|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05858 |
PRK05858 |
acetolactate synthase; |
65-373 |
1.44e-75 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 244.63 E-value: 1.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 65 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK05858 6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:PRK05858 166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361023 305 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 373
Cdd:PRK05858 213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG 280
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
64-392 |
4.52e-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: 243.53 E-value: 4.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 64 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DVLYpyfmvekEMIPTKLPNSLMGRVvvwylqnclanlfvgawEPRpegplpldiPQASPQQVQRCVEILSRAKRPLLVL 302
Cdd:COG0028 163 DVQA-------AEAEEEPAPPELRGY-----------------RPR---------PAPDPEAIEEAAELLAAAKRPVILA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 303 GSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSYG-R 374
Cdd:COG0028 210 GGGARRAGA-AEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALAEADLVLAVGARFDDRVTGNwD 288
|
330
....*....|....*...
gi 1720361023 375 VLNRKSSIIIVNRNRDDL 392
Cdd:COG0028 289 EFAPDAKIIHIDIDPAEI 306
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
68-221 |
1.60e-59 |
|
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: 190.82 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 68 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 147
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720361023 148 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 221
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
66-225 |
7.15e-59 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 189.37 E-value: 7.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 223
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 1720361023 224 VL 225
Cdd:pfam02776 161 VL 162
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
70-374 |
7.53e-39 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 146.67 E-value: 7.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 70 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 149
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 150 VAQSPVLLLGGAASTL---LQkRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVLY 226
Cdd:PRK09259 96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 227 PYFMVEKemiptklpnslmGRVVVWylqnclanlfvgawepRPEGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQA 306
Cdd:PRK09259 175 QTMDADE------------ALTSLV----------------KVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 307 LLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGR 374
Cdd:PRK09259 225 AYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGK 291
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
66-369 |
1.15e-37 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 143.33 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 LYPYFMVEkemIPTKLpnSLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:TIGR00118 163 TTAEIEYP---YPEKV--NLPG------------------YRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361023 305 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFR 369
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDR 281
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
66-368 |
1.49e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 140.66 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 226 YPYFMVEKEMIPTKLPnsLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGSQ 305
Cdd:PRK06276 163 EGELDLEKYPIPAKID--LPG------------------YKPTTFG---------HPLQIKKAAELIAEAERPVILAGGG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361023 306 ALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGavCDF 368
Cdd:PRK06276 214 VII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRF 280
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
64-363 |
6.59e-36 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 138.45 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 64 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 143
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 144 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 223
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 224 VLYPyfmvekemiPTKLPNslmgrvvvwylqnclanlfVGAWEPRPEGPlpldipqASPQQVQRCVEILSRAKRPLLVLG 303
Cdd:PRK08617 165 VVDA---------PVTSKA-------------------IAPLSKPKLGP-------ASPEDINYLAELIKNAKLPVLLLG 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361023 304 SQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL---------LGRNHP---LhirqnrsaaLKKADVVVLAG 363
Cdd:PRK08617 210 MRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvgLFRNQPgdeL---------LKKADLVITIG 276
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
74-343 |
3.55e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 136.11 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQS 153
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 154 PVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVrDIVPTL-RTAIAAAQSGTPGPVFVELPLDVlypyfmve 232
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 233 kemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 309
Cdd:PRK08322 162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRK 210
|
250 260 270
....*....|....*....|....*....|....
gi 1720361023 310 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL 343
Cdd:PRK08322 211 TA-SKALTEFVDKTGIPFFTTQMGKGVIPETHPL 243
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
66-371 |
2.42e-34 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 134.07 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DV-------LYPyfmvEKEMIPTKLPNslmgrvvvwYLQNclanlfvgaweprpegplpldipqasPQQVQRCVEILSRA 295
Cdd:PRK08527 163 DVtatlgefEYP----KEISLKTYKPT---------YKGN--------------------------SRQIKKAAEAIKEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 296 KRPLLVLGSQALLpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDF 368
Cdd:PRK08527 204 KKPLFYLGGGAIL-SNASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDD 282
|
...
gi 1720361023 369 RLS 371
Cdd:PRK08527 283 RVT 285
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
67-363 |
5.89e-34 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 132.79 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 67 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 146
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 147 NAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 223
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 224 VlypyfMVEKemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG 303
Cdd:PRK07524 165 V-----LAAP------------------------------ADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAG 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361023 304 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRS-----AALKKADVVVLAG 363
Cdd:PRK07524 210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVG 271
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
66-225 |
1.59e-33 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 131.41 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
66-363 |
1.70e-33 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 131.65 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAAST--LLQKRGAL-QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 221
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 222 LDvlypyfmvekemiptklpnsLMGRVVVWylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 301
Cdd:PRK07064 165 ID--------------------IQAAEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361023 302 LGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAA----LKKADVVVLAG 363
Cdd:PRK07064 210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVG 272
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
66-363 |
3.36e-32 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 127.82 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 143
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 144 AVKNAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVEL 220
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 221 PLDVLYpyfMVEKEMIPTKLpnslmgrvvvwylqnclanlfvgawepRPEGPLPLDipqasPQQVQRCVEILSRAKRPLL 300
Cdd:PRK08266 166 PWDVFG---QRAPVAAAPPL---------------------------RPAPPPAPD-----PDAIAAAAALIAAAKNPMI 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361023 301 VLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirQNRSAA---LKKADVVVLAG 363
Cdd:PRK08266 211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG--LNFAAAyelWPQTDVVIGIG 271
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
66-370 |
2.11e-31 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 126.07 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DvlypyfmVEKEMIPTKLPNSLmgrvvvwylqnclanlfvgawEPRPEGPlpldIPQASPQQVQRCVEILSRAKRPLLVL 302
Cdd:PRK06965 181 D-------VSKTPCEYEYPKSV---------------------EMRSYNP----VTKGHSGQIRKAVSLLLSAKRPYIYT 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361023 303 GSQALLpPTPANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRL 370
Cdd:PRK06965 229 GGGVIL-ANASRELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFDDRV 302
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
66-371 |
1.86e-29 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 120.26 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 226 -------YPyfmvEKEMIPtklpnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 298
Cdd:PRK06048 170 taeidfdYP----DKVELR--------------------------GYKPTYKG---------NPQQIKRAAELIMKAERP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 299 LL-----VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVC 366
Cdd:PRK06048 211 IIyagggVISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARF 284
|
....*
gi 1720361023 367 DFRLS 371
Cdd:PRK06048 285 DDRVT 289
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
64-371 |
7.75e-29 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 118.05 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 64 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:PRK08199 8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DVLYpyfmvekemiptklpnslmGRVVVwylqnclanlfvgaweprPEGPlPLDIPQASP--QQVQRCVEILSRAKRPLL 300
Cdd:PRK08199 168 DVLS-------------------ETAEV------------------PDAP-PYRRVAAAPgaADLARLAELLARAERPLV 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 301 VLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRS--AALKKADVVVLAGAvcdfRLS 371
Cdd:PRK08199 210 ILGG-SGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaARIREADLVLAVGT----RLG 282
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
68-372 |
1.23e-28 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 117.79 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 68 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 147
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 148 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLDvlYP 227
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 228 YFMVEKEmIPTklpnslmgrvvvwylqnclanlfvgaweprpegPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG---- 303
Cdd:PRK07525 167 YGVIDVE-IPQ---------------------------------PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvv 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361023 304 -SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH---IRQNRSAA----LKKADVVVLAGAvcdfRLSY 372
Cdd:PRK07525 213 lSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNP 279
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
55-371 |
1.63e-28 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 117.23 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 55 MHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVT 133
Cdd:PRK07282 1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 134 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTP 213
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 214 GPVFVELPLDVlypyfmVEKEmipTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPLDIPQASPQ--QVQRCVEI 291
Cdd:PRK07282 161 GPVVIDLPKDV------SALE---TDFIYD-------------------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 292 LSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGA 364
Cdd:PRK07282 207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
|
....*..
gi 1720361023 365 VCDFRLS 371
Cdd:PRK07282 286 RFDDRLT 292
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
66-369 |
1.78e-28 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 117.23 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:PRK08979 166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361023 305 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGAVCDFR 369
Cdd:PRK08979 216 GAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDR 286
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
66-369 |
1.99e-28 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 116.90 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 226 ypyfmvekemiptklpnslmgrvvvwylqncLANLFVGAWEPRPEGPlpldiPQASPQQVQRCVEILSRAKRPLLVLG-- 303
Cdd:PRK08978 163 -------------------------------LAEGELEPHLTTVENE-----PAFPAAELEQARALLAQAKKPVLYVGgg 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 304 ---SQAllppTPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFR 369
Cdd:PRK08978 207 vgmAGA----VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDR 276
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
66-371 |
3.96e-28 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 116.22 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 226 ---YPYFMVEKEMIPTKLPnslmgrvvvwylqnclanlfvgawEPRPEgplpldipqasPQQVQRCVEILSRAKRPLLVL 302
Cdd:PRK06725 177 nekVTSFYNEVVEIPGYKP------------------------EPRPD-----------SMKLREVAKAISKAKRPLLYI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361023 303 GSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLS 371
Cdd:PRK06725 222 GG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT 296
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
68-343 |
6.32e-28 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 115.85 E-value: 6.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 68 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 145
Cdd:PRK11269 8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 225
Cdd:PRK11269 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 226 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 305
Cdd:PRK11269 168 ----VAEIE------------------------------FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG- 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720361023 306 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL 343
Cdd:PRK11269 213 GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPL 250
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
66-369 |
2.84e-27 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 113.79 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:PRK07979 166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361023 305 QALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFR 369
Cdd:PRK07979 216 GAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMTMHNADVIFAVGVRFDDR 286
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
66-227 |
5.47e-27 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 113.09 E-value: 5.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGgIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
...
gi 1720361023 225 LYP 227
Cdd:PRK06882 166 VNP 168
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
66-373 |
1.71e-26 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 111.37 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DVLYPYFMVEKEMiPTKlpnslmgrvvvwylqnclanLFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL-- 300
Cdd:PRK06466 164 DMTNPAEKFEYEY-PKK--------------------VKLRSYSPAVRG---------HSGQIRKAVEMLLAAKRPVIys 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 301 ----VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSY 372
Cdd:PRK06466 214 gggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAMHHADVILAVGARFDDRVTN 289
|
.
gi 1720361023 373 G 373
Cdd:PRK06466 290 G 290
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
66-386 |
3.92e-26 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 110.31 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 141
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 142 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 221
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 222 LDVLYpyfmvEKemiptklpnslMGRVVvwylqnclanlfvgaWEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLL 300
Cdd:PRK06456 164 RDIFY-----EK-----------MEEIK---------------WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPII 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 301 VLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFR--LS 371
Cdd:PRK06456 213 LVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTS 291
|
330
....*....|....*
gi 1720361023 372 YGRVLNRKSSIIIVN 386
Cdd:PRK06456 292 YDEMVETRKKFIMVN 306
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
77-345 |
4.49e-26 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 110.17 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 77 HGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 152
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 153 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV---LYPYF 229
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 230 MVEKEMIPTKLPnslmgrvvvwylqnclanlfvgAWEPrpegplpldIPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 309
Cdd:CHL00099 183 PPEPGNTIIKIL----------------------GCRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720361023 310 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI 345
Cdd:CHL00099 232 DA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLCL 266
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
66-363 |
4.87e-26 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 110.24 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVELP 221
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 222 LDVLypyfmvEKEMIPTKLPNSlmgrvvvwylqnclANLfvGAWeprpegplPLDIPQASPQQVQRCVEILSRAKRPLLV 301
Cdd:PRK06112 170 ADLL------TAAAAAPAAPRS--------------NSL--GHF--------PLDRTVPAPQRLAEAASLLAQAQRPVVV 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361023 302 LG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI------------RQNRSAALKKADVVVLAG 363
Cdd:PRK06112 220 AGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDETHPLSLgvvgslmgprspGRHLRDLVREADVVLLVG 292
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
66-326 |
6.23e-26 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 109.80 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 lypYFMVEKEMIPTKLPnslmgrvvvwylqnclanlFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:PRK09107 173 ---QFATGTYTPPQKAP-------------------VHVSYQPKVKG---------DAEAITEAVELLANAKRPVIYSGG 221
|
250 260
....*....|....*....|...
gi 1720361023 305 QALLPPTPANK-LRAAVETLGVP 326
Cdd:PRK09107 222 GVINSGPEASRlLRELVELTGFP 244
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
56-398 |
1.16e-25 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 109.13 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 56 HKVDKTSIRHGGESVAAVLRAHGVRFVFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTG--TVGVAAVT 133
Cdd:PRK06154 12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 134 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTllqkrgALQAID----QMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQ 209
Cdd:PRK06154 89 YGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 210 SGTPGPVFVELPLDVLYpyfmvekemipTKLPNSlmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV 289
Cdd:PRK06154 163 NGRPGPVVLELPVDVLA-----------EELDEL-----------------------PLDHRPSRRSRPGADPVEVVEAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 290 EILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLGRNHPLHIRQNRSAA-------LKKADVVV 360
Cdd:PRK06154 209 ALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FPEDHPLALGSGGRARpatvahfLREADVLF 285
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720361023 361 LAGavCDF-RLSYGRVLNRKSSIIIVnrNRDDLLLNSDI 398
Cdd:PRK06154 286 GIG--CSLtRSYYGLPMPEGKTIIHS--TLDDADLNKDY 320
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
66-369 |
2.29e-25 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 108.26 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 lypyfmvekemiptklpnslmgrvvvwylQNclANLFVGAWePRPEGPLPldIPQASPQQVQRCVEILSRAKRPLLVLGS 304
Cdd:PRK08155 175 -----------------------------QT--AVIELEAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361023 305 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFR 369
Cdd:PRK08155 221 GVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR 291
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
66-369 |
7.37e-25 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 106.99 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 142
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 143 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 223 DVLypyfmvEKEMiptklpnslmgrvvvwylqnclanLFvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVL 302
Cdd:PRK07789 191 DAL------QAQT------------------------TF--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720361023 303 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDFR 369
Cdd:PRK07789 239 GGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVAALQRSDLLIALGARFDDR 311
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
67-224 |
1.96e-24 |
|
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: 98.39 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 67 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 145
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 146 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRR---VRDIVPT-LRTAIAaaqsgTPGPVFVELP 221
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157
|
...
gi 1720361023 222 LDV 224
Cdd:cd07039 158 GDV 160
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
66-343 |
2.79e-24 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 105.13 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 141
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 142 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 221
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 222 LDV---LYPYFMVEKEMIptKLPnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 298
Cdd:PRK07418 181 KDVgqeEFDYVPVEPGSV--KPP----------------------GYRPTVKG---------NPRQINAALKLIEEAERP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720361023 299 LLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL 343
Cdd:PRK07418 228 LLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPL 271
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
53-371 |
1.22e-23 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 102.92 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 53 QLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAV 132
Cdd:PRK07710 5 RTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 133 TAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGT 212
Cdd:PRK07710 85 TSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 213 PGPVFVELPLDVLYP--YFMVEKEM-----IPTKLPNSLmgrvvvwylqnclanlfvgaweprpegplpldipqaspqQV 285
Cdd:PRK07710 165 PGPVLIDIPKDMVVEegEFCYDVQMdlpgyQPNYEPNLL---------------------------------------QI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 286 QRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADV 358
Cdd:PRK07710 206 RKLVQAVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgmagmHGTYTANMALYECDL 284
|
330
....*....|...
gi 1720361023 359 VVLAGAVCDFRLS 371
Cdd:PRK07710 285 LINIGARFDDRVT 297
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
74-361 |
2.55e-20 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 93.14 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 147
Cdd:PRK08327 17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 148 AQVAQSPVLLLGGAASTLlqKRGAL-----------QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPV 216
Cdd:PRK08327 97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 217 FVELPLDVLypyfmVEKemiptklpnslmgrvvvwylqnclanlfVGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAK 296
Cdd:PRK08327 175 YLTLPREVL-----AEE----------------------------VPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 297 RPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVL 361
Cdd:PRK08327 222 RPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLVLV 285
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
64-326 |
1.15e-19 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 90.95 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 64 RHGGESVAAVLRAHGVRFVFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGL 138
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 139 TNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFV 218
Cdd:PLN02470 89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 219 ELPLDVlYPYFMVEKEMIPTKLPNslmgrvvvwYLQNClanlfvgawePRPegplpldiPQASpqQVQRCVEILSRAKRP 298
Cdd:PLN02470 169 DIPKDI-QQQLAVPNWNQPMKLPG---------YLSRL----------PKP--------PEKS--QLEQIVRLISESKRP 218
|
250 260
....*....|....*....|....*...
gi 1720361023 299 LLVLGSQALlppTPANKLRAAVETLGVP 326
Cdd:PLN02470 219 VVYVGGGCL---NSSEELREFVELTGIP 243
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
66-364 |
1.92e-18 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 87.20 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 143
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 144 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLD 223
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 224 vlYPYFMVEKEMiptklpnslmgrvvvWYLQNCLANLFVgaweprpegplpldIPQASPQQVQRCVEILSRAKRPLLVLG 303
Cdd:TIGR02720 160 --FGWQEIPDND---------------YYASSVSYQTPL--------------LPAPDVEAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 304 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-RQNRSA------ALKKADVVVLAGA 364
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLgSAYRVAqkpaneALFQADLVLFVGN 273
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
70-221 |
7.02e-18 |
|
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: 80.08 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 70 VAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNA 148
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361023 149 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELP 221
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
74-365 |
1.61e-15 |
|
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: 78.28 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 152
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLdAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 153 SPVLLLGGAASTLLQKRGAL--------QAIDQMSLFRPLCkfCASVR-----------RVrdivptLRTAIAAAQsgtp 213
Cdd:COG3961 94 VPVVHIVGAPGTRAQRRGPLlhhtlgdgDFDHFLRMFEEVT--VAQAVltpenaaaeidRV------LAAALREKR---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 214 gPVFVELPLDVlypyfmVEKEMiptklpnslmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV---- 289
Cdd:COG3961 162 -PVYIELPRDV------ADAPI-------------------------------EPPEAPLPLPPPASDPAALAAAVaaaa 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 290 EILSRAKRPLLVLGSQAL---LpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI--------RQNRSAALKKADV 358
Cdd:COG3961 204 ERLAKAKRPVILAGVEVHrfgL----QEELLALAEKTGIPVATTLLGKSVLDESHPQFIgtyagaasSPEVREYVENADC 279
|
....*..
gi 1720361023 359 VVLAGAV 365
Cdd:COG3961 280 VLCLGVV 286
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
68-392 |
5.07e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 76.79 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 68 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 147
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 148 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLDVLYp 227
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPVDILR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 228 yfmvekemiptklpnslMGRvvvwylqnclanlfvgawEPRPEGPLPLDIPQASPqQVQRCVEILSRAKRPLLVLGSQAL 307
Cdd:PRK06457 164 -----------------KSS------------------EYKGSKNTEVGKVKYSI-DFSRAKELIKESEKPVLLIGGGTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 308 LPPTPANKLraaVETLGVPCF----------------LGGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLS 371
Cdd:PRK06457 208 GLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FP 271
|
330 340
....*....|....*....|.
gi 1720361023 372 YGRVLNRKSSIIIVNRNRDDL 392
Cdd:PRK06457 272 YVNFLNKSAKVIQVDIDNSNI 292
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
285-392 |
2.95e-14 |
|
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: 69.51 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 285 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 357
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720361023 358 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDL 392
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEI 116
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
74-221 |
2.74e-12 |
|
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: 64.44 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 152
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 153 SPVLLLGGAASTLLQKRGA-----LQAID---QMSLFRPLCkfCASVRRVRDIVPT------LRTAIAAAQsgtpgPVFV 218
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLllhhtLGDGDfdvFLKMFEEIT--CAAARLTDPENAAeeidrvLRTALRESR-----PVYI 158
|
...
gi 1720361023 219 ELP 221
Cdd:cd07038 159 EIP 161
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
66-363 |
6.34e-12 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 67.33 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 143
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 144 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLD 223
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 224 VLypyfmVEKEMIPTKLPNSLMgrvvvwylqnclanlfvgaweprpegplPLDIPQASPQQVQRCVEILSRAKRPLLVLG 303
Cdd:PRK08611 165 LP-----AQKIKDTTNKTVDTF----------------------------RPTVPSPKPKDIKKAAKLINKAKKPVILAG 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361023 304 SQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRSA--ALKKADVVVLAG 363
Cdd:PRK08611 212 LGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigTKPAyeAMQEADLLIMVG 275
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
74-224 |
1.72e-10 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 62.62 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVA 151
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 152 QSPVLLLGGAastllQKRGAL-----QAIDQMSLFR----PLCKFCASVRRVRDIVP-TLRTAIAaaqsgTPGPVFVELP 221
Cdd:PRK08273 93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
|
...
gi 1720361023 222 LDV 224
Cdd:PRK08273 163 NDV 165
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
66-364 |
2.69e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 61.78 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 224
Cdd:PRK07586 83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 225 lypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEP--RPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLLV 301
Cdd:PRK07586 163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 302 LGSQALLPPTPANKLRAAVET---LGVPCFLGGMSRGlLGRNH----PLHIRQNRsAALKKADVVVLAGA 364
Cdd:PRK07586 204 LGGRALRERGLAAAARIAAATgarLLAETFPARMERG-AGRPAverlPYFAEQAL-AQLAGVRHLVLVGA 271
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
68-224 |
1.86e-08 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 56.15 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 68 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 146
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 147 NAQVAQSPVLLLggaASTLLQKR---GALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELPLD 223
Cdd:PRK06546 87 DAHRSGAPVLAI---ASHIPSAQigsGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGD 162
|
.
gi 1720361023 224 V 224
Cdd:PRK06546 163 I 163
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
74-364 |
2.94e-08 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 55.73 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAVARLTGTVGV----AAVTAGPGLTNTVTAVKNaq 149
Cdd:PRK07092 22 LRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGNAMGNLFTAFKN-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 150 vaQSP-VLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDvlypy 228
Cdd:PRK07092 99 --HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYD----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 229 fmvekemiptklpnslmgrvvvwylqnclanlfvgAWEpRPEGPLPL-DIPQA---SPQQVQRCVEILSRAKRPLLVLGs 304
Cdd:PRK07092 172 -----------------------------------DWD-QPAEPLPArTVSSAvrpDPAALARLGDALDAARRPALVVG- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361023 305 qALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLGRNHPLH------IRQNRSAALKKADVVVLAGA 364
Cdd:PRK07092 215 -PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIGA 281
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
66-224 |
3.06e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 52.57 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 66 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 144
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 145 VKNAQVAQSPVL-LLGGAASTLLQKRGALQAiDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVEL 220
Cdd:PRK12474 87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASagaVDSDVARAVQAAQSAPGGIATLIM 162
|
....
gi 1720361023 221 PLDV 224
Cdd:PRK12474 163 PADV 166
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
70-224 |
5.38e-07 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 51.53 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 70 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNA 148
Cdd:PRK09124 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361023 149 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAqSGTPGPVFVELPLDV 224
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDV 163
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
74-222 |
3.50e-05 |
|
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: 43.64 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 74 LRAHGVRFVFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 149
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361023 150 VAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVR------RVRDIVPTLRTAIAAAQSGTPGPVFVELPL 222
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
279-340 |
7.40e-04 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 39.93 E-value: 7.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361023 279 QASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAVETLGVP-CFLGGMSRGLLGRN 340
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
110-304 |
4.47e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 39.45 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 110 EVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCA 189
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361023 190 SVRRVRDIVP------TLRTAIAAAQSGTPGPVFVELPldvlypyFMVEKEMIPTKlpnslmgrvvvWYLqNCLANLfvG 263
Cdd:PLN02980 428 NLPPPTDLIParmvltTLDSAVHWATSSPCGPVHINCP-------FREPLDGSPTN-----------WMS-SCLKGL--D 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720361023 264 AWEPRPEgPLP--LDIPQASPQQVQRC-----VEILSRAKRPLLVLGS 304
Cdd:PLN02980 487 MWMSNAE-PFTkyIQMQSSKADGDTTGqitevLEVIQEAKRGLLLIGA 533
|
|
| |
