NCBI Conserved Domain Search

Conserved domains on [gi|504853778|ref|WP_015040880|]

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acetolactate synthase catalytic subunit [Bordetella bronchiseptica]

Protein Classification

PRK06112 family protein( domain architecture ID 11482053)

PRK06112 family protein

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PRK06112

acetolactate synthase catalytic subunit; Validated

4-581

0e+00

acetolactate synthase catalytic subunit; Validated

Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 961.53 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   4 LPKPLSAPGFTLDGTVAHAIVRALARHGVDTLFGQSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTA 83
Cdd:PRK06112   1 LSKPLSAPGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  84 QNGPAATLLVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR 163
Cdd:PRK06112  81 QNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 164 PGPVALLLPADLLAAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETA 243
Cdd:PRK06112 161 PGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 244 HLPVATTVMGKGAVDERHPLSIGVVGSNMGPNGPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:PRK06112 241 GLPVATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 324 EVGRNYEALRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKHLEDSAAVRLSDASPIRPERIMHELQQQL 403
Cdd:PRK06112 321 EVGRNYEALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 404 DEQSIVVADASYSSIWITHFLTALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARM 483
Cdd:PRK06112 401 TGDTIVVADASYSSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 484 GVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICD 563
Cdd:PRK06112 481 GVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560

                        570
                 ....*....|....*...
gi 504853778 564 ENAFPPITFFTPDAGVQA 581
Cdd:PRK06112 561 PSAFPPISFFEPMDRAAG 578

Name

Accession

Description

Interval

E-value

PRK06112

acetolactate synthase catalytic subunit; Validated

4-581

0e+00

acetolactate synthase catalytic subunit; Validated

Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 961.53 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   4 LPKPLSAPGFTLDGTVAHAIVRALARHGVDTLFGQSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTA 83
Cdd:PRK06112   1 LSKPLSAPGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  84 QNGPAATLLVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR 163
Cdd:PRK06112  81 QNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 164 PGPVALLLPADLLAAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETA 243
Cdd:PRK06112 161 PGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 244 HLPVATTVMGKGAVDERHPLSIGVVGSNMGPNGPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:PRK06112 241 GLPVATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 324 EVGRNYEALRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKHLEDSAAVRLSDASPIRPERIMHELQQQL 403
Cdd:PRK06112 321 EVGRNYEALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 404 DEQSIVVADASYSSIWITHFLTALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARM 483
Cdd:PRK06112 401 TGDTIVVADASYSSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 484 GVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICD 563
Cdd:PRK06112 481 GVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560

                        570
                 ....*....|....*...
gi 504853778 564 ENAFPPITFFTPDAGVQA 581
Cdd:PRK06112 561 PSAFPPISFFEPMDRAAG 578

IlvB

COG0028

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...

18-569

2.07e-155

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: 456.54 E-value: 2.07e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:COG0028    4 TGADALVEALEAEGVETVFGVPGGAILPLydaLRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVA------ 168
Cdd:COG0028   84 GLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVldipkd 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 169 LLLPADLLAAAAPAPALPRNNSLgrfPLDRSVAAPQaiaraaSLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVA 248
Cdd:COG0028  164 VQAAEAEEEPAPPELRGYRPRPA---PDPEAIEEAA------ELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 249 TTVMGKGAVDERHPLSIGVVGSnmgpnGPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRN 328
Cdd:COG0028  235 TTLMGKGAFPEDHPLYLGMLGM-----HGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKN 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 329 YEA-LRLVGDARLTLEALTAALAgqdlaARRQARAGVEQAIALGHEKHLEDsaavRLSDASPIRPERIMHELQQQLDEQS 407
Cdd:COG0028  310 YPVdLPIVGDAKAVLAALLEALE-----PRADDRAAWLARIAAWRAEYLAA----YAADDGPIKPQRVIAALREALPDDA 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 408 IVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKV 487
Cdd:COG0028  381 IVVTDVGQHQMWAARYLRFRRPR-RFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPV 459

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 488 TLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICDENAF 567
Cdd:COG0028  460 KVVVLNNGGLGMVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539


                 ..
gi 504853778 568 PP 569
Cdd:COG0028  540 PP 541

acolac_lg

TIGR00118

acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ...

20-568

7.75e-94

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: 298.18 E-value: 7.75e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   20 AHAIVRALARHGVDTLFG----QSLP--SLLHLAAeqaGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:TIGR00118   4 AEAIIESLKDEGVKTVFGypggAILPiyDALYNDS---GIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   94 APLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPA 173
Cdd:TIGR00118  81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  174 DLLaaaapapalprnNSLGRFPLDRSVA----------APQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETA 243
Cdd:TIGR00118 161 DVT------------TAEIEYPYPEKVNlpgyrptvkgHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  244 HLPVATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:TIGR00118 229 QIPVTTTLMGLGSFPEDHPLSLGMLGMH-----GTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  324 EVGRNYEA-LRLVGDARLTLEALTAALAGQdlaARRQARAGVEQAIALGHEKHLEDSaavrlSDASPIRPERIMHELQQQ 402
Cdd:TIGR00118 304 EIGKNVRVdIPIVGDARNVLEELLKKLFEL---KERKESAWLEQINKWKKEYPLKMD-----YTEEGIKPQQVIEELSRV 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  403 LDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAAR 482
Cdd:TIGR00118 376 TKDEAIVTTDVGQHQMWAAQFYPFRKP-RRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQ 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  483 MGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPV-DHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVI 561
Cdd:TIGR00118 455 YDIPVKILILNNRYLGMVRQWQELFYEERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVV 534


                  ....*....
gi 504853778  562 CD--ENAFP 568
Cdd:TIGR00118 535 VDkpENVLP 543

TPP_PYR_POX_like

cd07035

Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...

21-167

5.73e-45

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: 156.15 E-value: 5.73e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  21 HAIVRALARHGVDTLFGQSLPSLLHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLAE 98
Cdd:cd07035    1 DALVEALKAEGVDHVFGVPGGAILPLldALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504853778  99 AMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:cd07035   81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPV 149

TPP_enzyme_N

pfam02776

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;

19-167

9.50e-45

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;

Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 156.24 E-value: 9.50e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   19 VAHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGHILPLldaLAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504853778   96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQ-ELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:pfam02776  81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPV 153

Name

Accession

Description

Interval

E-value

PRK06112

acetolactate synthase catalytic subunit; Validated

4-581

0e+00

acetolactate synthase catalytic subunit; Validated

Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 961.53 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   4 LPKPLSAPGFTLDGTVAHAIVRALARHGVDTLFGQSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTA 83
Cdd:PRK06112   1 LSKPLSAPGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  84 QNGPAATLLVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR 163
Cdd:PRK06112  81 QNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 164 PGPVALLLPADLLAAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETA 243
Cdd:PRK06112 161 PGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 244 HLPVATTVMGKGAVDERHPLSIGVVGSNMGPNGPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:PRK06112 241 GLPVATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 324 EVGRNYEALRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKHLEDSAAVRLSDASPIRPERIMHELQQQL 403
Cdd:PRK06112 321 EVGRNYEALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 404 DEQSIVVADASYSSIWITHFLTALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARM 483
Cdd:PRK06112 401 TGDTIVVADASYSSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 484 GVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICD 563
Cdd:PRK06112 481 GVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560

                        570
                 ....*....|....*...
gi 504853778 564 ENAFPPITFFTPDAGVQA 581
Cdd:PRK06112 561 PSAFPPISFFEPMDRAAG 578

IlvB

COG0028

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...

18-569

2.07e-155

Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 456.54 E-value: 2.07e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:COG0028    4 TGADALVEALEAEGVETVFGVPGGAILPLydaLRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVA------ 168
Cdd:COG0028   84 GLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVldipkd 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 169 LLLPADLLAAAAPAPALPRNNSLgrfPLDRSVAAPQaiaraaSLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVA 248
Cdd:COG0028  164 VQAAEAEEEPAPPELRGYRPRPA---PDPEAIEEAA------ELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 249 TTVMGKGAVDERHPLSIGVVGSnmgpnGPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRN 328
Cdd:COG0028  235 TTLMGKGAFPEDHPLYLGMLGM-----HGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKN 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 329 YEA-LRLVGDARLTLEALTAALAgqdlaARRQARAGVEQAIALGHEKHLEDsaavRLSDASPIRPERIMHELQQQLDEQS 407
Cdd:COG0028  310 YPVdLPIVGDAKAVLAALLEALE-----PRADDRAAWLARIAAWRAEYLAA----YAADDGPIKPQRVIAALREALPDDA 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 408 IVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKV 487
Cdd:COG0028  381 IVVTDVGQHQMWAARYLRFRRPR-RFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPV 459

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 488 TLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICDENAF 567
Cdd:COG0028  460 KVVVLNNGGLGMVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539


                 ..
gi 504853778 568 PP 569
Cdd:COG0028  540 PP 541

acolac_lg

TIGR00118

acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ...

20-568

7.75e-94

Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 298.18 E-value: 7.75e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   20 AHAIVRALARHGVDTLFG----QSLP--SLLHLAAeqaGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:TIGR00118   4 AEAIIESLKDEGVKTVFGypggAILPiyDALYNDS---GIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   94 APLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPA 173
Cdd:TIGR00118  81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  174 DLLaaaapapalprnNSLGRFPLDRSVA----------APQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETA 243
Cdd:TIGR00118 161 DVT------------TAEIEYPYPEKVNlpgyrptvkgHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  244 HLPVATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:TIGR00118 229 QIPVTTTLMGLGSFPEDHPLSLGMLGMH-----GTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  324 EVGRNYEA-LRLVGDARLTLEALTAALAGQdlaARRQARAGVEQAIALGHEKHLEDSaavrlSDASPIRPERIMHELQQQ 402
Cdd:TIGR00118 304 EIGKNVRVdIPIVGDARNVLEELLKKLFEL---KERKESAWLEQINKWKKEYPLKMD-----YTEEGIKPQQVIEELSRV 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  403 LDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAAR 482
Cdd:TIGR00118 376 TKDEAIVTTDVGQHQMWAAQFYPFRKP-RRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQ 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  483 MGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPV-DHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVI 561
Cdd:TIGR00118 455 YDIPVKILILNNRYLGMVRQWQELFYEERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVV 534


                  ....*....
gi 504853778  562 CD--ENAFP 568
Cdd:TIGR00118 535 VDkpENVLP 543

PRK06276

acetolactate synthase large subunit;

20-570

1.03e-88

acetolactate synthase large subunit;

Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 285.88 E-value: 1.03e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFG----QSLPslLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:PRK06276   4 AEAIIKALEAEGVKIIFGypggALLP--FYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVAL---LLP 172
Cdd:PRK06276  82 IATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdlpKDV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 173 ADLLAAAAPAPALPRNNSLGRFPldRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVM 252
Cdd:PRK06276 162 QEGELDLEKYPIPAKIDLPGYKP--TTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 253 GKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA- 331
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMH-----GTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVd 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 332 LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQaialghekhLEDSAAVRLS-DASPIRPERIMHELQQQLDE----- 405
Cdd:PRK06276 315 VPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKK---------LKKESIPRMDfDDKPIKPQRVIKELMEVLREidpsk 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 406 QSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGV 485
Cdd:PRK06276 386 NTIITTDVGQNQMWMAHFFKTSAP-RSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDI 464

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 486 KVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPV-DHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICDE 564
Cdd:PRK06276 465 PVVICIFDNRTLGMVYQWQNLYYGKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDP 544


                 ....*.
gi 504853778 565 NAFPPI 570
Cdd:PRK06276 545 AEALPM 550

PRK08199

thiamine pyrophosphate protein; Validated

18-537

5.57e-80

thiamine pyrophosphate protein; Validated

Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 261.73 E-value: 5.57e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLF---GQSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK08199   9 TGGQILVDALRANGVERVFcvpGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV------- 167
Cdd:PRK08199  89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVvlalped 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 168 --ALLLPADLLAAAAPAPALPRNNSLGRFpldrsvaapqaiaraASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHL 245
Cdd:PRK08199 169 vlSETAEVPDAPPYRRVAAAPGAADLARL---------------AELLARAERPLVILGGSGWTEAAVADLRAFAERWGL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 246 PVATTVMGKGAVDERHPLSIGVVGsnMGPNgPTRFQRrlIAEADVVLLVGNRTNQNGTDSWQL----YPKnAQYIHIDVD 321
Cdd:PRK08199 234 PVACAFRRQDLFDNRHPNYAGDLG--LGIN-PALAAR--IREADLVLAVGTRLGEVTTQGYTLldipVPR-QTLVHVHPD 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 322 GLEVGRNYEA-LRLVGDARltleALTAALAGQDLAARRQARAGVEQAialgHEKHLEDSAAVRLsdASPIRPERIMHELQ 400
Cdd:PRK08199 308 AEELGRVYRPdLAIVADPA----AFAAALAALEPPASPAWAEWTAAA----HADYLAWSAPLPG--PGAVQLGEVMAWLR 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 401 QQLDEQSIVVADASYSSIWITHFltalrpgMRFLTPRGLAG-----LGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWS 475
Cdd:PRK08199 378 ERLPADAIITNGAGNYATWLHRF-------FRFRRYRTQLAptsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQ 450

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504853778 476 ELETAARMGVKVTLIVINNGILG-FQKHAENvKFGAHTSAVAFAPVDHTAIARACGCTGIRVE 537
Cdd:PRK08199 451 ELATAVQYGLPIIVIVVNNGMYGtIRMHQER-EYPGRVSGTDLTNPDFAALARAYGGHGETVE 512

PRK06048

acetolactate synthase large subunit;

18-568

3.11e-79

acetolactate synthase large subunit;

Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 260.09 E-value: 3.11e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHLAAE--QAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:PRK06048   9 TGARAIIKCLEKEGVEVIFGYPGGAIIPVYDElyDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADL 175
Cdd:PRK06048  89 IATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 176 LAAAAPAPALPRNNSLGRFPLDRSvaAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKG 255
Cdd:PRK06048 169 TTAEIDFDYPDKVELRGYKPTYKG--NPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGIG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 256 AVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-LRL 334
Cdd:PRK06048 247 AIPTEHPLSLGMLGMH-----GTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVdVPI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 335 VGDARLTLEALTAALAGQDLAARRQARAGVEQAIALgHEKHLEDSaavrlsdaspIRPERIMHELqQQLDEQSIVVADAS 414
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQWKKEYPL-KYKEREDV----------IKPQYVIEQI-YELCPDAIIVTEVG 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 415 YSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVINN 494
Cdd:PRK06048 390 QHQMWAAQYFKYKYP-RTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNN 468

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504853778 495 GILGFQKHAENVKFGAHTSAVAFAP-VDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVI--CDENAFP 568
Cdd:PRK06048 469 GYLGMVRQWQELFYDKRYSHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIveCEENVSP 545

PRK06154

thiamine pyrophosphate-requiring protein;

19-539

1.00e-73

thiamine pyrophosphate-requiring protein;

Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 245.49 E-value: 1.00e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  19 VAHAIVRALARHGVDTLFGQSLPSLLHlAAEQAGMRQVAYRTENAGGYMADAYARVSG--KPAIVTAQNGPAATLLVAPL 96
Cdd:PRK06154  22 VAEAVAEILKEEGVELLFGFPVNELFD-AAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFGGV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTD-RNAFQELDHialFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADL 175
Cdd:PRK06154 101 AQAYGDSVPVLFLPTGYPRGSTDvAPNFESLRN---YRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVDV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 176 LaaaapapalprNNSLGRFPLD-------RSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVA 248
Cdd:PRK06154 178 L-----------AEELDELPLDhrpsrrsRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVM 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 249 TTVMGKGAVDERHPLSIGvVGSNMGPNGPTRFqrrlIAEADVVLLVG---NRTNQNGTdswqlYPKNAQYIHIDVDGLEV 325
Cdd:PRK06154 247 TTLNGKSAFPEDHPLALG-SGGRARPATVAHF----LREADVLFGIGcslTRSYYGLP-----MPEGKTIIHSTLDDADL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 326 GRNYE-ALRLVGDARLTLEALTAALaGQDLAARRQARAGVEQAIALGHEKHLEDSAAVRLSDASPIRPERIMHELQQQLD 404
Cdd:PRK06154 317 NKDYPiDHGLVGDAALVLKQMIEEL-RRRVGPDRGRAQQVAAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVD 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 405 -EQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARM 483
Cdd:PRK06154 396 iKTVIITHDAGSPRDQLSPFYVASRPG-SYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRE 474

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504853778 484 GVKVTLIVINNGILGfqKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK06154 475 RIPILTILLNNFSMG--GYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDP 528

sulphoacet_xsc

TIGR03457

sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ...

18-577

2.87e-67

sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]

Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 228.98 E-value: 2.87e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   18 TVAHAIVRALARHGVDTLFG---QSLPSLLHLAAeQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:TIGR03457   3 TPSEAFVEVLVANGVTHAFGimgSAFMDAMDLFP-PAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRpGPValllpad 174
Cdd:TIGR03457  82 AIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPA------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  175 llaaaapAPALPRNNSLGRF--------PLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLP 246
Cdd:TIGR03457 154 -------QLNIPRDYFYGEIdveiprpvRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  247 VATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTN------QNGTDSWqlyPKNAQYIHIDV 320
Cdd:TIGR03457 227 VVNSYLHNDSFPASHPLWVGPLGYQ-----GSKAAMKLISDADVVLALGTRLGpfgtlpQYGIDYW---PKNAKIIQVDA 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  321 DGLEVGRNYE-ALRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKHLED------------SAAVRLSDA 387
Cdd:TIGR03457 299 NAKMIGLVKKvTVGICGDAKAAAAEILQRLAGKAGDANRAERKAKIQAERSAWEQELSEmtherdpfsldmIVEQRQEEG 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  388 SPIRPERIMHELQQQLDEQSIVVAD-ASYSSIWITHFltALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVG 466
Cdd:TIGR03457 379 NWLHPRQVLRELEKAMPEDAIVSTDiGNINSVANSYL--RFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAG 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  467 DGGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAE----NVKF--GAHTSAVAFAPvdhtaIARACGCTGIRVEDPA 540
Cdd:TIGR03457 457 DGAWGMSMNEIMTAVRHDIPVTAVVFRNRQWGAEKKNQvdfyNNRFvgTELESELSFAG-----IADAMGAKGVVVDKPE 531

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 504853778  541 QLADALAQARAASG---SALIEVICDENAFPPitfFTPDA 577
Cdd:TIGR03457 532 DVGPALKKAIAAQAegkTTVIEIVCTRELGDP---FRRDA 568

PRK07524

5-guanidino-2-oxopentanoate decarboxylase;

18-560

1.86e-66

5-guanidino-2-oxopentanoate decarboxylase;

Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 225.62 E-value: 1.86e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGqsLPSL----LHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:PRK07524   3 TCGEALVRLLEAYGVETVFG--IPGVhtveLYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  94 APLAEAMKVSVP--VIALVQDVNRDQTDRNAFQEL-DHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALL 170
Cdd:PRK07524  81 TAMGQAYADSIPmlVISSVNRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 171 LPADLLAAAAPAPALPRnnslgRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVhiSDASAAMAALQETAHLPVATT 250
Cdd:PRK07524 161 IPLDVLAAPADHLLPAP-----PTRPARPGPAPAALAQAAERLAAARRPLILAGGGA--LAAAAALRALAERLDAPVALT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 251 VMGKGAVDERHPLSIGVVGSnmgpngpTRFQRRLIAEADVVLLVGnrTNQNGTDsWQLY-----PKNAQYIHIDVDGLEV 325
Cdd:PRK07524 234 INAKGLLPAGHPLLLGASQS-------LPAVRALIAEADVVLAVG--TELGETD-YDVYfdggfPLPGELIRIDIDPDQL 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 326 GRNYEA-LRLVGDARLTLEALTAALAGQDLAARrqarAGVEQAIALghekhledSAAVRLSDASPIRPERIMHELQQQLD 404
Cdd:PRK07524 304 ARNYPPaLALVGDARAALEALLARLPGQAAAAD----WGAARVAAL--------RQALRAEWDPLTAAQVALLDTILAAL 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 405 EQSIVVADAS---YSSiwiTHFLTALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAA 481
Cdd:PRK07524 372 PDAIFVGDSTqpvYAG---NLYFDADAPRRWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAV 448

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 482 RMGVKVTLIVINNGILG-FQKHAENVkfGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEV 560
Cdd:PRK07524 449 EADLPLIVLLWNNDGYGeIRRYMVAR--DIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526

PRK07418

acetolactate synthase large subunit;

2-568

3.96e-66

acetolactate synthase large subunit;

Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 226.47 E-value: 3.96e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   2 STLPKPLSAPGFTLDGTVAHAIVRALARHGVDTLFGQS----LP--SLLHLAAEQAGMRQVAYRTENAGGYMADAYARVS 75
Cdd:PRK07418   4 SPPKIGDSTTVTPQRATGAYALMDSLKRHGVKHIFGYPggaiLPiyDELYKAEAEGWLKHILVRHEQGAAHAADGYARAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  76 GKPAIVTAQNGPAATLLVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTK--WVRRvtEASRIEDYVD 153
Cdd:PRK07418  84 GKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKhsYVVR--DPSDMARIVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 154 QAFAAACSGRPGPV---------ALLLPADLLAAAAPAPALPRNNSLGRfplDRSVaapqaiARAASLLAQAQRPVVVAG 224
Cdd:PRK07418 162 EAFHIASSGRPGPVlidipkdvgQEEFDYVPVEPGSVKPPGYRPTVKGN---PRQI------NAALKLIEEAERPLLYVG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 225 GGVHISDASAAMAALQETAHLPVATTVMGKGAVDERHPLSIGVVGsnMgpNGpTRFQRRLIAEADVVLLVGNRTNQNGTD 304
Cdd:PRK07418 233 GGAISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLG--M--HG-TAYANFAVTECDLLIAVGARFDDRVTG 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 305 SWQLYPKNAQYIHIDVDGLEVGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQarAGVEQAialghEKHLEDSAAVR 383
Cdd:PRK07418 308 KLDEFASRAKVIHIDIDPAEVGKNRRPdVPIVGDVRKVLVKLLERSLEPTTPPRTQ--AWLERI-----NRWKQDYPLVV 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 384 LSDASPIRPERIMHELQQQLDEqSIVVADASYSSIWITHFltaLRPGMR-FLTPRGLAGLGWGFPMAMGAKLANPAAEVY 462
Cdd:PRK07418 381 PPYEGEIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAQF---LRNGPRrWISSAGLGTMGFGMPAAMGVKVALPDEEVI 456

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 463 ALVGDGGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAP--VDHTAIARACGCTGIRVEDPA 540
Cdd:PRK07418 457 CIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQWQESFYGERYSASNMEPgmPDFVKLAEAFGVKGMVISERD 536

                        570       580       590
                 ....*....|....*....|....*....|
gi 504853778 541 QLADALAQARAASGSALIEVIC--DENAFP 568
Cdd:PRK07418 537 QLKDAIAEALAHDGPVLIDVHVrrDENCYP 566

PRK11269

glyoxylate carboligase; Provisional

18-539

4.01e-65

glyoxylate carboligase; Provisional

Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 223.32 E-value: 4.01e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHLAA---EQAGMRQVAYRTENAGGYMADAYARVS-GKPAIVTAQNGPAATLLV 93
Cdd:PRK11269   5 RAVDAAVLVLEKEGVTTAFGVPGAAINPFYSamrKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  94 APLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPValllpa 173
Cdd:PRK11269  85 TGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPV------ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 174 dllaaaapapalprnnsLGRFPLD-------------------RSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASA 234
Cdd:PRK11269 159 -----------------LIDLPFDvqvaeiefdpdtyeplpvyKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASD 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 235 AMAALQETAHLPVATTVMGKGAVDERHPLSIGVVGSNMGpngpTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQ 314
Cdd:PRK11269 222 LLVEFAELTGVPVIPTLMGWGAIPDDHPLMAGMVGLQTS----HRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRK 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 315 YIHIDVDGLEVGRNYEA-LRLVGDARLTLEALTAAL----AGQDLAARRQARAGVEQAIALGHEK-HLedsaavrlsDAS 388
Cdd:PRK11269 298 FVHVDIEPTQIGRVFGPdLGIVSDAKAALELLVEVArewkAAGRLPDRSAWVADCQERKRTLLRKtHF---------DNV 368

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 389 PIRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgmRFLTPRGLAG-LGWGFPMAMGAKLANPAAEVYALVGD 467
Cdd:PRK11269 369 PIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKP--RHWINCGQAGpLGWTIPAALGVRAADPDRNVVALSGD 446

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 468 GGFGHVWSELETAARMGVKVTLIVINNGILGF--------------QKHAENVkfgaHTSAVAFAPVDHTAIARACGCTG 533
Cdd:PRK11269 447 YDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLirqaqrafdmdycvQLAFENI----NSPELNGYGVDHVKVAEGLGCKA 522


                 ....*.
gi 504853778 534 IRVEDP 539
Cdd:PRK11269 523 IRVFKP 528

PRK06725

acetolactate synthase large subunit;

18-578

5.04e-65

acetolactate synthase large subunit;

Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 222.54 E-value: 5.04e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:PRK06725  16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVydALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADL 175
Cdd:PRK06725  96 LADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 176 LAAAAPAPALPRNNSLGRFPldRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKG 255
Cdd:PRK06725 176 QNEKVTSFYNEVVEIPGYKP--EPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 256 AVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-LRL 334
Cdd:PRK06725 254 AYPPGDPLFLGMLGMH-----GTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVeYPV 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 335 VGDARLTLEALTaalagqDLAARRQARAGVEQAIALGHEKHLEDSAavrlsDASPIRPERIMHELQQQLDEQSIVVADAS 414
Cdd:PRK06725 329 VGDVKKALHMLL------HMSIHTQTDEWLQKVKTWKEEYPLSYKQ-----KESELKPQHVINLVSELTNGEAIVTTEVG 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 415 YSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVINN 494
Cdd:PRK06725 398 QHQMWAAHFYKAKNP-RTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINN 476

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 495 GILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICD--ENAFPPItf 572
Cdd:PRK06725 477 KFLGMVRQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEegENVFPMV-- 554


                 ....*.
gi 504853778 573 fTPDAG 578
Cdd:PRK06725 555 -PPNKG 559

PRK07525

sulfoacetaldehyde acetyltransferase; Validated

18-577

6.71e-65

sulfoacetaldehyde acetyltransferase; Validated

Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 222.57 E-value: 6.71e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFG---QSLPSLLHLAAEqAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK07525   7 TPSEAFVETLQAHGITHAFGiigSAFMDASDLFPP-AGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRpGPVALLLPad 174
Cdd:PRK07525  86 AVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIP-- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 175 llaaaapapalpRNNSLGRFP--------LDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLP 246
Cdd:PRK07525 163 ------------RDYFYGVIDveipqpvrLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 247 VATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTN------QNGTDSWqlyPKNAQYIHIDV 320
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYN-----GSKAAMELIAKADVVLALGTRLNpfgtlpQYGIDYW---PKDAKIIQVDI 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 321 DGLEVGRNYE-ALRLVGDARLTLEALTAALAGQDLA-ARRQARAGV--------EQAIA-LGHEK---HLEDSAAVRLSD 386
Cdd:PRK07525 303 NPDRIGLTKKvSVGICGDAKAVARELLARLAERLAGdAGREERKALiaaeksawEQELSsWDHEDddpGTDWNEEARARK 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 387 ASPIRPERIMHELQQQLDEQSIVVAD-ASYSSIWITHFltALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALV 465
Cdd:PRK07525 383 PDYMHPRQALREIQKALPEDAIVSTDiGNNCSIANSYL--RFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFA 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 466 GDGGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAE----NVKF-GAHTSavafAPVDHTAIARACGCTGIRV---E 537
Cdd:PRK07525 461 GDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQvdfyNNRFvGTELD----NNVSYAGIAEAMGAEGVVVdtqE 536

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 504853778 538 DPAQLADALAQARAASGSALIEVICDENAFPPitfFTPDA 577
Cdd:PRK07525 537 ELGPALKRAIDAQNEGKTTVIEIMCNQELGEP---FRRDA 573

PRK08611

pyruvate oxidase; Provisional

18-568

4.37e-63

pyruvate oxidase; Provisional

Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 217.56 E-value: 4.37e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFG---QSLPSLLH-LAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:PRK08611   5 KAGEALVKLLQDWGIDHVYGipgDSIDAVVDaLRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  94 APLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRpGPVALLLPA 173
Cdd:PRK08611  85 NGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 174 DLLAAAAPAPALPRNNSlgrFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHisDASAAMAALQETAHLPVATTVMG 253
Cdd:PRK08611 164 DLPAQKIKDTTNKTVDT---FRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEKAKIPIIHTLPA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 254 KGAVDERHPLSIGvvgsNMGPNGpTRFQRRLIAEADVVLLVGnrTNQNGTDswqLYPKNAQYIHIDVDGLEVGRNYEA-L 332
Cdd:PRK08611 239 KGIIPDDHPYSLG----NLGKIG-TKPAYEAMQEADLLIMVG--TNYPYVD---YLPKKAKAIQIDTDPANIGKRYPVnV 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 333 RLVGDARLTLEALTAALagqdlaARRQARAGVEQAIALGHE--KHLEDSaavRLSDASPIRPERIMHELQQQLDEQSIVV 410
Cdd:PRK08611 309 GLVGDAKKALHQLTENI------KHVEDRRFLEACQENMAKwwKWMEED---ENNASTPIKPERVMAAIQKIADDDAVLS 379

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 411 ADASYSSIWITHFLTaLRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLI 490
Cdd:PRK08611 380 VDVGTVTVWSARYLN-LGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVV 458

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778 491 VINNGILGFQKHAENVKfGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICDENAFP 568
Cdd:PRK08611 459 VLNNQQLAFIKYEQQAA-GELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAP 535

PRK08322

acetolactate synthase large subunit;

23-537

3.22e-62

acetolactate synthase large subunit;

Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 214.31 E-value: 3.22e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  23 IVRALARHGVDTLFGqsLPSL--LHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLAE 98
Cdd:PRK08322   7 FVKCLENEGVEYIFG--IPGEenLDLleALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  99 AMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLLAA 178
Cdd:PRK08322  85 AQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDIAAE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 179 AAPAPALPRNNSlgrfplDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGAVD 258
Cdd:PRK08322 165 ETDGKPLPRSYS------RRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 259 ERHPLSIGVVGsnmgpngptrFQRR-----LIAEADVVLLVGN--------RTNQNGtdswqlypkNAQYIHIDVDGLEV 325
Cdd:PRK08322 239 ETHPLSLGTAG----------LSQGdyvhcAIEHADLIINVGHdviekppfFMNPNG---------DKKVIHINFLPAEV 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 326 GRNY-EALRLVGDARLTLEALTAALAGQDLAARRQARAgVEQAIalghEKHLEDSAAvrlSDASPIRPERIMHELQQQLD 404
Cdd:PRK08322 300 DPVYfPQVEVVGDIANSLWQLKERLADQPHWDFPRFLK-IREAI----EAHLEEGAD---DDRFPMKPQRIVADLRKVMP 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 405 EQSIVVADASYSSIWITHFLTALRPGMrFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMG 484
Cdd:PRK08322 372 DDDIVILDNGAYKIWFARNYRAYEPNT-CLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLG 450

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504853778 485 VKVTLIVINNGILGFQKHAENVKFGAHtSAVAFAPVDHTAIARACGCTGIRVE 537
Cdd:PRK08322 451 LPLVVLILNDNAYGMIRWKQENMGFED-FGLDFGNPDFVKYAESYGAKGYRVE 502

PRK07789

acetolactate synthase 1 catalytic subunit; Validated

18-539

3.60e-62

acetolactate synthase 1 catalytic subunit; Validated

Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 216.00 E-value: 3.60e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGqsLPSLLHLAA-----EQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLL 92
Cdd:PRK07789  32 TGAQAVVRSLEELGVDVVFG--IPGGAILPVydplfDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  93 VAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLP 172
Cdd:PRK07789 110 VTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 173 ADLLAAAAPAPALPRNNSLGRFPLDRsvAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVM 252
Cdd:PRK07789 190 KDALQAQTTFSWPPRMDLPGYRPVTK--PHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLM 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 253 GKGAVDERHPLSIGVVGSNMGPNGPTRFQRrliaeADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA- 331
Cdd:PRK07789 268 ARGAFPDSHPQHLGMPGMHGTVAAVAALQR-----SDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHAd 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 332 LRLVGDARLTLEALTAALAGQ-------DLAARRQARAGVEQAIALGHEkhledsaavRLSDASpIRPERIMHELQQQLD 404
Cdd:PRK07789 343 VPIVGDVKEVIAELIAALRAEhaaggkpDLTAWWAYLDGWRETYPLGYD---------EPSDGS-LAPQYVIERLGEIAG 412

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 405 EQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMG 484
Cdd:PRK07789 413 PDAIYVAGVGQHQMWAAQFIDYEKPR-TWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEG 491

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504853778 485 VKVTLIVINNGILG---------FQKHAENVKFGAHTSAVAfapvDHTAIARACGCTGIRVEDP 539
Cdd:PRK07789 492 IPIKVALINNGNLGmvrqwqtlfYEERYSNTDLHTHSHRIP----DFVKLAEAYGCVGLRCERE 551

PRK08266

hypothetical protein; Provisional

18-560

3.67e-62

hypothetical protein; Provisional

Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 214.10 E-value: 3.67e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGqsLPSL--------LHLAAEQagMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAA 89
Cdd:PRK08266   5 TGGEAIVAGLVAHGVDTVFG--LPGAqlywlfdaLYKAGDR--IRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  90 TLLVAPLAEAMKVSVPVIALVQDVNRDQTD--RNAFQEL-DHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGP 166
Cdd:PRK08266  81 LNAGAALLTAYGCNSPVLCLTGQIPSALIGkgRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 167 VALLLPADLLAAAAPAPALPRNNSLGRFPLDRSvaapqAIARAASLLAQAQRPVVVAGGGVhiSDASAAMAALQETAHLP 246
Cdd:PRK08266 161 VALEMPWDVFGQRAPVAAAPPLRPAPPPAPDPD-----AIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 247 VATTVMGKGAVDERHPLSIGVVGSnmgpngptrfqRRLIAEADVVLLVGNRTNQNgTDSWQLYPKNAQYIHIDVDGLEVG 326
Cdd:PRK08266 234 VVAFRSGRGIVSDRHPLGLNFAAA-----------YELWPQTDVVIGIGSRLELP-TFRWPWRPDGLKVIRIDIDPTEMR 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 327 RNYEALRLVGDARLTLEALTAALAGqdLAARRQARagvEQAIAlghekHLEDSAAVRLSDaspIRPER-IMHELQQQLDE 405
Cdd:PRK08266 302 RLKPDVAIVADAKAGTAALLDALSK--AGSKRPSR---RAELR-----ELKAAARQRIQA---VQPQAsYLRAIREALPD 368

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 406 QSIVVADAS---YSSiWITHFLTALRpgmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAAR 482
Cdd:PRK08266 369 DGIFVDELSqvgFAS-WFAFPVYAPR---TFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQ 444

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778 483 MGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEV 560
Cdd:PRK08266 445 HNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEV 522

PRK07282

acetolactate synthase large subunit;

23-539

3.38e-61

acetolactate synthase large subunit;

Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 212.37 E-value: 3.38e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  23 IVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLAEA 99
Cdd:PRK07282  16 VLETLRDLGVDTIFGYPGGAVLPLydaIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 100 MKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLLAAA 179
Cdd:PRK07282  96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDVSALE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 180 APAPALPRNNSLGRFPLDRSvaAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGAVDE 259
Cdd:PRK07282 176 TDFIYDPEVNLPSYQPTLEP--NDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIAT 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 260 RHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-L 332
Cdd:PRK07282 254 SHPLFLGMGGmhgsyaANIA-----------MTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTdI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 333 RLVGDARLTLEALTAAlagqdlaarRQARAGVEQAIalghEKHLEDSAAVRLSDASP--IRPERIMHELQQQLDEQSIVV 410
Cdd:PRK07282 323 PVVGDAKKALQMLLAE---------PTVHNNTEKWI----EKVTKDKNRVRSYDKKErvVQPQAVIERIGELTNGDAIVV 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 411 ADASYSSIWITHFLtALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLI 490
Cdd:PRK07282 390 TDVGQHQMWAAQYY-PYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVV 468

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 504853778 491 VINNGILGFQKHAENVKFGAHTSAVAF-APVDHTAIARACGCTGIRVEDP 539
Cdd:PRK07282 469 MLNNHSLGMVRQWQESFYEGRTSESVFdTLPDFQLMAQAYGIKHYKFDNP 518

PRK08979

acetolactate synthase 3 large subunit;

20-539

5.43e-59

acetolactate synthase 3 large subunit;

Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 206.21 E-value: 5.43e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPL 96
Cdd:PRK08979   7 ASMIVRSLIDEGVKHIFGYPGGSVLDIydaLHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLL 176
Cdd:PRK08979  87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDCL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 177 AAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGA 256
Cdd:PRK08979 167 NPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLMGLGA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 257 VDERHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYE 330
Cdd:PRK08979 247 FPGTHKNSLGMLGmhgryeANMA-----------MHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVR 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 331 A-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKhleDSAAVRLSdASPIRPERIMHELQQQLDEQSIV 409
Cdd:PRK08979 316 VdIPIVGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSR---NCLAYDKS-SERIKPQQVIETLYKLTNGDAYV 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 410 VADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTL 489
Cdd:PRK08979 392 ASDVGQHQMFAALYYPFDKP-RRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKI 470

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504853778 490 IVINNGILGFQKHAENVKF-GAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK08979 471 INLNNRFLGMVKQWQDMIYqGRHSHSYMDSVPDFAKIAEAYGHVGIRISDP 521

PRK06456

acetolactate synthase large subunit;

20-537

3.44e-58

acetolactate synthase large subunit;

Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 204.30 E-value: 3.44e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGqsLPSLLHLA--------AEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATL 91
Cdd:PRK06456   5 ARILVDSLKREGVKVIFG--IPGLSNMQiydafvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  92 LVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLL 171
Cdd:PRK06456  83 LVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 172 PADLLAAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTV 251
Cdd:PRK06456 163 PRDIFYEKMEEIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTF 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 252 MGKGAVDERHPLSIGVvgsnMGPNGptRFQRRLIA-EADVVLLVGNRTNQNGTDSW-QLYPKNAQYIHIDVDGLEVGRNY 329
Cdd:PRK06456 243 PGKTAIPHDHPLYFGP----MGYYG--RAEASMAAlESDAMLVVGARFSDRTFTSYdEMVETRKKFIMVNIDPTDGEKAI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 330 EA-LRLVGDARLTLEALTAALAgqDLAARRQARAGVEQAialgheKHLED--SAAVRLSDASPIRPERIMHELQQQLDEQ 406
Cdd:PRK06456 317 KVdVGIYGNAKIILRELIKAIT--ELGQKRDRSAWLKRV------KEYKEyySQFYYTEENGKLKPWKIMKTIRQALPRD 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 407 SIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVK 486
Cdd:PRK06456 389 AIVTTGVGQHQMWAEVFWEVLEP-RTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIP 467

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504853778 487 VTLIVINNGILGFQKHAENVKFGAHTSAVAFAPV-DHTAIARACGCTGIRVE 537
Cdd:PRK06456 468 VISVIFDNRTLGLVRQVQDLFFGKRIVGVDYGPSpDFVKLAEAFGALGFNVT 519

PRK08155

acetolactate synthase large subunit;

18-568

5.13e-58

acetolactate synthase large subunit;

Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 203.40 E-value: 5.13e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFG----QSLPslLHLAAEQAG-MRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLL 92
Cdd:PRK08155  14 TGAELIVRLLERQGIRIVTGipggAILP--LYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  93 VAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTK---WVRRVTEASRIedyVDQAFAAACSGRPGPVAL 169
Cdd:PRK08155  92 VTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKhnyLVRDIEELPQV---ISDAFRIAQSGRPGPVWI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 170 LLPADLLAAAApapalprnnSLGRFPL--DRSVA---APQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAH 244
Cdd:PRK08155 169 DIPKDVQTAVI---------ELEALPApaEKDAApafDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 245 LPVATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLE 324
Cdd:PRK08155 240 LPTTMTLMALGMLPKAHPLSLGMLGMH-----GARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 325 VGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALgHEKHLEDsaavrlsdasPIRPERIMHELQQQL 403
Cdd:PRK08155 315 LGKIKQPhVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREFPC-PIPKADD----------PLSHYGLINAVAACV 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 404 DEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARM 483
Cdd:PRK08155 384 DDNAIITTDVGQHQMWTAQAYPLNRP-RQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAEN 462

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 484 GVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFA-PVDHTAIARACG---CTGIRVEDPaqlADALAQARAASGSALIE 559
Cdd:PRK08155 463 QLDVKIILMNNEALGLVHQQQSLFYGQRVFAATYPgKINFMQIAAGFGletCDLNNEADP---QAALQEAINRPGPALIH 539

                        570
                 ....*....|.
gi 504853778 560 VI--CDENAFP 568
Cdd:PRK08155 540 VRidAEEKVYP 550

ilvB

CHL00099

acetohydroxyacid synthase large subunit

18-568

1.25e-57

acetohydroxyacid synthase large subunit

Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 203.01 E-value: 1.25e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQS----LPSLLHLAA-EQAGM-RQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATL 91
Cdd:CHL00099  11 TGAFALIDSLVRHGVKHIFGYPggaiLPIYDELYAwEKKGLiKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  92 LVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLL 171
Cdd:CHL00099  91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 172 PADLLAAAAPAPALPRNNSLGRFPLDRSVAAPQAI--ARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVAT 249
Cdd:CHL00099 171 PKDVGLEKFDYYPPEPGNTIIKILGCRPIYKPTIKriEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 250 TVMGKGAVDERHPLSIGVVGsnMgpNGpTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRN- 328
Cdd:CHL00099 251 TLMGKGIFDEDHPLCLGMLG--M--HG-TAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNr 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 329 YEALRLVGDARLTLEALTAALA-GQDLAARRQARAGVEQAIALGHEKHLEDSAavrlsDASPIRPERIMHELqQQLDEQS 407
Cdd:CHL00099 326 IPQVAIVGDVKKVLQELLELLKnSPNLLESEQTQAWRERINRWRKEYPLLIPK-----PSTSLSPQEVINEI-SQLAPDA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 408 IVVADASYSSIWITHFLTALRpgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKV 487
Cdd:CHL00099 400 YFTTDVGQHQMWAAQFLKCKP--RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPI 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 488 TLIVINNGILGFQKHAENVKFG---AHTSAVAFAPvDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIE--VIC 562
Cdd:CHL00099 478 KIIIINNKWQGMVRQWQQAFYGerySHSNMEEGAP-DFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDcqVIE 556


                 ....*.
gi 504853778 563 DENAFP 568
Cdd:CHL00099 557 DENCYP 562

PRK07710

acetolactate synthase large subunit;

20-568

2.80e-57

acetolactate synthase large subunit;

Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 201.53 E-value: 2.80e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLA 97
Cdd:PRK07710  19 AQMLIEALEKEGVEVIFGYPGGAVLPLydALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  98 EAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTK---WVRRVTEASRIedyVDQAFAAACSGRPGPVALLLPAD 174
Cdd:PRK07710  99 DAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKhnyQVRKASDLPRI---IKEAFHIATTGRPGPVLIDIPKD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 175 LLAAAAPAPALPRNNSLGRFPLDRSvaAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGK 254
Cdd:PRK07710 176 MVVEEGEFCYDVQMDLPGYQPNYEP--NLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 255 GAVDERHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRN 328
Cdd:PRK07710 254 GGFPADHPLFLGMAGmhgtytANMA-----------LYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKN 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 329 YE-ALRLVGDARLTLEALTAALAGQ-DLAARRQARAGVEQAIALGHEKhledsaavrlsDASPIRPERIMHELQQQLDEQ 406
Cdd:PRK07710 323 VPtEIPIVADAKQALQVLLQQEGKKeNHHEWLSLLKNWKEKYPLSYKR-----------NSESIKPQKAIEMLYEITKGE 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 407 SIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVK 486
Cdd:PRK07710 392 AIVTTDVGQHQMWAAQYYPFKTPD-KWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLP 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 487 VTLIVINNGILGFQKHAENVKFGAHTSAVAFA--PvDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIE--VIC 562
Cdd:PRK07710 471 VKVVILNNEALGMVRQWQEEFYNQRYSHSLLScqP-DFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDcrVLQ 549


                 ....*.
gi 504853778 563 DENAFP 568
Cdd:PRK07710 550 SEKVMP 555

PRK06466

acetolactate synthase 3 large subunit;

20-539

1.35e-56

acetolactate synthase 3 large subunit;

Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 199.97 E-value: 1.35e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHLAA---EQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPL 96
Cdd:PRK06466   7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDalfKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLl 176
Cdd:PRK06466  87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 177 aaaapapalprNNSLGRFPLD-------RSVAAPQAIAR-----AASLLAQAQRPVVVAGGGVHISDASAAMAALQETAH 244
Cdd:PRK06466 166 -----------TNPAEKFEYEypkkvklRSYSPAVRGHSgqirkAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 245 LPVATTVMGKGAVDERHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHI 318
Cdd:PRK06466 235 LPVTNTLMGLGGFPGTDRQFLGMLGmhgtyeANMA-----------MHHADVILAVGARFDDRVTNGPAKFCPNAKIIHI 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 319 DVDGLEVGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKHleDSAAVRLSDASPIRPERIMH 397
Cdd:PRK06466 304 DIDPASISKTIKAdIPIVGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRH--GLFPYDKGDGGIIKPQQVVE 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 398 ELQQQLDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSEL 477
Cdd:PRK06466 382 TLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPN-RWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQEL 460

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504853778 478 ETAARMGVKVTLIVINNGILGFQKHAENVKFGA-HTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK06466 461 STCLQYGLPVKIINLNNGALGMVRQWQDMQYEGrHSHSYMESLPDFVKLAEAYGHVGIRITDL 523

PRK08527

acetolactate synthase large subunit;

20-568

1.14e-55

acetolactate synthase large subunit;

Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 197.24 E-value: 1.14e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHLAAE---QAGMRQVAYRTENAGGYMADAYARVSGK--PAIVTAqnGPAATLLVA 94
Cdd:PRK08527   6 SQMVCEALKEEGVKVVFGYPGGAILNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKvgVAIVTS--GPGFTNAVT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTK---WVRRVTEASRIedyVDQAFAAACSGRPGPVALLL 171
Cdd:PRK08527  84 GLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKhnyLVKSIEELPRI---LKEAFYIARSGRPGPVHIDI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 172 PADLLAAaapapalprnnsLGRFPLDRSVAAPQ----------AIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQE 241
Cdd:PRK08527 161 PKDVTAT------------LGEFEYPKEISLKTykptykgnsrQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 242 TAHLPVATTVMGKGAVDERHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNAQY 315
Cdd:PRK08527 229 KTGIPAVETLMARGVLRSDDPLLLGMLGmhgsyaANMA-----------MSECDLLISLGARFDDRVTGKLSEFAKHAKI 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 316 IHIDVDGLEVGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALgHEKHLEDSAAVrlsdaspIRPER 394
Cdd:PRK08527 298 IHVDIDPSSISKIVNAdYPIVGDLKNVLKEMLEELKEENPTTYKEWREILKRYNEL-HPLSYEDSDEV-------LKPQW 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 395 IMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVW 474
Cdd:PRK08527 370 VIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYP-RQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNI 448

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 475 SELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHTSA--VAFAPvDHTAIARACGCTGIRVEDPAQLADALAQARAA 552
Cdd:PRK08527 449 QELMTAVEYKIPVINIILNNNFLGMVRQWQTFFYEERYSEtdLSTQP-DFVKLAESFGGIGFRVTTKEEFDKALKEALES 527

                        570
                 ....*....|....*...
gi 504853778 553 SGSALIEVICD--ENAFP 568
Cdd:PRK08527 528 DKVALIDVKIDrfENVLP 545

Gcl

COG3960

Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];

18-539

5.15e-55

Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 196.04 E-value: 5.15e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGqsLPSllhlAA---------EQAGMRQVAYRTENAGGYMADAYAR-VSGKPAIVTAQNGP 87
Cdd:COG3960    4 RAVDAAVAVLEKEGVTTAFG--VPG----AAinpfysamrKHGGIRHVLARHVEGASHMAEGYTRaKAGNIGVCIGTSGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  88 AATLLVAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:COG3960   78 AGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 168 ALLLPADLLAAAAPAPAlprnNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPV 247
Cdd:COG3960  158 LIDLPIDVQMAEIEFDI----DTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 248 ATTVMGKGAVDERHPLSIGVVGSNMGpngpTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGR 327
Cdd:COG3960  234 IPTLMGWGSIPDDHPLMAGMVGLQTS----HRYGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 328 NYEA-LRLVGDARLTLEALTAalagqdlAARRQARAGveqaiALGHEKHLEDSAAVRLS--------DASPIRPERIMHE 398
Cdd:COG3960  310 VFAPdLGIVSDAKAALELFVE-------VARERKAAG-----KLPDRSAWAAECQERKRtmlrkthfDNVPIKPQRVYEE 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 399 LQQQLDEQSIVVADASYSSIWITHFLTALRPgmRFLTPRGLAG-LGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSEL 477
Cdd:COG3960  378 MNKAFGRDTRYVSTIGLSQIAAAQFLHVYKP--RHWINCGQAGpLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEEL 455

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504853778 478 ETAARMGVKVTLIVINNGILGFQKHA--------------ENVkfgaHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:COG3960  456 AVGAQFKLPYIHVVVNNSYLGLIRQAqrgfdmdycvqlafENI----NAPELGGYGVDHVKVAEGLGCKAIRVTDP 527

PRK08617

acetolactate synthase AlsS;

20-539

2.99e-54

acetolactate synthase AlsS;

Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 193.15 E-value: 2.99e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGqsLPS----LLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:PRK08617   8 ADLVVDSLINQGVKYVFG--IPGakidRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPG---------- 165
Cdd:PRK08617  86 LVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGaafvslpqdv 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 166 ---PVALLLPADLLAAaapapalprnnSLGRFPLDrsvaapqAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQET 242
Cdd:PRK08617 166 vdaPVTSKAIAPLSKP-----------KLGPASPE-------DINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLER 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 243 AHLPVATTVMGKGAVDERH-PLSIGVVGsnMGPNGPTRfqrRLIAEADVVLLVGnrtnqngTDSWQLYPKN------AQY 315
Cdd:PRK08617 228 TNLPVVETFQAAGVISRELeDHFFGRVG--LFRNQPGD---ELLKKADLVITIG-------YDPIEYEPRNwnsegdATI 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 316 IHIDVDGLEVGRNYE-ALRLVGDARLTLEALTAALAGQDLAarrqaRAGVEQAIALGHEKHLEDSAAVRLsDASPIRPER 394
Cdd:PRK08617 296 IHIDVLPAEIDNYYQpERELIGDIAATLDLLAEKLDGLSLS-----PQSLEILEELRAQLEELAERPARL-EEGAVHPLR 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 395 IMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVW 474
Cdd:PRK08617 370 IIRALQDIVTDDTTVTVDVGSHYIWMARYFRSYEP-RHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSA 448

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778 475 SELETAARMGVKVTLIVINNG---ILGFQkhaENVKFGaHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK08617 449 MELETAVRLKLNIVHIIWNDGhynMVEFQ---EEMKYG-RSSGVDFGPVDFVKYAESFGAKGLRVTSP 512

PRK07064

thiamine pyrophosphate-binding protein;

18-560

7.10e-53

thiamine pyrophosphate-binding protein;

Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 189.05 E-value: 7.10e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFG----QSLPsLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:PRK07064   4 TVGELIAAFLEQCGVKTAFGvisiHNMP-ILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  94 APLAEAMKVSVPVIALVQDVNRDQTDRNA---FQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALL 170
Cdd:PRK07064  83 GALVEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 171 LPADLLAAAAPAPALprnnsLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGvhisdASAAMAALQETAHL--PVA 248
Cdd:PRK07064 163 IPIDIQAAEIELPDD-----LAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGG-----ARHAGAEVKRLVDLgfGVV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 249 TTVMGKGAVDERHPLSIGVVgsNMGPNGptrfqRRLIAEADVVLLVGNRTNQNGTDSWQL-YPKNaqYIHIDVDGLEVGR 327
Cdd:PRK07064 233 TSTQGRGVVPEDHPASLGAF--NNSAAV-----EALYKTCDLLLVVGSRLRGNETLKYSLaLPRP--LIRVDADAAADGR 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 328 NYEA-LRLVGDARLTLEALTAALAGQ---DLAARRQARAGVEQAIAlGHEKHLEDSAavrlsdaspirpeRIMHELQQQL 403
Cdd:PRK07064 304 GYPNdLFVHGDAARVLARLADRLEGRlsvDPAFAADLRAAREAAVA-DLRKGLGPYA-------------KLVDALRAAL 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 404 DEQSIVVADASYS-SIWITHFLTALRPGMRfLTPRGlAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAAR 482
Cdd:PRK07064 370 PRDGNWVRDVTISnSTWGNRLLPIFEPRAN-VHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQ 447

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778 483 MGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEV 560
Cdd:PRK07064 448 ENANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525

PRK05858

acetolactate synthase;

23-539

9.33e-52

acetolactate synthase;

Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 186.08 E-value: 9.33e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  23 IVRALARHGVDTLFGQSLPSLLHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKP--AIVTAqnGPAATLLVAPLAE 98
Cdd:PRK05858  11 AARRLKAHGVDTMFTLSGGHLFPLydGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPgvAVLTA--GPGVTNGMSAMAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  99 AMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV---ALLLPADL 175
Cdd:PRK05858  89 AQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVfvdFPMDHAFS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 176 LAAAAPAPALPRNNSLGRFPLDRSVAAPQAiaraasLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKG 255
Cdd:PRK05858 169 MADDDGRPGALTELPAGPTPDPDALARAAG------LLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 256 AVDERHPLSIgvvgsnmgpngpTRFQRRLIAEADVVLLVGnrTNQNGTDSWQLYPKNAQYIHI-DVDGLEVGRNYEALRL 334
Cdd:PRK05858 243 VVPADHPLAF------------SRARGKALGEADVVLVVG--VPMDFRLGFGVFGGTAQLVHVdDAPPQRAHHRPVAAGL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 335 VGDARLTLEALTAALAGQDLAAR--RQARAGVEQAIALghekhledSAAVRLSDASPIRPERIMHELQQQLDEQSIVVAD 412
Cdd:PRK05858 309 YGDLSAILSALAGAGGDRTDHQGwiEELRTAETAARAR--------DAAELADDRDPIHPMRVYGELAPLLDRDAIVIGD 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 413 ASYSSIWITHFLTALRPGMrFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVI 492
Cdd:PRK05858 381 GGDFVSYAGRYIDPYRPGC-WLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIG 459

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 504853778 493 NNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK05858 460 NNGIWGLEKHPMEALYGYDVAADLRPGTRYDEVVRALGGHGELVTVP 506

PRK08978

acetolactate synthase 2 catalytic subunit; Reviewed

20-498

4.71e-50

acetolactate synthase 2 catalytic subunit; Reviewed

Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 181.23 E-value: 4.71e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQS----LPslLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:PRK08978   4 AQWVVHALRAQGVDTVFGYPggaiMP--VYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADL 175
Cdd:PRK08978  82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 176 LAAAAPAPALPRNnslgrfPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKG 255
Cdd:PRK08978 162 QLAEGELEPHLTT------VENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 256 AVDERHPLSIGVVGsnMgpNGpTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRnyeaLR-- 333
Cdd:PRK08978 236 AVEADHPYYLGMLG--M--HG-TKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINK----LRqa 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 334 ---LVGDARLTLEALTAALagqDLAARRQaragveqaialgHEKHLEDSAAVRLsDA--SPIRPERIMHELQQQLDEQSI 408
Cdd:PRK08978 307 hvaLQGDLNALLPALQQPL---NIDAWRQ------------HCAQLRAEHAWRY-DHpgEAIYAPALLKQLSDRKPADTV 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 409 VVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVT 488
Cdd:PRK08978 371 VTTDVGQHQMWVAQHMRFTRP-ENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVK 449

                        490
                 ....*....|
gi 504853778 489 LIVINNGILG 498
Cdd:PRK08978 450 IVLLDNQRLG 459

PRK09107

acetolactate synthase 3 catalytic subunit; Validated

18-539

2.00e-49

acetolactate synthase 3 catalytic subunit; Validated

Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 180.67 E-value: 2.00e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHLAAE---QAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK09107  12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEifqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKW---VRRVTEASRIedyVDQAFAAACSGRPGPVALLL 171
Cdd:PRK09107  92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHnwlVKDVNDLARV---IHEAFHVATSGRPGPVVVDI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 172 PADLLAAAAPAPALPRNNSLGRFPlDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHIS--DASAAMAALQETAHLPVAT 249
Cdd:PRK09107 169 PKDVQFATGTYTPPQKAPVHVSYQ-PKVKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITS 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 250 TVMGKGAVDERHPLSIGVVG------SNMGPNGptrfqrrliaeADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGL 323
Cdd:PRK09107 248 TLMGLGAYPASGKNWLGMLGmhgtyeANMAMHD-----------CDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 324 EVGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIAlghEKHLEDSAAVRLSDaSPIRPERIMHELQQQ 402
Cdd:PRK09107 317 SINKNVRVdVPIIGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIA---RWRARNSLAYTPSD-DVIMPQYAIQRLYEL 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 403 -LDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAA 481
Cdd:PRK09107 393 tKGRDTYITTEVGQHQMWAAQFFGFEEPN-RWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAV 471

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504853778 482 RMGVKVTLIVINNGILGFQKHAENVKFGAHTS-AVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK09107 472 QYNLPVKIFILNNQYMGMVRQWQQLLHGNRLShSYTEAMPDFVKLAEAYGAVGIRCEKP 530

PRK06882

acetolactate synthase 3 large subunit;

20-539

4.13e-48

acetolactate synthase 3 large subunit;

Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 176.64 E-value: 4.13e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPL 96
Cdd:PRK06882   7 AEMVVQSLRDEGVEYVFGYPGGSVLDIydaIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLL 176
Cdd:PRK06882  87 ATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDMV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 177 aaaapapalprnNSLGRFPLD-------RSVAAP-----QAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAH 244
Cdd:PRK06882 167 ------------NPANKFTYEypeevslRSYNPTvqghkGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 245 LPVATTVMGKGAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLE 324
Cdd:PRK06882 235 LPVTSSLMGLGAYPSTDKQFLGMLGMH-----GTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 325 VGRNYEA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEK---HLEDSAAVrlsdaspIRPERIMHELQ 400
Cdd:PRK06882 310 ISKNVPAyIPIVGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKkclEFDRTSDV-------IKPQQVVEAIY 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 401 QQLDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETA 480
Cdd:PRK06882 383 RLTNGDAYVASDVGQHQMFAALHYPFDKP-RRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTA 461

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 481 ARMGVKVTLIVINNGILGFQKHAENVKF-GAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK06882 462 KQYDIPVVIVSLNNRFLGMVKQWQDLIYsGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTP 521

PRK07979

acetolactate synthase 3 large subunit;

20-539

2.70e-47

acetolactate synthase 3 large subunit;

Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 174.27 E-value: 2.70e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPL 96
Cdd:PRK07979   7 AEMVVRSLIDQGVKQVFGYPGGAVLDIydaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLL 176
Cdd:PRK07979  87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDIL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 177 AAAAPAPALPRNNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGA 256
Cdd:PRK07979 167 NPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMGLGA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 257 VDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-LRLV 335
Cdd:PRK07979 247 FPATHRQSLGMLGMH-----GTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAdIPIV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 336 GDARLTLEALTAALA----GQDLAARRQARAGVEQAIALGHEKHLEDSAAvrlsdaspIRPERIMHELQQQLDEQSIVVA 411
Cdd:PRK07979 322 GDARQVLEQMLELLSqesaHQPLDEIRDWWQQIEQWRARQCLKYDTHSEK--------IKPQAVIETLWRLTKGDAYVTS 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 412 DASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIV 491
Cdd:PRK07979 394 DVGQHQMFAALYYPFDKP-RRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLN 472

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 504853778 492 INNGILGFQKHAENVKF-GAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK07979 473 LNNRYLGMVKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGIQISHP 521

PLN02470

acetolactate synthase

23-536

5.86e-47

acetolactate synthase

Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 173.38 E-value: 5.86e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  23 IVRALARHGVDTLF----GQSLPslLHLA-AEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLA 97
Cdd:PLN02470  19 LVEALEREGVDTVFaypgGASME--IHQAlTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  98 EAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLLA 177
Cdd:PLN02470  97 DALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQQ 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 178 AAAP---APALPRNNSLGRFPldrSVAAPQAIARAASLLAQAQRPVVVAGGGVhiSDASAAMAALQETAHLPVATTVMGK 254
Cdd:PLN02470 177 QLAVpnwNQPMKLPGYLSRLP---KPPEKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVASTLMGL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 255 GAVDERHPLSIGVVGSNmgpngPTRFQRRLIAEADVVLLVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-LR 333
Cdd:PLN02470 252 GAFPASDELSLQMLGMH-----GTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPhVS 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 334 LVGDARLTLEALTAALAGQ-----DLAARRQARAGVEQAIALGHEKhledsaavrLSDAspIRPERIMHELQQQLDEQSI 408
Cdd:PLN02470 327 VCADVKLALQGLNKLLEERkakrpDFSAWRAELDEQKEKFPLSYPT---------FGDA--IPPQYAIQVLDELTDGNAI 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 409 VVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVT 488
Cdd:PLN02470 396 ISTGVGQHQMWAAQWYKYKEP-RRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVK 474

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504853778 489 LIVINNGILGFQKHAENVKFGA---HT-----SAVAFAPVDHTAIARACGCTGIRV 536
Cdd:PLN02470 475 IMVLNNQHLGMVVQWEDRFYKAnraHTylgdpDAEAEIFPDFLKFAEGCKIPAARV 530

TPP_PYR_POX_like

cd07035

Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...

21-167

5.73e-45

Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 156.15 E-value: 5.73e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  21 HAIVRALARHGVDTLFGQSLPSLLHL--AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPLAE 98
Cdd:cd07035    1 DALVEALKAEGVDHVFGVPGGAILPLldALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504853778  99 AMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:cd07035   81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPV 149

TPP_enzyme_N

pfam02776

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;

19-167

9.50e-45

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;

Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 156.24 E-value: 9.50e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   19 VAHAIVRALARHGVDTLFGQSLPSLLHL---AAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGHILPLldaLAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504853778   96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQ-ELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:pfam02776  81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPV 153

TPP_enzymes

cd00568

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...

394-562

2.65e-44

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: 155.11 E-value: 2.65e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 394 RIMHELQQQLDEQSIVVADASYSSIWITHFLtALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHV 473
Cdd:cd00568    1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYL-PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 474 WSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAAS 553
Cdd:cd00568   80 GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAG 159


                 ....*....
gi 504853778 554 GSALIEVIC 562
Cdd:cd00568  160 GPALIEVKT 168

TPP_enzyme_M

pfam00205

Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ...

212-345

1.91e-40

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: 143.47 E-value: 1.91e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  212 LLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGAVDERHPLSIGVVGSNMgpngpTRFQRRLIAEADVV 291
Cdd:pfam00205   7 LLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHG-----TPAANEALEEADLV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504853778  292 LLVGNRTN-QNGTDSWQLYPKNAQYIHIDVDGLEVGRNYEA-LRLVGDARLTLEAL 345
Cdd:pfam00205  82 LAVGARFDdIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVdVPIVGDAKETLEAL 137

PRK06965

acetolactate synthase 3 catalytic subunit; Validated

20-539

1.18e-39

acetolactate synthase 3 catalytic subunit; Validated

Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 153.03 E-value: 1.18e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHLAAE---QAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAPL 96
Cdd:PRK06965  24 AEILMKALAAEGVEFIWGYPGGAVLYIYDElykQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  97 AEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVALLLPADLL 176
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDVS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 177 AAAAPAPALPRNNSLGRFPLDRSvaAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGA 256
Cdd:PRK06965 184 KTPCEYEYPKSVEMRSYNPVTKG--HSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLGA 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 257 VDERHPLSIGVVG------SNMGpngptrfqrrlIAEADVVLLVGNRTNQNGTDSWQLYPKNA-QYIHIDVDGLEVGRNY 329
Cdd:PRK06965 262 YPASDKKFLGMLGmhgtyeANMA-----------MQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRV 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 330 EA-LRLVGDARLTLEALTAALAGQDLAARRQARAGVEQAIALGHEKhleDSAAVRLSDaSPIRPERIMHELQQQLDEQSI 408
Cdd:PRK06965 331 KVdIPIVGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSR---DCLKYDRES-EIIKPQYVVEKLWELTDGDAF 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 409 VVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVT 488
Cdd:PRK06965 407 VCSDVGQHQMWAAQFYRFNEP-RRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVK 485

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504853778 489 LIVINNGILGFQKHAENVKF-GAHTSAVAFAPVDHTAIARACGCTGIRVEDP 539
Cdd:PRK06965 486 IISLNNRYLGMVRQWQEIEYsKRYSHSYMDALPDFVKLAEAYGHVGMRIEKT 537

TPP_POX

cd02014

Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...

389-568

2.60e-38

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: 139.20 E-value: 2.60e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 389 PIRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTaLRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDG 468
Cdd:cd02014    1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLR-MNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 469 GFGHVWSELETAARMGVKVTLIVINNGILGFQKHaENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQ 548
Cdd:cd02014   80 GFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKW-EQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDE 158

                        170       180
                 ....*....|....*....|
gi 504853778 549 ARAASGSALIEVICDENAFP 568
Cdd:cd02014  159 ALAADGPVVIDVVTDPNEPP 178

PDC1

COG3961

TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...

18-496

4.22e-38

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: 147.61 E-value: 4.22e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGqsLP-----SLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVT--------AQ 84
Cdd:COG3961    6 TVGDYLLDRLAELGIRHIFG--VPgdynlPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTtygvgelsAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  85 NGpaatllvapLAEAMKVSVPVIALV-----QDVNRDQ--------TDRNAFQELdhialFQPVTKWVRRVTEASRIEDy 151
Cdd:COG3961   84 NG---------IAGAYAERVPVVHIVgapgtRAQRRGPllhhtlgdGDFDHFLRM-----FEEVTVAQAVLTPENAAAE- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 152 VDQAFAAACSGR-------PGPVALLLPADLLAAAAPAPALPRNNSLGRFpldrsvaapqaIARAASLLAQAQRPVVVAG 224
Cdd:COG3961  149 IDRVLAAALREKrpvyielPRDVADAPIEPPEAPLPLPPPASDPAALAAA-----------VAAAAERLAKAKRPVILAG 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 225 GGVHISDASAAMAALQETAHLPVATTVMGKGAVDERHPLSIGV-VGSNMGPNGptrfqRRLIAEADVVLLVGNRTNQNGT 303
Cdd:COG3961  218 VEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEV-----REYVENADCVLCLGVVFTDTNT 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 304 DSWQLYPKNAQYIHIDVDGLEVG-RNYEALRLvGDArltLEALTAALAGQDLAARRQARAgveqaialghekhledSAAV 382
Cdd:COG3961  293 GGFTAQLDPERTIDIQPDSVRVGgHIYPGVSL-ADF---LEALAELLKKRSAPLPAPAPP----------------PPPP 352

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 383 RLSDASPIRPERIMHELQQQLDEQSIVVADASYSSIwithFLTALR--PGMRFLTPRGLAGLGWGFPMAMGAKLANPAAE 460
Cdd:COG3961  353 PAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLF----GAADLRlpEGATFIAQPLWGSIGYTLPAALGAALAAPDRR 428

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 504853778 461 VYALVGDGGFGHVWSELETAARMGVKVTLIVINNGI 496
Cdd:COG3961  429 VILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDG 464

TPP_enzyme_C

pfam02775

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;

412-560

4.96e-38

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;

Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 137.33 E-value: 4.96e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  412 DASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIV 491
Cdd:pfam02775   1 DIGCHQMWAAQYYRFRPPR-RYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504853778  492 INNGILGFQKHAENVKFGAHTSAVA---FAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEV 560
Cdd:pfam02775  80 LNNGGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151

PRK06457

pyruvate dehydrogenase; Provisional

18-572

1.06e-37

pyruvate dehydrogenase; Provisional

Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 146.90 E-value: 1.06e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLF---GQSLPSLLHlAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK06457   3 SVAEVIIRVLEDNGIQRIYgipGDSIDPLVD-AIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPgpVALLLPAD 174
Cdd:PRK06457  82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRG--VAHINLPV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 175 LLAAAAPAPALPRNNSLGR--FPLDRSvaapqaiaRAASLLAQAQRPVVVAGGGvhISDASAAMAALQETAHLPVATTVM 252
Cdd:PRK06457 160 DILRKSSEYKGSKNTEVGKvkYSIDFS--------RAKELIKESEKPVLLIGGG--TRGLGKEINRFAEKIGAPIIYTLN 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 253 GKGAVDERHPLSIGVVGSnMGpngpTRFQRRLIAEADVVLLVGNRTNQNgtdswQLYPKNAQYIHIDVDGLEVGRNYEA- 331
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGL-LG----TKPSIEAMDKADLLIMLGTSFPYV-----NFLNKSAKVIQVDIDNSNIGKRLDVd 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 332 LRLVGDARltlEALTAALAGQDLAARRQARAGVEQAIalghekhleDSAAVRLSDAS-PIRPERIMHELQQQLDEQSIVV 410
Cdd:PRK06457 300 LSYPIPVA---EFLNIDIEEKSDKFYEELKGKKEDWL---------DSISKQENSLDkPMKPQRVAYIVSQKCKKDAVIV 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 411 ADASYSSIWITHFLTALRPGMRFLTPrGLAGLGWGFPMAMGAKLA-NPAAEVYALVGDGGFGHVWSELETAARMGVKVTL 489
Cdd:PRK06457 368 TDTGNVTMWTARHFRASGEQTFIFSA-WLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKI 446

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 490 IVINNGILGFQKHAENVkFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSALIEVICD--ENAF 567
Cdd:PRK06457 447 IIYNNSKLGMIKFEQEV-MGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDpnERPM 525


                 ....*.
gi 504853778 568 PP-ITF 572
Cdd:PRK06457 526 PPkLTF 531

PRK08273

thiamine pyrophosphate protein; Provisional

18-570

4.88e-37

thiamine pyrophosphate protein; Provisional

Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 145.44 E-value: 4.88e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQS------LPSLLHLAAEQagMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATL 91
Cdd:PRK08273   4 TVADFILERLREWGVRRVFGYPgdgingLLGALGRADDK--PEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  92 LVAPLAEAMKVSVPVIALVqdvnrDQTDRNAF-----QELDHIALFQPV-TKWVRRVTEASRIEDYVDQAFAAACSGR-- 163
Cdd:PRK08273  82 LLNGLYDAKLDHVPVVAIV-----GQQARAALgghyqQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAERtv 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 164 -----PGPVALLLPADLLAAAAPAPalprnNSLGrFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHisDASAAMAA 238
Cdd:PRK08273 157 tavilPNDVQELEYEPPPHAHGTVH-----SGVG-YTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEVIA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 239 LQETAHLPVATTVMGKGAVDERHPL---SIGVVGsnmgpngpTRFQRRLIAEADVVLLVGNrtnqngTDSW-QLYPK--N 312
Cdd:PRK08273 229 VAERLGAGVAKALLGKAALPDDLPWvtgSIGLLG--------TKPSYELMRECDTLLMVGS------SFPYsEFLPKegQ 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 313 AQYIHIDVDGLEVGRNYEA-LRLVGDARLTLEALTAALAGQDlaaRRQARAGVEQAIALGHEKhLEDSAAVrlsDASPIR 391
Cdd:PRK08273 295 ARGVQIDIDGRMLGLRYPMeVNLVGDAAETLRALLPLLERKK---DRSWRERIEKWVARWWET-LEARAMV---PADPVN 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 392 PERIMHELQQQLDEQSIVVADASYSSIWITHFLTaLRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGF- 470
Cdd:PRK08273 368 PQRVFWELSPRLPDNAILTADSGSCANWYARDLR-MRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMq 446

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 471 --GHvwSELETAARM-----GVKVTLIVINNGILGFQKHAENVKFGA--HTSAVAFAPVDHTAIARACGCTGIRVEDPAQ 541
Cdd:PRK08273 447 mnGM--AELITVAKYwrqwsDPRLIVLVLNNRDLNQVTWEQRVMEGDpkFEASQDLPDVPYARFAELLGLKGIRVDDPEQ 524

                        570       580
                 ....*....|....*....|....*....
gi 504853778 542 LADALAQARAASGSALIEVICDENaFPPI 570
Cdd:PRK08273 525 LGAAWDEALAADRPVVLEVKTDPN-VPPL 552

PRK09124

ubiquinone-dependent pyruvate dehydrogenase;

18-569

4.80e-33

ubiquinone-dependent pyruvate dehydrogenase;

Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 133.57 E-value: 4.80e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFG---QSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK09124   4 TVADYIAKTLEQAGVKRIWGvtgDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR-------PGPV 167
Cdd:PRK09124  84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRgvavvvlPGDV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 168 ALLLPADLLAAAAPapalprnnslgRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVhiSDASAAMAALQETAHLPV 247
Cdd:PRK09124 164 ALKPAPERATPHWY-----------HAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 248 ATTVMGKGAVDERHPLSIGVVGSNMGPNGptrfqRRLIAEADVVLLVGnrtnqngTD--SWQLYPKNAQYIHIDVDGLEV 325
Cdd:PRK09124 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSG-----YHAMMNCDTLLMLG-------TDfpYRQFYPTDAKIIQIDINPGSL 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 326 GRNYE-ALRLVGDARLTLEALTAALAGQD--------LAARRQARAGVeqaialghekhleDSAAVRLSDASPIRPERIM 396
Cdd:PRK09124 299 GRRSPvDLGLVGDVKATLAALLPLLEEKTdrkfldkaLEHYRKARKGL-------------DDLAVPSDGGKPIHPQYLA 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 397 HELQQQLDEQSIVVADASYSSIWITHFLTAlrPGMRfltpRGLAGLGWG-----FPMAMGAKLANPAAEVYALVGDGGFG 471
Cdd:PRK09124 366 RQISEFAADDAIFTCDVGTPTVWAARYLKM--NGKR----RLLGSFNHGsmanaMPQALGAQAAHPGRQVVALSGDGGFS 439

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 472 HVWSELETAARMGVKVTLIVINNGILGF----QKHAENVKFGahtsaVAFAPVDHTAIARACGCTGIRVEDPAQLADALA 547
Cdd:PRK09124 440 MLMGDFLSLVQLKLPVKIVVFNNSVLGFvameMKAGGYLTDG-----TDLHNPDFAAIAEACGITGIRVEKASELDGALQ 514

                        570       580
                 ....*....|....*....|....
gi 504853778 548 QARAASGSALIEVICD--ENAFPP 569
Cdd:PRK09124 515 RAFAHDGPALVDVVTAkqELAMPP 538

PRK08327

thiamine pyrophosphate-requiring protein;

18-563

2.87e-32

thiamine pyrophosphate-requiring protein;

Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 131.28 E-value: 2.87e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLF---GQSLPSLLH--LAAEQAGMRQVAYRT---ENAGGYMADAYARVSGKP----------- 78
Cdd:PRK08327   8 TAAELFLELLKELGVDYIFinsGTDYPPIIEakARARAAGRPLPEFVIcphEIVAISMAHGYALVTGKPqavmvhvdvgt 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  79 -----AIVTAQNGPAATLLVA---PLAEAMKV---SVPvIALVQDVnRDQTdrnafqeldhiALFQPVTKWVRRVTEASR 147
Cdd:PRK08327  88 analgGVHNAARSRIPVLVFAgrsPYTEEGELgsrNTR-IHWTQEM-RDQG-----------GLVREYVKWDYEIRRGDQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 148 IEDYVDQAFAAACSGRPGPVALLLPADLLAAAAPAPALPRnnslGRF-PLDRSVAAPQAIARAASLLAQAQRPVVVAGGG 226
Cdd:PRK08327 155 IGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADA----GRQmAPAPPAPDPEDIARAAEMLAAAERPVIITWRA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 227 VHISDASAAMAALQETAHLPVATTVMGKGAVDERHPLsigvvgsNMGPNgptrfQRRLIAEADVVLLVgnrtnqngtDS- 305
Cdd:PRK08327 231 GRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPL-------HLGPD-----PRADLAEADLVLVV---------DSd 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 306 --W---QLYPK-NAQYIHIDVDGLEVG---RNYEA-LRLVGDARLTLEALTAALAGQ--DLAARRQARAGVEQAIALGHE 373
Cdd:PRK08327 290 vpWipkKIRPDaDARVIQIDVDPLKSRiplWGFPCdLCIQADTSTALDQLEERLKSLasAERRRARRRRAAVRELRIRQE 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 374 KHLEDSAAvRLSDASPIRPERIMHELQQQLDEQSIVVAdaSYSSIWitHFLTALRPGMRFLTPRGlAGLGWGFPMAMGAK 453
Cdd:PRK08327 370 AAKRAEIE-RLKDRGPITPAYLSYCLGEVADEYDAIVT--EYPFVP--RQARLNKPGSYFGDGSA-GGLGWALGAALGAK 443

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 454 LANPAAEVYALVGDGG--FGHVWSELETAARMGVKVTLIVINNGilGFQKHAENVKfGAHTSAVA----------FAP-V 520
Cdd:PRK08327 444 LATPDRLVIATVGDGSfiFGVPEAAHWVAERYGLPVLVVVFNNG--GWLAVKEAVL-EVYPEGYAarkgtfpgtdFDPrP 520

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 504853778 521 DHTAIARACGCTGIRVEDPAQLADA----LAQARAASGSALIEVICD 563
Cdd:PRK08327 521 DFAKIAEAFGGYGERVEDPEELKGAlrraLAAVRKGRRSAVLDVIVD 567

PRK06546

pyruvate dehydrogenase; Provisional

17-571

1.21e-31

pyruvate dehydrogenase; Provisional

Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 129.34 E-value: 1.21e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  17 GTVAHAIVRALARHGVDTLFG---QSLPSLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLV 93
Cdd:PRK06546   3 KTVAEQLVEQLVAAGVKRIYGivgDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  94 APLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR-------PGP 166
Cdd:PRK06546  83 NGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGgvsvvtlPGD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 167 VALLLPADLLAaaapapalprnNSLGRFPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVhiSDASAAMAALQETAHLP 246
Cdd:PRK06546 163 IADEPAPEGFA-----------PSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAP 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 247 VATTVMGKGAVDERHPLSIGVVGSnMGPNGPTRfqrrLIAEADVVLLVGnrtnqngTDswqlYPKN-----AQYIHIDVD 321
Cdd:PRK06546 230 VGHSLRGKEWIQYDNPFDVGMSGL-LGYGAAHE----AMHEADLLILLG-------TD----FPYDqflpdVRTAQVDID 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 322 GLEVGRNYEA-LRLVGDARLTLEALTAalagqdLAARRQARAGVEQAIALgHEKHLEDSAAVRLSDAS---PIRPERIMH 397
Cdd:PRK06546 294 PEHLGRRTRVdLAVHGDVAETIRALLP------LVKEKTDRRFLDRMLKK-HARKLEKVVGAYTRKVEkhtPIHPEYVAS 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 398 ELQQQLDEQSIVVADASYSSIWITHFLTALrpGMRFLTPRGLAG-LGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSE 476
Cdd:PRK06546 367 ILDELAADDAVFTVDTGMCNVWAARYITPN--GRRRVIGSFRHGsMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGE 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 477 LETAARMGVKVTLIVINNGILGFQKhAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARAASGSA 556
Cdd:PRK06546 445 LLTVKLYDLPVKVVVFNNSTLGMVK-LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPA 523

                        570
                 ....*....|....*...
gi 504853778 557 LIEVICDENAF---PPIT 571
Cdd:PRK06546 524 LVDVVTDPNALsipPTIT 541

PRK09259

putative oxalyl-CoA decarboxylase; Validated

16-566

1.25e-30

putative oxalyl-CoA decarboxylase; Validated

Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 126.25 E-value: 1.25e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  16 DGtvAHAIVRALARHGVDTLFGqsLPSL----LHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATL 91
Cdd:PRK09259  11 DG--FHLVIDALKLNGIDTIYG--VVGIpitdLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  92 LVAPLAEAMKVSVPVIALVQDVNRDQTD--RNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPVAL 169
Cdd:PRK09259  87 GLTALANATTNCFPMIMISGSSEREIVDlqQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 170 LLPADLLAAAAPAPALPRnnSLGRF--PLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPV 247
Cdd:PRK09259 167 DLPAKVLAQTMDADEALT--SLVKVvdPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPF 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 248 ATTVMGKGAVDERHPLSIGVVGSnmgpngptrfqrRLIAEADVVLLVGNRTNqngtdsWQL-------YPKNAQYIHIDV 320
Cdd:PRK09259 245 LPMSMAKGLLPDTHPQSAAAARS------------LALANADVVLLVGARLN------WLLshgkgktWGADKKFIQIDI 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 321 DGLEVGRNYE-ALRLVGDARLTLEALTAALAGQDLAARRQARAgveqAIALGHEKHLEDSAAVRLSDASPIRPERIMHEL 399
Cdd:PRK09259 307 EPQEIDSNRPiAAPVVGDIGSVMQALLAGLKQNTFKAPAEWLD----ALAERKEKNAAKMAEKLSTDTQPMNFYNALGAI 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 400 QQQLDE--QSIVVADASYSsiwithfLTALRPGMRFLTPR--------GLAGLGWGFPMAMGAKLANPaaeVYALVGDGG 469
Cdd:PRK09259 383 RDVLKEnpDIYLVNEGANT-------LDLARNIIDMYKPRhrldcgtwGVMGIGMGYAIAAAVETGKP---VVAIEGDSA 452

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 470 FGHVWSELETAARMGVKVTLIVINNGilGFQKHAENVKFGAHTSAV-AFAP-VDHTAIARACGCTGIRVEDPAQLADALA 547
Cdd:PRK09259 453 FGFSGMEVETICRYNLPVTVVIFNNG--GIYRGDDVNLSGAGDPSPtVLVHhARYDKMMEAFGGVGYNVTTPDELRHALT 530

                        570
                 ....*....|....*....
gi 504853778 548 QARAASGSALIEVICDENA 566
Cdd:PRK09259 531 EAIASGKPTLINVVIDPAA 549

PRK07092

benzoylformate decarboxylase; Reviewed

213-563

1.74e-28

benzoylformate decarboxylase; Reviewed

Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 119.29 E-value: 1.74e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 213 LAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVM-GKGAVDERHPLSIGVVgsnmgPNGPTRFQRRLiAEADVV 291
Cdd:PRK07092 203 LDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPEDHPLFAGFL-----PASREKISALL-DGHDLV 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 292 LLVG---NRTNQNGTDSWqlYPKNAQYIHIDVDGLEVGRNYEALRLVGDARLTLEALTAALAgqdlAARRQARAGVEQAi 368
Cdd:PRK07092 277 LVIGapvFTYHVEGPGPH--LPEGAELVQLTDDPGEAAWAPMGDAIVGDIRLALRDLLALLP----PSARPAPPARPMP- 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 369 alghekhledsaAVRLSDASPIRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPGMRFLTPRGlaGLGWGFPM 448
Cdd:PRK07092 350 ------------PPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRPAMQEHLPMRRQGSFYTMASG--GLGYGLPA 415

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 449 AMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAENVkFGA-HTSAVAFAPVDHTAIAR 527
Cdd:PRK07092 416 AVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPV-FGVrDVPGLDLPGLDFVALAR 494

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 504853778 528 ACGCTGIRVEDPAQLADALAQARAASGSALIEVICD 563
Cdd:PRK07092 495 GYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530

TPP_AHAS

cd02015

Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...

390-570

4.28e-28

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: 111.05 E-value: 4.28e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 390 IRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGG 469
Cdd:cd02015    1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPR-SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 470 FGHVWSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAP-VDHTAIARACGCTGIRVEDPAQLADALAQ 548
Cdd:cd02015   80 FQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSnPDFVKLAEAYGIKGLRVEKPEELEAALKE 159

                        170       180
                 ....*....|....*....|....
gi 504853778 549 ARAASGSALIEVICD--ENAFPPI 570
Cdd:cd02015  160 ALASDGPVLLDVLVDpeENVLPMV 183

TPP_BZL_OCoD_HPCL

cd02004

Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...

392-563

1.66e-25

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: 103.00 E-value: 1.66e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 392 PERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFG 471
Cdd:cd02004    1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPR-HRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 472 HVWSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAH-TSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQAR 550
Cdd:cd02004   80 FSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGlPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRAL 159

                        170
                 ....*....|...
gi 504853778 551 AASGSALIEVICD 563
Cdd:cd02004  160 ASGKPALINVIID 172

TPP_BFDC

cd02002

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...

390-561

9.74e-25

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: 101.13 E-value: 9.74e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 390 IRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGlAGLGWGFPMAMGAKLANPAAEVYALVGDGG 469
Cdd:cd02002    1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPG-SYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 470 FGHVWSELETAARMGVKVTLIVINNG---ILgfQKHAENVKFGAHTSAVAFAP------VDHTAIARACGCTGIRVEDPA 540
Cdd:cd02002   79 FMYTIQALWTAARYGLPVTVVILNNRgygAL--RSFLKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPE 156

                        170       180
                 ....*....|....*....|.
gi 504853778 541 QLADALAQARAASGSALIEVI 561
Cdd:cd02002  157 ELDEALREALAEGGPALIEVV 177

TPP_ALS

cd02010

Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...

392-565

1.69e-24

Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.

Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 100.44 E-value: 1.69e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 392 PERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPGmRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFG 471
Cdd:cd02010    1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPN-TCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 472 HVWSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHtSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALAQARA 551
Cdd:cd02010   80 MNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRD-SGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALA 158

                        170
                 ....*....|....*.
gi 504853778 552 ASGSALIEVICD--EN 565
Cdd:cd02010  159 ADGVHVIDCPVDysEN 174

TPP_PYR_POX

cd07039

Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...

18-163

1.52e-22

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: 94.54 E-value: 1.52e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHLAA---EQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:cd07039    1 TVADVIVETLENWGVKRVYGIPGDSINGLMDalrREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGR 163
Cdd:cd07039   81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR 149

TPP_Gcl

cd02006

Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ...

386-539

3.14e-18

Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.

Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 83.10 E-value: 3.14e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 386 DASPIRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgmRFLTPRGLAG-LGWGFPMAMGAKLANPAAEVYAL 464
Cdd:cd02006    4 DDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKP--RHWINCGQAGpLGWTVPAALGVAAADPDRQVVAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 465 VGDGGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAE---------NVKF-GAHTSAVAFAPVDHTAIARACGCTGI 534
Cdd:cd02006   82 SGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafdmdyqvNLAFeNINSSELGGYGVDHVKVAEGLGCKAI 161


                 ....*
gi 504853778 535 RVEDP 539
Cdd:cd02006  162 RVTKP 166

TPP_Xsc_like

cd02013

Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...

388-577

8.07e-18

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: 81.79 E-value: 8.07e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 388 SPIRPERIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGD 467
Cdd:cd02013    2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKP-RSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 468 GGFGHVWSELETAARMGVKVTLIVINNGILGFQKHAENVKFGAHTSAVAFAPVDHTAIARACGCTGIRVEDPAQLADALA 547
Cdd:cd02013   81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 504853778 548 QARAASGSA---LIEVICDENAFPPitfFTPDA 577
Cdd:cd02013  161 KAIAMMAEGkttVIEIVCDQELGDP---FRRDA 190

PRK12474

hypothetical protein; Provisional

18-494

5.29e-15

hypothetical protein; Provisional

Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 77.99 E-value: 5.29e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  18 TVAHAIVRALARHGVDTLFGQSLPSLLHLAA---EQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAQNGPAATLLVA 94
Cdd:PRK12474   6 NGADSVVDTLLNCGVEVCFANPGTSEMHFVAaldRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  95 PLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGpVALLLPAD 174
Cdd:PRK12474  86 NLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGG-IATLIMPA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 175 LLAAAAPAPALPRNNSLGRFPLDR-SVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMG 253
Cdd:PRK12474 165 DVAWNEAAYAAQPLRGIGPAPVAAeTVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCDTFAPRIERG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 254 KGAVD-ERHPLSIGVVGsnmgpngptrfqrRLIAEADVVLLVGNRTNQN-----GTDSWqLYPKNAQYIHI---DVDGLe 324
Cdd:PRK12474 245 AGRVPiERIPYFHEQIT-------------AFLKDVEQLVLVGAKPPVSffaypGKPSW-GAPPGCEIVYLaqpDEDLA- 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 325 vgrnyEALRLVGDA--RLTLEALTAALAGQDLAARRQARAGVEQAIAlghekhledsaavrlsdaspirperimhelqQQ 402
Cdd:PRK12474 310 -----QALQDLADAvdAPAEPAARTPLALPALPKGALNSLGVAQLIA-------------------------------HR 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 403 LDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAgLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAAR 482
Cdd:PRK12474 354 TPDQAIYADEALTSGLFFDMSYDRARP-HTHLPLTGGS-IGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMAR 431

                        490
                 ....*....|..
gi 504853778 483 MGVKVTLIVINN 494
Cdd:PRK12474 432 ENLDVTVVIFAN 443

TPP_PDC_IPDC

cd02005

Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...

389-494

2.08e-14

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: 71.80 E-value: 2.08e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 389 PIRPERIMHELQQQLDEQSIVVADASysSIWITHFLTALRPGMRFLTPRGLAGLGWGFPMAMGAKLANPAAEVYALVGDG 468
Cdd:cd02005    1 PLTQARLWQQVQNFLKPNDILVAETG--TSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDG 78

                         90       100
                 ....*....|....*....|....*.
gi 504853778 469 GFGHVWSELETAARMGVKVTLIVINN 494
Cdd:cd02005   79 SFQMTVQELSTMIRYGLNPIIFLINN 104

TPP_enzyme_PYR

cd06586

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...

22-167

8.60e-13

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: 66.21 E-value: 8.60e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  22 AIVRALARHGVDTLFG----QSLPsLLHLAAEQAGMRQVAYRTENAGGYMADAYARVSGKPAIVTAqNGPAATLLVAPLA 97
Cdd:cd06586    2 AFAEVLTAWGVRHVFGypgdEISS-LLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVT-SGTGLLNAINGLA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  98 EAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGrPGPV 167
Cdd:cd06586   80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPV 148

PLN02573

pyruvate decarboxylase

5-495

1.18e-11

pyruvate decarboxylase

Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 67.42 E-value: 1.18e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778   5 PKPLSAPGFTLDGTVAHAIVRALARHGVDTLFgqSLP-----SLL-HLAAEqAGMRQVAYRTENAGGYMADAYARVSGKP 78
Cdd:PLN02573   4 APKPATPVSSSDATLGRHLARRLVEIGVTDVF--SVPgdfnlTLLdHLIAE-PGLNLIGCCNELNAGYAADGYARARGVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  79 A-IVTAQNGPAATLlvAPLAEAMKVSVPVIALVQDVNRDQ--TDR--------NAF-QELdhiALFQPVTKWVRRVTEAS 146
Cdd:PLN02573  81 AcVVTFTVGGLSVL--NAIAGAYSENLPVICIVGGPNSNDygTNRilhhtiglPDFsQEL---RCFQTVTCYQAVINNLE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 147 RIEDYVDQAFAAA--------------CSGRPGPvalllpADLLAAAAPAPALPRNNSLGrfpLDRSVAAPQaiaraaSL 212
Cdd:PLN02573 156 DAHELIDTAISTAlkeskpvyisvscnLAAIPHP------TFSREPVPFFLTPRLSNKMS---LEAAVEAAA------EF 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 213 LAQAQRPVVVAGGGVHISDASAAMAALQETAHLPVATTVMGKGAVDERHPLSIgvvGSNMGPNGpTRFQRRLIAEADVVL 292
Cdd:PLN02573 221 LNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFI---GTYWGAVS-TPFCAEIVESADAYL 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 293 LVGNRTNQNGTDSWQLYPKNAQYIHIDVDGLEVGrNYEALRLVGDARLtLEALTAALAGQDLAARRQARAGVEQAIALGH 372
Cdd:PLN02573 297 FAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIG-NGPAFGCVLMKDF-LEALAKRVKKNTTAYENYKRIFVPEGEPLKS 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 373 EKHledsaavrlsdaSPIRPERIMHELQQQLDEQSIVVADASYSsiWITHFLTALRPG------MRFltprglAGLGWGF 446
Cdd:PLN02573 375 EPG------------EPLRVNVLFKHIQKMLSGDTAVIAETGDS--WFNCQKLKLPEGcgyefqMQY------GSIGWSV 434

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 504853778 447 PMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVINNG 495
Cdd:PLN02573 435 GATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNG 483

TPP_IolD

cd02003

Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...

442-538

4.49e-11

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: 62.32 E-value: 4.49e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 442 LGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELETAARMGVKVTLIVINN-------------GILGFQKHAENVKF 508
Cdd:cd02003   50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNhgfgcinnlqestGSGSFGTEFRDRDQ 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 504853778 509 GAHTSAVAFAPVDHTAIARACGCTGIRVED 538
Cdd:cd02003  130 ESGQLDGALLPVDFAANARSLGARVEKVKT 159

PRK07586

acetolactate synthase large subunit;

20-560

8.09e-10

acetolactate synthase large subunit;

Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 61.40 E-value: 8.09e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  20 AHAIVRALARHGVDTLFGQSLPSLLHLAA---EQAGMRQVAYRTENAGGYMADAYARVSGKPAivtaqngpaATLL---- 92
Cdd:PRK07586   4 AESLVRTLVDGGVDVCFANPGTSEMHFVAaldRVPGMRCVLGLFEGVATGAADGYARMAGKPA---------ATLLhlgp 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  93 -----VAPLAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDYVDQAFAAACSGRPGPV 167
Cdd:PRK07586  75 glangLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 168 ALLLPADLLAAAAPAPALPRNnslgrfPLDRSVAAPQAIARAASLLAQAQRPVVVAGGGVHISDASAAMAA--------- 238
Cdd:PRK07586 155 TLILPADVAWSEGGPPAPPPP------APAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARiaaatgarl 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 239 LQETAhlpVATTVMGKGAVD-ERHPLSIGVVgsnmgpngptrfqRRLIAEADVVLLVGNRTnqngTDSWQLYPknaqyih 317
Cdd:PRK07586 229 LAETF---PARMERGAGRPAvERLPYFAEQA-------------LAQLAGVRHLVLVGAKA----PVAFFAYP------- 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 318 iDVDGLEVGRNYEALRLVG---DARLTLEALTAALAGQDLAARRQARAgveqaialghekhledsaavRLSDAS-PIRPE 393
Cdd:PRK07586 282 -GKPSRLVPEGCEVHTLAGpgeDAAAALEALADALGAKPAAPPLAAPA--------------------RPPLPTgALTPE 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 394 RIMHELQQQLDEQSIVVADASYSSIWITHFLTALRPgMRFLTPRGLAgLGWGFPMAMGAKLANPAAEVYALVGDGGFGHV 473
Cdd:PRK07586 341 AIAQVIAALLPENAIVVDESITSGRGFFPATAGAAP-HDWLTLTGGA-IGQGLPLATGAAVACPDRKVLALQGDGSAMYT 418

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 474 WSELETAARMGVKVTLIVINNG---ILgfqkHAENVKFGAHTSAVAFA--------PVDHTAIARACGCTGIRVEDPAQL 542
Cdd:PRK07586 419 IQALWTQARENLDVTTVIFANRayaIL----RGELARVGAGNPGPRALdmldlddpDLDWVALAEGMGVPARRVTTAEEF 494

                        570
                 ....*....|....*...
gi 504853778 543 ADALAQARAASGSALIEV 560
Cdd:PRK07586 495 ADALAAALAEPGPHLIEA 512

PRK05778

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated

447-532

2.42e-09

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated

Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 58.74 E-value: 2.42e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 447 PMAMGAKLANPAAEVYALVGDG-----GFGHvwseLETAARMGVKVTLIVINNGILGFQK--HAENVKFGAHTSAVAFA- 518
Cdd:PRK05778  77 AFATGAKLANPDLEVIVVGGDGdlasiGGGH----FIHAGRRNIDITVIVENNGIYGLTKgqASPTTPEGSKTKTAPYGn 152

                         90
                 ....*....|....*..
gi 504853778 519 ---PVDHTAIARACGCT 532
Cdd:PRK05778 153 iepPIDPCALALAAGAT 169

TPP_OGFOR

cd03375

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...

447-498

6.08e-07

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.

Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 50.22 E-value: 6.08e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504853778 447 PMAMGAKLANPAAEVYALVGDG-----GFGHvwseLETAARMGVKVTLIVINNGILG 498
Cdd:cd03375   58 AVATGVKLANPDLTVIVVSGDGdlaaiGGNH----FIHAARRNIDITVIVHNNQIYG 110

TPP_PYR_MenD

cd07037

Pyrimidine (PYR) binding domain of ...

21-167

3.83e-06

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: 47.11 E-value: 3.83e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  21 HAIVRALARHGVDTLF----GQSLPslLHLAAEQAGMRQVAYRT-ENAGGYMADAYARVSGKPAIVTAQNGPAATLLVAP 95
Cdd:cd07037    1 QALVEELKRLGVRDVVispgSRSAP--LALAAAEHPEFRLHVRVdERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778  96 LAEAMKVSVPVIALVQDVNRDQTDRNAFQELDHIALFQPVTKWVRRVTEASRIEDY------VDQAFAAACSGRPGPV 167
Cdd:cd07037   79 VVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLwyllrlANRAVLEALSAPPGPV 156

TPP_PYR_PDC_IPDC_like

cd07038

Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ...

23-165

5.31e-06

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: 46.72 E-value: 5.31e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  23 IVRALARHGVDTLFGQ----SLPsLLHLAAEQAGMRQVAYRTE-NAGgYMADAYARVSGKPAIVTaQNGPAATLLVAPLA 97
Cdd:cd07038    3 LLERLKQLGVKHVFGVpgdyNLP-LLDAIEENPGLRWVGNCNElNAG-YAADGYARVKGLGALVT-TYGVGELSALNGIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778  98 EAMKVSVPVIALV-----QDVNRDQ--------TDRNAFQEldhiaLFQPVTKWVRRVTEASRIEDYVDQAFAAACS-GR 163
Cdd:cd07038   80 GAYAEHVPVVHIVgapstKAQASGLllhhtlgdGDFDVFLK-----MFEEITCAAARLTDPENAAEEIDRVLRTALReSR 154


                 ..
gi 504853778 164 PG 165
Cdd:cd07038  155 PV 156

PorB

COG1013

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...

447-532

7.71e-06

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation

Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 47.83 E-value: 7.71e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 447 PMAMGAKLANPAAEVYALVGDG-----GFGHvwseLETAARMGVKVTLIVINNGILGfqkhaeNVK--------FGAHTS 513
Cdd:COG1013   71 AVATGIKLANPDLTVIVFGGDGdtydiGGNH----LIHAARRNEDITYIVYDNEIYG------NTGgqrspttpLGAKTT 140

                         90       100
                 ....*....|....*....|...
gi 504853778 514 A----VAFAPVDHTAIARACGCT 532
Cdd:COG1013  141 TtpygKPEPPKDPAEIAAAHGAT 163

PRK11866

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional

433-498

2.78e-05

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional

Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 46.29 E-value: 2.78e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504853778 433 FLTPRGLAGL-GWGFPMAMGAKLANPAAEVYALVGDG-GFGHVWSELETAARMGVKVTLIVINNGILG 498
Cdd:PRK11866  51 FLNTYGIHGIhGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYG 118

PRK06163

hypothetical protein; Provisional

439-530

6.81e-05

hypothetical protein; Provisional

Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.05 E-value: 6.81e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 439 LAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSELET-AARMGVKVTLIVINNGILGFQkhaenvkfGAHTSAVAF 517
Cdd:PRK06163  56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQIT--------GGQPTLTSQ 127

                         90
                 ....*....|...
gi 504853778 518 ApVDHTAIARACG 530
Cdd:PRK06163 128 T-VDVVAIARGAG 139

TPP_IOR_alpha

cd02008

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...

422-539

1.23e-04

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.

Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 43.03 E-value: 1.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 422 HFLTALRPGMRFLTprgLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGH-VWSELETAARMGVKVTLIVINNGIL--- 497
Cdd:cd02008   36 YTLGALPPLNAIDT---CTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFHsGILGLINAVYNKANITVVILDNRTTamt 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504853778 498 GFQKHAENVKFGAHTSAVafapVDHTAIARACGCTGIRVEDP 539
Cdd:cd02008  113 GGQPHPGTGKTLTEPTTV----IDIEALVRAIGVKRVVVVDP 150

TPP_PpyrDC

cd03371

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...

402-562

1.14e-03

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.

Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 40.37 E-value: 1.14e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 402 QLDEQSIVVADASYSSIWIthFLTALRPGMR----FLTprgLAGLGWGFPMAMGAKLANPAAEVYALVGDGGFGHVWSEL 477
Cdd:cd03371   11 RAPATAAVVSTTGMTSREL--FELRDRPGGGhaqdFLT---VGSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504853778 478 ETAARMGVK-VTLIVINNGilgfqkhaenvkfgAHTSA-----VAFApVDHTAIARACG-CTGIRVEDPAQLADALAQAR 550
Cdd:cd03371   86 ATIGGLAPAnLIHIVLNNG--------------AHDSVggqptVSFD-VSLPAIAKACGyRAVYEVPSLEELVAALAKAL 150

                        170
                 ....*....|..
gi 504853778 551 AASGSALIEVIC 562
Cdd:cd03371  151 AADGPAFIEVKV 162

TPP_TK

cd02012

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...

442-496

2.83e-03

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.

Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 39.79 E-value: 2.83e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504853778 442 LGWGFP----MAMGAKLANPAAEVYALVGDGGF--GHVWSELETAARMGV-KVTLIVINNGI 496
Cdd:cd02012  107 LGQGLSvavgMALAEKLLGFDYRVYVLLGDGELqeGSVWEAASFAGHYKLdNLIAIVDSNRI 168

PRK11867

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed

447-498

4.19e-03

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed

Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 39.44 E-value: 4.19e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504853778 447 PMAMGAKLANPAAEVYALVGDG-----GFGHvwseLETAARMGVKVTLIVINNGILG 498
Cdd:PRK11867  76 AIATGLKLANPDLTVIVVTGDGdalaiGGNH----FIHALRRNIDITYILFNNQIYG 128

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01