQWLWASIGFsvgatvgaavaaaegfqentkkrkaeeeetvasnGDGAdengGDGEAKGR--R 480
Cdd:COG0028 390 QMWAARyLRFRRPRRFLTSGGLGTMGY----------------------------------GLPA----AIGAKLARpdR 431
|
490 500 510
....*....|....*....|....*....|....*...
gi 813212725 481 RVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:COG0028 432 PVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGL 469
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
17-189 |
1.54e-34 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 130.43 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:pfam02776 3 EALADVLKA-LGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGLPSTSQLssseilhhSLGHPHQTLLYSSFFKEISGSMLVVSETTRA-EEIDRALEIGV-RRCLPV 173
Cdd:pfam02776 82 ANAYVDSVPLLVISGQRPRSLV--------GRGALQQELDQLALFRPVTKWAVRVTSADEIpEVLRRAFRAALsGRPGPV 153
|
170
....*....|....*.
gi 813212725 174 YIALPQDLVEMPLKKE 189
Cdd:pfam02776 154 YLEIPLDVLLEEVDED 169
|
|
| Ribosomal_S30 |
pfam04758 |
Ribosomal protein S30; |
1507-1559 |
5.44e-32 |
|
Ribosomal protein S30;
Pssm-ID: 398432 Cd Length: 58 Bit Score: 118.91 E-value: 5.44e-32
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 813212725 1507 KVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKRR 1559
Cdd:pfam04758 1 KVHGSLARAGKVRNQTPKVEKQEKKKKPTGRAKKRLQYNRRFVNVVPGGGRKK 53
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
17-179 |
1.72e-26 |
|
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: 107.05 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLrDDLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHA 96
Cdd:cd06586 1 AAFAEVL-TAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 97 GAYAEQIPLIHLVGLPSTSQlssseilhHSLGHpHQTLLYSSFFKEISGSMLVV-SETTRAEEIDRALEIGVRRCLPVYI 175
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISA--------QAKQT-FQSMFDLGMYRSIPEANISSpSPAELPAGIDHAIRTAYASQGPVVV 150
|
....
gi 813212725 176 ALPQ 179
Cdd:cd06586 151 RLPR 154
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
17-179 |
6.59e-23 |
|
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: 96.83 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:cd07035 1 DALVEALKA-EGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGLPSTSQLSSseilhhslgHPHQTLLYSSFFKEIS-GSMLVvsetTRAEEIDRALEIGVRRCL--- 171
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGR---------GAFQEIDQVALFRPITkWAYRV----TSPEEIPEALRRAFRIALsgr 145
|
170
....*....|
gi 813212725 172 --PVYIALPQ 179
Cdd:cd07035 146 pgPVALDLPK 155
|
|
| PTZ00467 |
PTZ00467 |
40S ribosomal protein S30; Provisional |
1505-1558 |
1.75e-18 |
|
40S ribosomal protein S30; Provisional
Pssm-ID: 185646 Cd Length: 66 Bit Score: 80.97 E-value: 1.75e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 813212725 1505 MGKVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKR 1558
Cdd:PTZ00467 1 MGKIHGSLARAGKVKNQTPKVAKQEKPKQPRGRALKRLKYTRRFLAKTVKPGEK 54
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
210-305 |
3.92e-17 |
|
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: 79.53 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 210 ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPtWPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAA 289
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLG-IPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEA 78
|
90
....*....|....*.
gi 813212725 290 DFVLSIGALASDFNTG 305
Cdd:pfam00205 79 DLVLAVGARFDDIRTT 94
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
32-296 |
1.91e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 84.49 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 32 IFGVPGDFNLPALDYVEDFPgMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHL-- 108
Cdd:PRK08322 19 IFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAItg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 109 -VGLPSTSQLSsseilhhslghpHQTLLYSSFFKEI--------SGSML--VVSETTR-AEEidraleigvRRCLPVYIA 176
Cdd:PRK08322 98 qKPIKRSKQGS------------FQIVDVVAMMAPLtkwtrqivSPDNIpeVVREAFRlAEE---------ERPGAVHLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 177 LPQDLVEMplkkEGLSRPLVKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTwPLFVSA 256
Cdd:PRK08322 157 LPEDIAAE----ETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGI-PFFTTQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 813212725 257 MGKGSVNEQHPSFagtyMGTLSLPP---VRTAVEAADFVLSIG 296
Cdd:PRK08322 232 MGKGVIPETHPLS----LGTAGLSQgdyVHCAIEHADLIINVG 270
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
21-296 |
4.87e-16 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 83.66 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 21 HRLRDDLH---INSIFG--VPGDFNLPALDYvedfpGMKWIGAVNELNGGYAADGYARVKGAGALVTtfgvgelsAMNAH 95
Cdd:PRK06112 18 HAIARALKrhgVEQIFGqsLPSALFLAAEAI-----GIRQIAYRTENAGGAMADGYARVSGKVAVVT--------AQNGP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGA-----YAE----QIPLIHLVGLPSTSQLSSSEIlhhslghphQTLLYSSFFKEISGSMLVVSETTRAEE-IDRALEI 165
Cdd:PRK06112 85 AATllvapLAEalkaSVPIVALVQDVNRDQTDRNAF---------QELDHIALFQSCTKWVRRVTVAERIDDyVDQAFTA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 166 GVR-RCLPVYIALPQDLVEMPLKKEGLSRPlvkdiDNL-------SAAEMRVISEVLGLLSSCSKPIIIADAGASRDNIS 237
Cdd:PRK06112 156 ATSgRPGPVVLLLPADLLTAAAAAPAAPRS-----NSLghfpldrTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGAS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725 238 AEVSNLiSSLPTWPLFVSAMGKGSVNEQHPSFAG---TYMGTLSLPP-VRTAVEAADFVLSIG 296
Cdd:PRK06112 231 AALAAL-QSLAGLPVATTNMGKGAVDETHPLSLGvvgSLMGPRSPGRhLRDLVREADVVLLVG 292
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
29-305 |
5.50e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 83.27 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIH 107
Cdd:PRK06276 16 VKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGIATAYADSSPVIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 108 LVGLPSTsqlssseilhhslghphqTLLYSSFFKEISGSMLVVSET------TRAEEI----DRALEIGVR-RCLPVYIA 176
Cdd:PRK06276 95 LTGQVPT------------------KLIGNDAFQEIDALGIFMPITkhnfqiKKPEEIpeifRAAFEIAKTgRPGPVHID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 177 LPQDLVEMPLKKEglSRPLVKDID-----NLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLiSSLPTWP 251
Cdd:PRK06276 157 LPKDVQEGELDLE--KYPIPAKIDlpgykPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIEL-SELVKIP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 813212725 252 LFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK06276 234 VCTTLMGKGAFPEDHPLALGM-VGMHGTKAANYSVTESDVLIAIGCRFSDRTTG 286
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
19-518 |
2.72e-13 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 74.61 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 19 LLHRLRddlhINSIFGVPGDFNLPAL-DYVEDFpgmKWIGAVNELNGGYAADGYARVKGAGALV---TTFGVGelSAMNA 94
Cdd:PRK07092 21 LLRRFG----ITTVFGNPGSTELPFLrDFPDDF---RYVLGLQEAVVVGMADGYAQATGNAAFVnlhSAAGVG--NAMGN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 95 HAGAYAEQIPLIHLVGLPSTSQLssseilhhslghPHQTLLYSSFFKEISGSMLVVS-ETTRAEEIDRALEIGVR----- 168
Cdd:PRK07092 92 LFTAFKNHTPLVITAGQQARSIL------------PFEPFLAAVQAAELPKPYVKWSiEPARAEDVPAAIARAYHiamqp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 169 RCLPVYIALPQDLVEMPlkKEGLSRPLVKDIDNLSAAEMRVISEVLGllsSCSKPIIIADAGASRDNISAEVSNLISSLP 248
Cdd:PRK07092 160 PRGPVFVSIPYDDWDQP--AEPLPARTVSSAVRPDPAALARLGDALD---AARRPALVVGPAVDRAGAWDDAVRLAERHR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 249 TwPLFVSAM-GKGSVNEQHPSFAGTymgtlsLPPVRTAVEAA----DFVLSIGALASDFNT-GFGSMDFEGKVVVEL--- 319
Cdd:PRK07092 235 A-PVWVAPMsGRCSFPEDHPLFAGF------LPASREKISALldghDLVLVIGAPVFTYHVeGPGPHLPEGAELVQLtdd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 320 --HATWTSVDGSTF--PGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYfwprveKWLREDDV 395
Cdd:PRK07092 308 pgEAAWAPMGDAIVgdIRLALRDLLALLPPSARPAPPARPMPPPAPAPGE-----PLSVAFVLQTL------AALRPADA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 396 LCVEAGTSSFGAadvrlprgatmlsqwlwasigfsvgatvgaavaaaegFQENTKKRKAEEEETVASNGDGADENGGDGE 475
Cdd:PRK07092 377 IVVEEAPSTRPA-------------------------------------MQEHLPMRRQGSFYTMASGGLGYGLPAAVGV 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 813212725 476 AKGR--RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:PRK07092 420 ALAQpgRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
28-296 |
5.55e-13 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 73.49 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 28 HINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGelsAMNAhAGAYAEQI--- 103
Cdd:PRK07064 17 GVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGlGVALTSTGTG---AGNA-AGALVEALtag 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 104 -PLIHLvglpsTSQLsSSEILHHSLGHPHQTLLYSSFFKEISGSMLVVSETTRAEEIdraLEIGVRRCL-----PVYIAL 177
Cdd:PRK07064 93 tPLLHI-----TGQI-ETPYLDQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETALAT---IREAVRVALtaptgPVSVEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 178 PQDL----VEMPLkkegLSRPLVKDIDNLSAAEmrvISEVLGLLSSCSKPIIIADAGASrdNISAEVSNLISSlpTWPLF 253
Cdd:PRK07064 164 PIDIqaaeIELPD----DLAPVHVAVPEPDAAA---VAELAERLAAARRPLLWLGGGAR--HAGAEVKRLVDL--GFGVV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 813212725 254 VSAMGKGSVNEQHPSFAGTYMGTlslPPVRTAVEAADFVLSIG 296
Cdd:PRK07064 233 TSTQGRGVVPEDHPASLGAFNNS---AAVEALYKTCDLLLVVG 272
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
65-311 |
5.68e-13 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 73.47 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 65 GYAADGYARVKG--AGALVTTfGVGELSAMNAHAGAYAEQIPLIHLVGLPSTSQLSsseilhHSLGHPHQTLLYSSFFKE 142
Cdd:PRK07524 52 GFMADGYARVSGkpGVCFIIT-GPGMTNIATAMGQAYADSIPMLVISSVNRRASLG------KGRGKLHELPDQRAMVAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 143 ISgsmlVVSET-TRAEE----IDRA---LEIGvrRCLPVYIALPQDLVEMPLkKEGLSRPLVKDIDNLSAAEMrvISEVL 214
Cdd:PRK07524 125 VA----AFSHTlMSAEDlpevLARAfavFDSA--RPRPVHIEIPLDVLAAPA-DHLLPAPPTRPARPGPAPAA--LAQAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 215 GLLSSCSKPIIIADAGASRDNisAEVSNLISSLPTwPLFVSAMGKGSVNEQHPSFAGtymGTLSLPPVRTAVEAADFVLS 294
Cdd:PRK07524 196 ERLAAARRPLILAGGGALAAA--AALRALAERLDA-PVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLA 269
|
250
....*....|....*..
gi 813212725 295 IGalasdfnTGFGSMDF 311
Cdd:PRK07524 270 VG-------TELGETDY 279
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
29-305 |
1.69e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 72.11 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIH 107
Cdd:PRK06048 23 VEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGATNLVTGIATAYMDSVPIVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 108 LVGLPSTSqlssseilhhslghphqtLLYSSFFKE--ISGSMLVVSE----TTRAEEIDR----ALEIG-VRRCLPVYIA 176
Cdd:PRK06048 102 LTGQVPRS------------------MIGNDAFQEadITGITMPITKhnylVQDAKDLPRiikeAFHIAsTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 177 LPQDL------------VEMPLKKeglsrPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLI 244
Cdd:PRK06048 164 LPKDVttaeidfdypdkVELRGYK-----PTYK-------GNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 813212725 245 SSLPTwPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK06048 232 ETIPA-PVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTG 290
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
476-518 |
3.25e-12 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 65.68 E-value: 3.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:pfam02775 43 ARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGY 85
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
29-336 |
4.08e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 71.02 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALD-YVEDFPG--MKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK06456 17 VKVIFGIPGLSNMQIYDaFVEDLANgeLRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTTNLVTGLITAYWDSSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 105 LIHLVGlpstsQLSSSEILHHSLGHPHQTLLYSSFFKeisgsmlVVSETTRAEEIDRALE-----IGVRRCLPVYIALPQ 179
Cdd:PRK06456 97 VIAITG-----QVPRSVMGKMAFQEADAMGVFENVTK-------YVIGIKRIDEIPQWIKnafyiATTGRPGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 180 DLVEMPLKK-EGLSRPLVKDIDNLSAAEMRV-ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLiSSLPTWPLFVSAM 257
Cdd:PRK06456 165 DIFYEKMEEiKWPEKPLVKGYRDFPTRIDRLaLKKAAEILINAERPIILVGTGVVWSNATPEVLEL-AELLHIPIVSTFP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 258 GKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFN-TGFGSMDFEGKVVVELHATWTSVDGSTFPGVGM 336
Cdd:PRK06456 244 GKTAIPHDHPLYFGP-MGYYGRAEASMAALESDAMLVVGARFSDRTfTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVGI 322
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
17-305 |
7.84e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 69.85 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAH 95
Cdd:PRK07282 14 DLVLETLRD-LGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKlGVAVVTSGPGATNAITGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGLPSTSQLSSSEILH-HSLGHPHQTLLYSSFFKEISGSMLVVSEttraeeidrALEIGVR-RCLPV 173
Cdd:PRK07282 93 ADAMSDSVPLLVFTGQVARAGIGKDAFQEaDIVGITMPITKYNYQIRETADIPRIITE---------AVHIATTgRPGPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 174 YIALPQDLVEmpLKKEGLSRPLVK---DIDNLSAAEMRvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTw 250
Cdd:PRK07282 164 VIDLPKDVSA--LETDFIYDPEVNlpsYQPTLEPNDMQ-IKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQI- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725 251 PLFVSAMGKGSVNEQHPSFAGtyMGTLSLP-PVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07282 240 PVVTTLLGQGTIATSHPLFLG--MGGMHGSyAANIAMTEADFMINIGSRFDDRLTG 293
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
390-518 |
4.96e-11 |
|
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: 63.04 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 390 LREDDVLCVEAGTSSFGAAD-VRLPRGATMLSQWLWASIGFSVGAtvgaavaaaegfqentkkrkaeeeetvasnGDGAd 468
Cdd:cd00568 10 LPEDAIVVNDAGNSAYWAYRyLPLRRGRRFLTSTGFGAMGYGLPA------------------------------AIGA- 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 813212725 469 enggdGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd00568 59 -----ALAAPDRPVVCIAGDGGFMMTGQELATAVRYGLPVIVVVFNNGGY 103
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
17-516 |
9.02e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 66.48 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 17 QYLLHRLRDDlHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:PRK06882 8 EMVVQSLRDE-GVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 96 AGAYAEQIPLIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE----------ISGSMLVVSETTRAEEIDRALEI 165
Cdd:PRK06882 87 ATAYTDSVPLVILSG-----QVPSN-------------LIGTDAFQEcdmlgisrpvVKHSFIVKNAEDIPSTIKKAFYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 166 G-VRRCLPVYIALPQDLVEmPLKKEGLSRPlvkdidnlSAAEMRV-----------ISEVLGLLSSCSKPIIIADAGASR 233
Cdd:PRK06882 149 AsTGRPGPVVIDIPKDMVN-PANKFTYEYP--------EEVSLRSynptvqghkgqIKKALKALLVAKKPVLFVGGGVIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 234 DNISAEVSNLISSLpTWPLFVSAMGKGSvneqHPSFAGTYMGTLSLP---PVRTAVEAADFVLSIGALASDFNTGFGSMD 310
Cdd:PRK06882 220 AECSEQLTQFAQKL-NLPVTSSLMGLGA----YPSTDKQFLGMLGMHgtyEANNAMHESDLILGIGVRFDDRTTNNLAKY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 311 FEGKVVVELHATWTSVD---GSTFPGVG-MKSLLPRLASSLSpitssapippspslslPLPTIRPASDKfvrhAYFWPRV 386
Cdd:PRK06882 295 CPNAKVIHIDIDPTSISknvPAYIPIVGsAKNVLEEFLSLLE----------------EENLAKSQTDL----TAWWQQI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 387 EKWlreDDVLCVEAGTSSfgaaDVRLPRGATMLSQWLWASIGFSVGATVGAAVAAAEGFQENtKKRKAEEEETVASNGDG 466
Cdd:PRK06882 355 NEW---KAKKCLEFDRTS----DVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFD-KPRRWINSGGAGTMGFG 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 813212725 467 ADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK06882 427 LPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
26-516 |
2.29e-09 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 62.18 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK07979 16 DQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 105 LIHLVGlpstsQLSSSEILHHSLGHPHQTLLYSSFFKEisgSMLVvsetTRAEEIDRALE-----IGVRRCLPVYIALPQ 179
Cdd:PRK07979 96 LVVLSG-----QVATSLIGYDAFQECDMVGISRPVVKH---SFLV----KQTEDIPQVLKkafwlAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 180 DLVEmPLKKEGLSRP---LVKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSA 256
Cdd:PRK07979 164 DILN-PANKLPYVWPesvSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKL-NLPVVSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 257 MGKGsvneqhpSFAGTYMGTLSLPPVRTAVEA------ADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGST 330
Cdd:PRK07979 242 MGLG-------AFPATHRQSLGMLGMHGTYEAnmtmhnADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 331 ---FPGVG--------MKSLLPRLASSLSPitssapippspslslplPTIRPasdkfvrhayFWPRVEKWlREDDVLCVE 399
Cdd:PRK07979 315 tadIPIVGdarqvleqMLELLSQESAHQPL-----------------DEIRD----------WWQQIEQW-RARQCLKYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 400 AGTSSFGAADV-----RLPRGATMLSQWLWASIGFSvgatvgaavaaaEGFQENTKKRKAEEEETVASNGDGADENGGDG 474
Cdd:PRK07979 367 THSEKIKPQAVietlwRLTKGDAYVTSDVGQHQMFA------------ALYYPFDKPRRWINSGGLGTMGFGLPAALGVK 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 813212725 475 EAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK07979 435 MALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 476
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
29-311 |
6.48e-09 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 60.40 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYvedFP--GMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPL 105
Cdd:PRK07525 21 ITHAFGIIGSAFMDASDL---FPpaGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYWAHTPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 106 IhLVglpsTSQLSSSEIlhhSLGHpHQTLLYSSFFKEISGSMLVVSETTRAEEI-DRALEIGVRRCLPVYIALPQDL--- 181
Cdd:PRK07525 98 V-LV----TPQAGTKTI---GQGG-FQEAEQMPMFEDMTKYQEEVRDPSRMAEVlNRVFDKAKRESGPAQINIPRDYfyg 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 182 ---VEMPlKKEGLSRPlvkdidnlsAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSAMG 258
Cdd:PRK07525 169 vidVEIP-QPVRLERG---------AGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERL-DAPVACGYLH 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 259 KGSVNEQHPSFAGT--YMGTlslppvRTAVE---AADFVLSIGALASDFNT--GFGsMDF 311
Cdd:PRK07525 238 NDAFPGSHPLWVGPlgYNGS------KAAMEliaKADVVLALGTRLNPFGTlpQYG-IDY 290
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
476-516 |
2.39e-08 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 55.58 E-value: 2.39e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:cd02015 65 ARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNG 105
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
26-516 |
4.88e-08 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 57.52 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK08979 16 DEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDSIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 105 LIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE----------ISGSMLVVSETTRAEEIDRALEIGVR-RCLPV 173
Cdd:PRK08979 96 MVVLSG-----QVPSN-------------LIGNDAFQEcdmigisrpvVKHSFLVKDAEDIPEIIKKAFYIASTgRPGPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 174 YIALPQDLVEmPLKKEGLSRPlvkdidnlSAAEMRV-----------ISEVLGLLSSCSKPIIIADAGASRDNISAEVSN 242
Cdd:PRK08979 158 VIDLPKDCLN-PAILHPYEYP--------ESIKMRSynpttsghkgqIKRGLQALLAAKKPVLYVGGGAIISGADKQILQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 243 LISSLpTWPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTgfGSMDFEGKVVVELHat 322
Cdd:PRK08979 229 LAEKL-NLPVVSTLMGLGAFPGTHKNSLGM-LGMHGRYEANMAMHNADLIFGIGVRFDDRTT--NNLEKYCPNATILH-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 323 wTSVDGSTFPGVgMKSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIrpasdkfvrhAYFWPRVEKWlREDDVLCVEAGT 402
Cdd:PRK08979 303 -IDIDPSSISKT-VRVDIPIVGSADKVLDSMLALLDESGETNDEAAI----------ASWWNEIEVW-RSRNCLAYDKSS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 403 SSFGAADV-----RLPRGATMLSQWLWASIGFSvgatvgaavaaaEGFQENTKKRKAEEEETVASNGDGADENGGDGEAK 477
Cdd:PRK08979 370 ERIKPQQVietlyKLTNGDAYVASDVGQHQMFA------------ALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAM 437
|
490 500 510
....*....|....*....|....*....|....*....
gi 813212725 478 GRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK08979 438 PDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNR 476
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
32-185 |
5.14e-08 |
|
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: 54.09 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:cd07039 18 VYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKlGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAG 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 813212725 111 lpstsQLSSSEILHHSlghpHQTLLYSSFFKEISG-SMLVVSETTRAEEIDRALEIGV-RRCLPVyIALPQDLVEMP 185
Cdd:cd07039 98 -----QVPTDELGTDY----FQEVDLLALFKDVAVyNETVTSPEQLPELLDRAIRTAIaKRGVAV-LILPGDVQDAP 164
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
66-543 |
7.98e-08 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 57.12 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 66 YAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLI--------HLVGLPSTSQLSSSEILHHSLGHphqtlly 136
Cdd:PRK06965 73 HAADGYARATGkVGVALVTSGPGVTNAVTGIATAYMDSIPMVvisgqvptAAIGQDAFQECDTVGITRPIVKH------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 137 ssffkeisgSMLVVSETTRAEEIDRALEIG-VRRCLPVYIALPQDLvemPLKKEGLSRPlvkdidnlSAAEMRV------ 209
Cdd:PRK06965 146 ---------NFLVKDVRDLAETVKKAFYIArTGRPGPVVVDIPKDV---SKTPCEYEYP--------KSVEMRSynpvtk 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 210 -----ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRT 284
Cdd:PRK06965 206 ghsgqIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLL-GYPVTNTLMGLGAYPASDKKFLGM-LGMHGTYEANM 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 285 AVEAADFVLSIGALASDFNTG----FGSMdfEGKVV-VELHATWTS----VDgstFPGVG-MKSLLPRLASSLSpitssa 354
Cdd:PRK06965 284 AMQHCDVLIAIGARFDDRVIGnpahFASR--PRKIIhIDIDPSSISkrvkVD---IPIVGdVKEVLKELIEQLQ------ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 355 pippspslslpLPTIRPASDKFvrhAYFWPRVEKWLREDdvlCVEAGTSSfgaaDVRLPRgatMLSQWLWASIGFSVGAT 434
Cdd:PRK06965 353 -----------TAEHGPDADAL---AQWWKQIEGWRSRD---CLKYDRES----EIIKPQ---YVVEKLWELTDGDAFVC 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 435 VGAAVAAAEGFQentKKRKAEEEETVASNGDGADENG-----GDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGAT 509
Cdd:PRK06965 409 SDVGQHQMWAAQ---FYRFNEPRRWINSGGLGTMGVGlpyamGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVK 485
|
490 500 510
....*....|....*....|....*....|....
gi 813212725 510 IFVVDNRgytvekYIrGITREYNAINTGWDYSST 543
Cdd:PRK06965 486 IISLNNR------YL-GMVRQWQEIEYSKRYSHS 512
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
29-516 |
9.56e-08 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 56.63 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYV---EDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:CHL00099 25 VKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQMDSVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 105 LIHLVGlpstsQLSSSEIlhhslGhphqtllySSFFKE--ISGSML-------VVSETTRAEEI-DRALEIGVR-RCLPV 173
Cdd:CHL00099 105 LLVITG-----QVGRAFI-----G--------TDAFQEvdIFGITLpivkhsyVVRDARDISRIvAEAFYIAKHgRPGPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 174 YIALPQDL------------VEMPLKKEGLsRPLVKDidnlsaaEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVS 241
Cdd:CHL00099 167 LIDIPKDVglekfdyyppepGNTIIKILGC-RPIYKP-------TIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 242 NLISSLPTwPLFVSAMGKGSVNEQHPsfagTYMGTLSL---PPVRTAVEAADFVLSIGALASDFNTG----FGSmdfeGK 314
Cdd:CHL00099 239 ELAELYKI-PVTTTLMGKGIFDEDHP----LCLGMLGMhgtAYANFAVSECDLLIALGARFDDRVTGkldeFAC----NA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 315 VVVELHATWTSVDGSTFPGVGM----KSLLPRLASSLSpitssapippspslslpLPTIRPASDKFvrhaYFW-PRVEKW 389
Cdd:CHL00099 310 QVIHIDIDPAEIGKNRIPQVAIvgdvKKVLQELLELLK-----------------NSPNLLESEQT----QAWrERINRW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 390 lREDDVLCVEAGTSSFGAADV-----RLPRGA---TMLSQ-WLWASigfsvgatvgaavaaaeGFQEnTKKRKAEEEETV 460
Cdd:CHL00099 369 -RKEYPLLIPKPSTSLSPQEVineisQLAPDAyftTDVGQhQMWAA-----------------QFLK-CKPRKWLSSAGL 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725 461 ASNGDGADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:CHL00099 430 GTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNK 485
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
29-296 |
1.30e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 56.17 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYVEDFPG-MKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLI 106
Cdd:PRK08266 19 VDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGrPGVCSVVPGPGVLNAGAALLTAYGCNSPVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 107 HLvglpsTSQLSSSEI------LHHSlghPHQTLLYSSFFKeISGSMLVVSE--TTRAEEIDRALEiGVRRclPVYIALP 178
Cdd:PRK08266 99 CL-----TGQIPSALIgkgrghLHEM---PDQLATLRSFTK-WAERIEHPSEapALVAEAFQQMLS-GRPR--PVALEMP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 179 QDL------VEMPLKKEGLSRPLVkDIDNLSAAEmrvisevlGLLSSCSKPIIIADAGASrdNISAEVSNLISSLPTwPL 252
Cdd:PRK08266 167 WDVfgqrapVAAAPPLRPAPPPAP-DPDAIAAAA--------ALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQA-PV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 813212725 253 FVSAMGKGSVNEQHPSFagtymgtLSLPPVRTAVEAADFVLSIG 296
Cdd:PRK08266 235 VAFRSGRGIVSDRHPLG-------LNFAAAYELWPQTDVVIGIG 271
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
25-305 |
6.56e-07 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 54.22 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 25 DDLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQI 103
Cdd:PRK07789 42 EELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrVGVCMATSGPGATNLVTPIADANMDSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 104 PLIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE--ISG--------SMLVvsetTRAEEIDRALEIGVR----- 168
Cdd:PRK07789 122 PVVAITG-----QVGRG-------------LIGTDAFQEadIVGitmpitkhNFLV----TDADDIPRVIAEAFHiastg 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 169 RCLPVYIALPQDL------------VEMPlkkeGLsRPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNI 236
Cdd:PRK07789 180 RPGPVLVDIPKDAlqaqttfswpprMDLP----GY-RPVTK-------PHGKQIREAAKLIAAARRPVLYVGGGVIRAEA 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725 237 SAEVSNLiSSLPTWPLFVSAMGKGSVNEQHPSFAGtyM----GTLslpPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07789 248 SAELREL-AELTGIPVVTTLMARGAFPDSHPQHLG--MpgmhGTV---AAVAALQRSDLLIALGARFDDRVTG 314
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
476-518 |
9.41e-07 |
|
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: 50.67 E-value: 9.41e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd02002 64 ANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGY 106
|
|
| PRK09336 |
PRK09336 |
30S ribosomal protein S30e; Provisional |
1509-1552 |
1.84e-06 |
|
30S ribosomal protein S30e; Provisional
Pssm-ID: 181786 Cd Length: 50 Bit Score: 46.32 E-value: 1.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 813212725 1509 HGSLARAGKVKSQCPKVEKQEKKKTPKgRAYKRMVYNRRFVNVT 1552
Cdd:PRK09336 4 HGSLTKAGKVRSQTPKIPPKPKKNEVP-RVRNRREYERRVLKAR 46
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
27-516 |
2.03e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 52.28 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 27 LHINSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPL 105
Cdd:PRK06725 28 LGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNLVTGLADAYMDSIPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 106 IHLVGLPSTSqlssseilhhslghphqtLLYSSFFKEISGSMLVVSETTRAEEIDRALEIG--VRRCL---------PVY 174
Cdd:PRK06725 107 VVITGQVATP------------------LIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSriVQEAFyiaesgrpgPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 175 IALPQDLVEMPLKKEGLSRPLVKDIDNLSAAEMRVISEVLGLLSSCSKPII-----IADAGASRDNISAEVSNLIsslpt 249
Cdd:PRK06725 169 IDIPKDVQNEKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLyigggVIHSGGSEELIEFARENRI----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 250 wPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTG---------------FGSMDFEGK 314
Cdd:PRK06725 244 -PVVSTLMGLGAYPPGDPLFLGM-LGMHGTYAANMAVTECDLLLALGVRFDDRVTGklelfsphskkvhidIDPSEFHKN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 315 VVVELhatwtsvdgstfPGVG-MKSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIRPASDKFVRHAYFWPRVEKWLRED 393
Cdd:PRK06725 322 VAVEY------------PVVGdVKKALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 394 DVLCVEAGTSSFGAA---DVRLPRgaTMLSQWLWASIGFSvgatvgaavaaaegFQENTKKRKAEEEETvasngdgaden 470
Cdd:PRK06725 390 AIVTTEVGQHQMWAAhfyKAKNPR--TFLTSGGLGTMGFG--------------FPAAIGAQLAKEEEL----------- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 813212725 471 ggdgeakgrrrVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK06725 443 -----------VICIAGDASFQMNIQELQTIAENNIPVKVFIINNK 477
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
19-297 |
2.66e-06 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 52.05 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 19 LLHRLRDDlHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAG 97
Cdd:PRK06466 10 LVRALRDE-GVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATNAITGIAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 98 AYAEQIPLIHLVG-LPSTS------QLS-----SSEILHHSLGHPHQtllyssffKEIsgsmlvvsettrAEEIDRALEI 165
Cdd:PRK06466 89 AYMDSIPMVVLSGqVPSTLigedafQETdmvgiSRPIVKHSFMVKHA--------SEI------------PEIIKKAFYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 166 -GVRRCLPVYIALPQDLVEmPLKKEGLSRPLVKDIDNLSAA---EMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVS 241
Cdd:PRK06466 149 aQSGRPGPVVVDIPKDMTN-PAEKFEYEYPKKVKLRSYSPAvrgHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLT 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725 242 NLISSLpTWPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGA 297
Cdd:PRK06466 228 ELAHLL-NLPVTNTLMGLGGFPGTDRQFLG-MLGMHGTYEANMAMHHADVILAVGA 281
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
32-305 |
4.32e-05 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 48.22 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 32 IFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:PRK07710 34 IFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGkPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 111 LPSTSqlssseilhhslghphqtLLYSSFFKE--ISGSMLVVS----ETTRAEEIDR----ALEIGVR-RCLPVYIALPQ 179
Cdd:PRK07710 113 QVATS------------------VIGSDAFQEadIMGITMPVTkhnyQVRKASDLPRiikeAFHIATTgRPGPVLIDIPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 180 DLV----------EMPLKK-EGLSRPLVKDIDNLSAAemrvisevlglLSSCSKPIIIADAGASRDNISAEVSNLISSLP 248
Cdd:PRK07710 175 DMVveegefcydvQMDLPGyQPNYEPNLLQIRKLVQA-----------VSVAKKPVILAGAGVLHAKASKELTSYAEQQE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725 249 TwPLFVSAMGKGSVNEQHPSFA------GTYMGTLslppvrtAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07710 244 I-PVVHTLLGLGGFPADHPLFLgmagmhGTYTANM-------ALYECDLLINIGARFDDRVTG 298
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
32-518 |
5.65e-05 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 47.56 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGelsAMNAHAG---AYAEQIPLIH 107
Cdd:PRK08199 26 VFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRpGICFVTRGPG---ATNASIGvhtAFQDSTPMIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 108 LVGlpstsQLSSseilHHSLGHPHQTLLYSSFFkeisGSMlvvseTTRAEEIDRALEIG--VRRCL---------PVYIA 176
Cdd:PRK08199 103 FVG-----QVAR----DFREREAFQEIDYRRMF----GPM-----AKWVAEIDDAARIPelVSRAFhvatsgrpgPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 177 LPQD-LVE------MPLKKEGLSRPLVKDIDNLSAaemrvisevlgLLSSCSKPIIIA-----DAGASRDNIS-AEVSNL 243
Cdd:PRK08199 165 LPEDvLSEtaevpdAPPYRRVAAAPGAADLARLAE-----------LLARAERPLVILggsgwTEAAVADLRAfAERWGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 244 isslptwPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGALASDFNT-GFGSMDFEG--KVVVELH 320
Cdd:PRK08199 234 -------PVACAFRRQDLFDNRHPNYAG-DLGLGINPALAARIREADLVLAVGTRLGEVTTqGYTLLDIPVprQTLVHVH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 321 ATwTSVDGSTF-PGVGMKSLLPRLASSLSPITSSApippspslslplpTIRPASDKFVRHAYF--W------------PR 385
Cdd:PRK08199 306 PD-AEELGRVYrPDLAIVADPAAFAAALAALEPPA-------------SPAWAEWTAAAHADYlaWsaplpgpgavqlGE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 386 VEKWLRE----DDVLCVEAGT-SSFGAADVRLPRGATMLSqwlwasigfsvgatvgaavaaaegfqentkkrkaeeeETV 460
Cdd:PRK08199 372 VMAWLRErlpaDAIITNGAGNyATWLHRFFRFRRYRTQLA-------------------------------------PTS 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 813212725 461 ASNGDGADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:PRK08199 415 GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMY 472
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
480-516 |
6.19e-05 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 45.21 E-value: 6.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 813212725 480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:cd02014 70 RQVIALSGDGGFAMLMGDLITAVKYNLPVIVVVFNNS 106
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
476-517 |
7.70e-05 |
|
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: 44.83 E-value: 7.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRG 517
Cdd:cd02004 63 ARPDKRVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGG 104
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
18-231 |
2.17e-04 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 46.06 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 18 YLLHRLRDdLHINSIFGVPGDFN---LPALDYVEDfpGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMN 93
Cdd:PRK08273 8 FILERLRE-WGVRRVFGYPGDGInglLGALGRADD--KPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGAIHLLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 94 AHAGAYAEQIPLIHLVGLPSTSQLSsseilhhslGHPHQTLLYSSFFKEISGS---MLVVSETTRaEEIDRALEIGVRRC 170
Cdd:PRK08273 85 GLYDAKLDHVPVVAIVGQQARAALG---------GHYQQEVDLQSLFKDVAGAfvqMVTVPEQLR-HLVDRAVRTALAER 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725 171 LPVYIALPQDLVEMPLKKE-----------GLSRP-LVKDIDNLSAAemrviSEVlglLSSCSKPIIIADAGA 231
Cdd:PRK08273 155 TVTAVILPNDVQELEYEPPphahgtvhsgvGYTRPrVVPYDEDLRRA-----AEV---LNAGRKVAILVGAGA 219
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
32-305 |
4.83e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 44.70 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:PRK08527 21 VFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATAYMDSIPLVLISG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 111 LPSTSQLSS---SEILHHSLGHP---HQTLLyssffKEISGSMLVVSEttrAEEIDRALEIGvrrclPVYIALPQDL--- 181
Cdd:PRK08527 101 QVPNSLIGTdafQEIDAVGISRPcvkHNYLV-----KSIEELPRILKE---AFYIARSGRPG-----PVHIDIPKDVtat 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 182 ---------VEMPLKKeglsrPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTwPL 252
Cdd:PRK08527 168 lgefeypkeISLKTYK-----PTYK-------GNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGI-PA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 813212725 253 FVSAMGKGSVNEQHPSFA------GTYMGTLslppvrtAVEAADFVLSIGALASDFNTG 305
Cdd:PRK08527 235 VETLMARGVLRSDDPLLLgmlgmhGSYAANM-------AMSECDLLISLGARFDDRVTG 286
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
26-115 |
4.85e-04 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 44.70 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK09107 23 DQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNAVTPLQDALMDSIP 102
|
90
....*....|.
gi 813212725 105 LIHLVGLPSTS 115
Cdd:PRK09107 103 LVCITGQVPTH 113
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
480-522 |
4.96e-04 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 42.88 E-value: 4.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 813212725 480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEK 522
Cdd:cd02013 72 RPVVAIAGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
480-516 |
5.70e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 44.66 E-value: 5.70e-04
10 20 30
....*....|....*....|....*....|....*..
gi 813212725 480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK07418 453 EEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNG 489
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
476-518 |
7.18e-04 |
|
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: 42.68 E-value: 7.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd02003 63 AKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
29-305 |
9.82e-04 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 43.82 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 29 INSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA--GALVTTFGVGELSAMNAHAGAYAEQIPLI 106
Cdd:PRK11269 19 VTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGniGVCIGTSGPAGTDMITGLYSASADSIPIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 107 HLVGLPSTSQLSSSEIlhhslghphQTLLYSSFFKEISGSMLVVSETTRAEEI-DRALEIgVR--RCLPVYIALPQDlVE 183
Cdd:PRK11269 99 CITGQAPRARLHKEDF---------QAVDIESIAKPVTKWAVTVREPALVPRVfQQAFHL-MRsgRPGPVLIDLPFD-VQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725 184 M-----------PLKkegLSRPlvkdidnlsAAEMRVISEVLGLLSSCSKPIIIADAGAsrdnISAEVSNLI---SSLPT 249
Cdd:PRK11269 168 VaeiefdpdtyePLP---VYKP---------AATRAQIEKALEMLNAAERPLIVAGGGV----INADASDLLvefAELTG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725 250 WPLFVSAMGKGSVNEQHPSFAGTyMGtlslppVRTA-------VEAADFVLSIGALASDFNTG 305
Cdd:PRK11269 232 VPVIPTLMGWGAIPDDHPLMAGM-VG------LQTShrygnatLLASDFVLGIGNRWANRHTG 287
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
480-523 |
1.48e-03 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 43.07 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 813212725 480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKY 523
Cdd:PRK08611 427 RQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKY 470
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
482-515 |
1.91e-03 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 42.77 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|....
gi 813212725 482 VICVVGDGALQMGIQEISNLVRYNLGATIFVVDN 515
Cdd:PRK09107 451 VIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
476-515 |
5.43e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 41.23 E-value: 5.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 813212725 476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDN 515
Cdd:PRK08155 434 ANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNN 473
|
|
| |
