|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
19-591 |
0e+00 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 913.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 19 ARQDLSAYQAANAIADVLKAAGVAQIFGQSCPTALFLAADAIGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAA 98
Cdd:PRK06112 7 APGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 99 ALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVL 178
Cdd:PRK06112 87 TLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 179 LVSQDVLTTACPqaRPVAQDSDEpLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLP 258
Cdd:PRK06112 167 LLPADLLTAAAA--APAAPRSNS-LGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 259 VATTNMGKGAIDETHPLSLGVIGNAMGTRSPAKHFMDYVRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVG 338
Cdd:PRK06112 244 VATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 339 RNYGAMRFAGDAAATLQALGDALQERGQAVAARRMAELAPAFEACRQAHRAELAPYAQSDASPMRPERIMAELRAS-HGD 417
Cdd:PRK06112 324 RNYEALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVlTGD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 418 IIWVADASYSSIWLAQFIPCTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVP 497
Cdd:PRK06112 404 TIVVADASYSSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 498 VTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPSA 577
Cdd:PRK06112 484 VTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDPSA 563
|
570
....*....|....
gi 504854683 578 FPPISAFESQLRPL 591
Cdd:PRK06112 564 FPPISFFEPMDRAA 577
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
28-585 |
6.87e-150 |
|
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: 443.06 E-value: 6.87e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVA 103
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLY-DALrrqsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 104 GFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQD 183
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 184 VlttacpQARPVAQDSDEPLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTN 263
Cdd:COG0028 164 V------QAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 264 MGKGAIDETHPLSLGVIGnaMGTRSPAkhfMDYVRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNYGA 343
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLG--MHGTPAA---NEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 344 -MRFAGDAAATLQALGDALQERGQAVAARRmaelapafEACRQAHRAELAPYAqSDASPMRPERIMAELR-ASHGDIIWV 421
Cdd:COG0028 313 dLPIVGDAKAVLAALLEALEPRADDRAAWL--------ARIAAWRAEYLAAYA-ADDGPIKPQRVIAALReALPDDAIVV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 422 ADASYSSIWLAQFIPCTQAGtRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIV 501
Cdd:COG0028 384 TDVGQHQMWAARYLRFRRPR-RFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 502 VLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPSAFPPI 581
Cdd:COG0028 463 VLNNGGLGMVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPG 542
|
....
gi 504854683 582 SAFE 585
Cdd:COG0028 543 ATLD 546
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
29-581 |
3.08e-83 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 271.63 E-value: 3.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQSCPTALFLAaDAI---GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGF 105
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFY-DALydsDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 106 SEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVl 185
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 186 ttacpqarpvaQDSDEPLGRFPLDRTVPVAG----------RLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLA 255
Cdd:PRK06276 162 -----------QEGELDLEKYPIPAKIDLPGykpttfghplQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 256 GLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKhfmDYVRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSE 335
Cdd:PRK06276 231 KIPVCTTLMGKGAFPEDHPLALGMVG--MHGTKAAN---YSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 336 EVGRNYGA-MRFAGDAAATLQALGDALQERGQAVAARRMAELapafeacrQAHRAELAPYAQSDASPMRPERIMAEL--- 411
Cdd:PRK06276 306 EIGKNVRVdVPIVGDAKNVLRDLLAELMKKEIKNKSEWLERV--------KKLKKESIPRMDFDDKPIKPQRVIKELmev 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 412 ---RASHGDIIWVADASYSSIWLAQFIPcTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAEL 488
Cdd:PRK06276 378 lreIDPSKNTIITTDVGQNQMWMAHFFK-TSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQEL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 489 ETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFG-AIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPF 567
Cdd:PRK06276 457 ATIAEYDIPVVICIFDNRTLGMVYQWQNLYYGKRQSEVHLGeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPY 536
|
570
....*....|....
gi 504854683 568 VIDVKTEPSAFPPI 581
Cdd:PRK06276 537 LLDIIIDPAEALPM 550
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
28-577 |
6.02e-78 |
|
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: 256.96 E-value: 6.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQscPT-ALFLAADAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLV 102
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGY--PGgAILPIYDALyndsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 103 AGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQ 182
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 183 DVLTTACPQarPVAQDSDEPlGRFPldRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATT 262
Cdd:TIGR00118 161 DVTTAEIEY--PYPEKVNLP-GYRP--TVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 263 NMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMDyvrSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNYG 342
Cdd:TIGR00118 236 LMGLGSFPEDHPLSLGMLG--MHGTKTANLAVH---ECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 343 A-MRFAGDAAATLQALGDALQERGQAVAARRMAELapafeacrQAHRAELAPYAQSDASPMRPERIMAEL-RASHGDIIW 420
Cdd:TIGR00118 311 VdIPIVGDARNVLEELLKKLFELKERKESAWLEQI--------NKWKKEYPLKMDYTEEGIKPQQVIEELsRVTKDEAIV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 421 VADASYSSIWLAQFIPcTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTI 500
Cdd:TIGR00118 383 TTDVGQHQMWAAQFYP-FRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKI 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504854683 501 VVLNNGVLGFQINAEESRFGTHTDVCHFGAI-DHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPSA 577
Cdd:TIGR00118 462 LILNNRYLGMVRQWQELFYEERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPE 539
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
28-580 |
5.71e-75 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 249.02 E-value: 5.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIF---GQScptalFLAA-----DAIGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAA 99
Cdd:PRK08199 10 GGQILVDALRANGVERVFcvpGES-----YLAVldalhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 100 LLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLL 179
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 180 VSQDVL--TTACPQARPVAQdsdeplgrfplDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGL 257
Cdd:PRK08199 165 LPEDVLseTAEVPDAPPYRR-----------VAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 258 PVATTNMGKGAIDETHPLSLGVIGNAMgtrSPAkhFMDYVRSADFVLFVGTRTNENGTASWSLF----PEQaQYAQIDID 333
Cdd:PRK08199 234 PVACAFRRQDLFDNRHPNYAGDLGLGI---NPA--LAARIREADLVLAVGTRLGEVTTQGYTLLdipvPRQ-TLVHVHPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 334 SEEVGRNYGA-MRFAGDAAATLQALgDALQERGQAVAARRMAELapafeacRQAHRAELAPYAQSDASPMrpERIMAELR 412
Cdd:PRK08199 308 AEELGRVYRPdLAIVADPAAFAAAL-AALEPPASPAWAEWTAAA-------HADYLAWSAPLPGPGAVQL--GEVMAWLR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 413 ASHG-DIIWVADASYSSIWLAQFIPCTQAGTRFVTPRGiaGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETA 491
Cdd:PRK08199 378 ERLPaDAIITNGAGNYATWLHRFFRFRRYRTQLAPTSG--SMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 492 RRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PRK08199 456 VQYGLPIIVIVVNNGMYGTIRMHQEREYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEI 535
|
....*....
gi 504854683 572 KTEPSAFPP 580
Cdd:PRK08199 536 RIDPEAITP 544
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
28-573 |
1.95e-69 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 234.71 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQSCpTALFLAADAIGIRQIGYRTENAGAAMADGAARV--GRQLTVITAQNGPAAALLVAGF 105
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFPV-NELFDAAAAAGIRPVIARTERVAVHMADGYARAtsGERVGVFAVQYGPGAENAFGGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 106 SEATKASVPILAIVQEVPRANAD-KNAFQELDHvqlFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV 184
Cdd:PRK06154 101 AQAYGDSVPVLFLPTGYPRGSTDvAPNFESLRN---YRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LttacpqarpvaqdsDEPLGRFPLDRTVPVAGRLA-------QLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGL 257
Cdd:PRK06154 178 L--------------AEELDELPLDHRPSRRSRPGadpvevvEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 258 PVATTNMGKGAIDETHPLSLGVIGNAMgtrsPAK--HFmdyVRSADFVLFVG---TRTNENGTaswslFPEQAQYAQIDI 332
Cdd:PRK06154 244 PVMTTLNGKSAFPEDHPLALGSGGRAR----PATvaHF---LREADVLFGIGcslTRSYYGLP-----MPEGKTIIHSTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 333 DSEEVGRNYG-AMRFAGDAAATLQALGDALQERgQAVAARRMAELAPAFEACRQAHRAELAPYAQSDASPMRPERIMAEL 411
Cdd:PRK06154 312 DDADLNKDYPiDHGLVGDAALVLKQMIEELRRR-VGPDRGRAQQVAAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 412 RAS--HGDIIWVADASYSSIWLAQFIPCTQAGTRFVTPRGIAgLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELE 489
Cdd:PRK06154 391 QHAvdIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQ-LGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 490 TARRHEVPVTIVVLNNGVLGfqINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAER---SPVP 566
Cdd:PRK06154 470 TAVRERIPILTILLNNFSMG--GYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALRkvkEGTP 547
|
....*..
gi 504854683 567 FVIDVKT 573
Cdd:PRK06154 548 ALLEVIT 554
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
5-571 |
1.08e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 225.70 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 5 TESPPGARTSTGSWARQDLSAYqaanAIADVLKAAGVAQIFGQscP--------TALFLAADAIGIRQIGYRTENAGAAM 76
Cdd:PRK07418 2 TSSPPKIGDSTTVTPQRATGAY----ALMDSLKRHGVKHIFGY--PggailpiyDELYKAEAEGWLKHILVRHEQGAAHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 77 ADGAARVGRQLTVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAK--WVRR--ID 152
Cdd:PRK07418 76 ADGYARATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKhsYVVRdpSD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 153 VAERAAEyterAIRIATSGRPGPVVLLVSQDVLTTACpQARPVAQDSDEPLGRFPldrtvPVAGRLAQLAQRL---LDAK 229
Cdd:PRK07418 156 MARIVAE----AFHIASSGRPGPVLIDIPKDVGQEEF-DYVPVEPGSVKPPGYRP-----TVKGNPRQINAALkliEEAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 230 RPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaMgtrspakHFMDY----VRSADFVLF 305
Cdd:PRK07418 226 RPLLYVGGGAISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLG--M-------HGTAYanfaVTECDLLIA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 306 VGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNYGA-MRFAGDAAATLQALgdaLQERGQAVAARRMAELAPAFEACR 384
Cdd:PRK07418 297 VGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPdVPIVGDVRKVLVKL---LERSLEPTTPPRTQAWLERINRWK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 385 QAHRAELAPYAQSdaspMRPERIMAELRASHGDIIWVADASYSSIWLAQFIPCtqAGTRFVTPRGIAGLGWGVPMAIGAK 464
Cdd:PRK07418 374 QDYPLVVPPYEGE----IYPQEVLLAVRDLAPDAYYTTDVGQHQMWAAQFLRN--GPRRWISSAGLGTMGFGMPAAMGVK 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 465 IARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGFQINAEESRFG---THTDVCHfGAIDHVAIAKACG 541
Cdd:PRK07418 448 VALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQWQESFYGerySASNMEP-GMPDFVKLAEAFG 526
|
570 580 590
....*....|....*....|....*....|
gi 504854683 542 CDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PRK07418 527 VKGMVISERDQLKDAIAEALAHDGPVLIDV 556
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
95-571 |
1.43e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 221.24 E-value: 1.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 95 GPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPG 174
Cdd:PRK08322 72 GPGATNLVTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 175 PVVLLVSQDVlttacpqarpVAQDSDE-PLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQS 253
Cdd:PRK08322 152 AVHLELPEDI----------AAEETDGkPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 254 LAGLPVATTNMGKGAIDETHPLSLGVIGnamgtrspakhFM--DYV----RSADFVLFVG--------TRTNENGTAsws 319
Cdd:PRK08322 222 KTGIPFFTTQMGKGVIPETHPLSLGTAG-----------LSqgDYVhcaiEHADLIINVGhdviekppFFMNPNGDK--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 320 lfpeqaQYAQIDIDSEEVGRNYG-AMRFAGDAAATLQALGDALQERGQavaarrmaELAPAFEACRQAHRAELAPYAQSD 398
Cdd:PRK08322 288 ------KVIHINFLPAEVDPVYFpQVEVVGDIANSLWQLKERLADQPH--------WDFPRFLKIREAIEAHLEEGADDD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 399 ASPMRPERIMAELRASHG--DIIWVADASYSsIWLAQFIPCTQAGTRFVTpRGIAGLGWGVPMAIGAKIARPGARVICLT 476
Cdd:PRK08322 354 RFPMKPQRIVADLRKVMPddDIVILDNGAYK-IWFARNYRAYEPNTCLLD-NALATMGAGLPSAIAAKLVHPDRKVLAVC 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 477 GDGGFAHCWAELETARRHEVPVTIVVLNNGVLGF----QINaeesRFGTHTDVcHFGAIDHVAIAKACGCDGASVSDAAS 552
Cdd:PRK08322 432 GDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMirwkQEN----MGFEDFGL-DFGNPDFVKYAESYGAKGYRVESADD 506
|
490
....*....|....*....
gi 504854683 553 LRQAMAAAERSPVPFVIDV 571
Cdd:PRK08322 507 LLPTLEEALAQPGVHVIDC 525
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
28-574 |
5.63e-63 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 217.93 E-value: 5.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGqsCPTAL---FLAA--DAIGIRQIGYRTENAGAAMADGAARV--GRqLTVITAQNGPAAAL 100
Cdd:PRK11269 6 AVDAAVLVLEKEGVTTAFG--VPGAAinpFYSAmrKHGGIRHILARHVEGASHMAEGYTRAtaGN-IGVCIGTSGPAGTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 101 LVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLV 180
Cdd:PRK11269 83 MITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 181 SQDVlttacpQARPVAQDSD--EPLgrfPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLP 258
Cdd:PRK11269 163 PFDV------QVAEIEFDPDtyEPL---PVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 259 VATTNMGKGAIDETHPLSLGVIGNAMGTRSPAKHFMdyvrSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVG 338
Cdd:PRK11269 234 VIPTLMGWGAIPDDHPLMAGMVGLQTSHRYGNATLL----ASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 339 RNYGA-MRFAGDAAATLQALGDALQERGqavAARRMAELAPAFEACRQAHRAELAPyAQSDASPMRPERIMAELRASHG- 416
Cdd:PRK11269 310 RVFGPdLGIVSDAKAALELLVEVAREWK---AAGRLPDRSAWVADCQERKRTLLRK-THFDNVPIKPQRVYEEMNKAFGr 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 417 DIIWVADASYSSIWLAQF---------IPCTQAGTrfvtprgiagLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAE 487
Cdd:PRK11269 386 DTCYVSTIGLSQIAAAQFlhvykprhwINCGQAGP----------LGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 488 LETARRHEVPVTIVVLNNGVLGF-------------------QINAEEsrfgthtdVCHFGaIDHVAIAKACGCDGASVS 548
Cdd:PRK11269 456 LAVGAQFNLPYIHVLVNNAYLGLirqaqrafdmdycvqlafeNINSPE--------LNGYG-VDHVKVAEGLGCKAIRVF 526
|
570 580 590
....*....|....*....|....*....|
gi 504854683 549 D----AASLRQAMAAAERSPVPFVIDVKTE 574
Cdd:PRK11269 527 KpediAPALEQAKALMAEFRVPVVVEVILE 556
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
31-571 |
4.08e-61 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 211.77 E-value: 4.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 31 AIADVLKAAGVAQIFG----QSCPTAlflaaDAIG----IRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLV 102
Cdd:PRK07064 8 LIAAFLEQCGVKTAFGvisiHNMPIL-----DAIGrrgkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 103 AGFSEATKASVPILAIVQEVPRANADKNA---FQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLL 179
Cdd:PRK07064 83 GALVEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 180 VSQDVlttacpQARPVAQDSDepLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVhlSGACDALARLQSLaGLPV 259
Cdd:PRK07064 163 IPIDI------QAAEIELPDD--LAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGA--RHAGAEVKRLVDL-GFGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 260 ATTNMGKGAIDETHPLSLGvignAMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSL-FPEQaqYAQIDIDSEEVG 338
Cdd:PRK07064 232 VTSTQGRGVVPEDHPASLG----AFNNSAAVEALY---KTCDLLLVVGSRLRGNETLKYSLaLPRP--LIRVDADAAADG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 339 RNYGAMRF-AGDAAATLQALGDALQERGQaVAARRMAELAPAFEACRQAHRAELAPYAQsdaspmrperIMAELRASHG- 416
Cdd:PRK07064 303 RGYPNDLFvHGDAARVLARLADRLEGRLS-VDPAFAADLRAAREAAVADLRKGLGPYAK----------LVDALRAALPr 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 417 DIIWVADASYS-SIWLAQFIPcTQAGTRFVTPRGiAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHE 495
Cdd:PRK07064 372 DGNWVRDVTISnSTWGNRLLP-IFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQEN 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504854683 496 VPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PRK07064 450 ANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
28-583 |
1.27e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 210.79 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQScPTALFLAADAI---GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYP-GGAIIPVYDELydsDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV 184
Cdd:PRK06048 89 IATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTTACPQARPvaqDSDEPLGRFPldrtvPVAGRLAQL---AQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVAT 261
Cdd:PRK06048 169 TTAEIDFDYP---DKVELRGYKP-----TYKGNPQQIkraAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 262 TNMGKGAIDETHPLSLGVIGnAMGTRspakhFMDY-VRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRN 340
Cdd:PRK06048 241 TLMGIGAIPTEHPLSLGMLG-MHGTK-----YANYaIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 341 YGA-MRFAGDAAATLQALGDALQERgqavaarrmaELAPAFEACRQAHRAELAPYAQSDASpMRPERIMAELRASHGDII 419
Cdd:PRK06048 315 VKVdVPIVGDAKQVLKSLIKYVQYC----------DRKEWLDKINQWKKEYPLKYKEREDV-IKPQYVIEQIYELCPDAI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 420 WVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVT 499
Cdd:PRK06048 384 IVTEVGQHQMWAAQYFKYKYPRT-FITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 500 IVVLNNGVLGFQINAEESRFG---THTdvCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVID--VKTE 574
Cdd:PRK06048 463 VAILNNGYLGMVRQWQELFYDkrySHT--CIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDfiVECE 540
|
....*....
gi 504854683 575 PSAFPPISA 583
Cdd:PRK06048 541 ENVSPMVPA 549
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
32-592 |
5.68e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 209.29 E-value: 5.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 32 IADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSE 107
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLY-DAIynfeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 108 ATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRI-DVAERAAEYTErAIRIATSGRPGPVVLLVSQDVLT 186
Cdd:PRK07282 95 AMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIrETADIPRIITE-AVHIATTGRPGPVVIDLPKDVSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 187 TAC----------PQARPVAQDSDEPLGRFpldrtvpvagrLAQLAQrlldAKRPLVVAGGGVHLSGACDALARLQSLAG 256
Cdd:PRK07282 174 LETdfiydpevnlPSYQPTLEPNDMQIKKI-----------LKQLSK----AKKPVILAGGGINYAEAATELNAFAERYQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 257 LPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMDyvrSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEE 336
Cdd:PRK07282 239 IPVVTTLLGQGTIATSHPLFLGMGG--MHGSYAANIAMT---EADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 337 VGRNYGA-MRFAGDAAATLQALgdaLQERGQAVAARRMAELAPAfeacrqahRAELAPYAQSDASPMRPERIMAEL-RAS 414
Cdd:PRK07282 314 IGKIIKTdIPVVGDAKKALQML---LAEPTVHNNTEKWIEKVTK--------DKNRVRSYDKKERVVQPQAVIERIgELT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 415 HGDIIWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRH 494
Cdd:PRK07282 383 NGDAIVVTDVGQHQMWAAQYYPYQNE-RQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 495 EVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAI-DHVAIAKACGCDGASVSDAASLRQAMAA-AERSPVPFVIDVK 572
Cdd:PRK07282 462 KVPIKVVMLNNHSLGMVRQWQESFYEGRTSESVFDTLpDFQLMAQAYGIKHYKFDNPETLAQDLEViTEDVPMLIEVDIS 541
|
570 580
....*....|....*....|
gi 504854683 573 TEPSAFPPISAFESQLRPLG 592
Cdd:PRK07282 542 RKEHVLPMVPAGKSNHEMLG 561
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
28-579 |
6.35e-60 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 209.47 E-value: 6.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGqscptalfLAADAIG------------IRQIGYRTENAGAAMADGAARVGRQLTVITAQNG 95
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYG--------IPGDSIDavvdalrkeqdkIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 96 PAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGP 175
Cdd:PRK08611 78 PGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 176 VVLLVSQDVLttacpqARPVAQDSDEPLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHlsGACDALARLQSLA 255
Cdd:PRK08611 157 AVLTIPDDLP------AQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 256 GLPVATTNMGKGAIDETHPLSLGVIGNaMGTRsPAKHFMdyvRSADFVLFVGTR---TNengtaswsLFPEQAQYAQIDI 332
Cdd:PRK08611 229 KIPIIHTLPAKGIIPDDHPYSLGNLGK-IGTK-PAYEAM---QEADLLIMVGTNypyVD--------YLPKKAKAIQIDT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 333 DSEEVGRNYGA-MRFAGDAAATLQALgdalQERGQAVAARRMaelapaFEACrQAHRA----ELAPYAQSDASPMRPERI 407
Cdd:PRK08611 296 DPANIGKRYPVnVGLVGDAKKALHQL----TENIKHVEDRRF------LEAC-QENMAkwwkWMEEDENNASTPIKPERV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 408 MAEL-RASHGDIIWVADASYSSIWLAQFIPcTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWA 486
Cdd:PRK08611 365 MAAIqKIADDDAVLSVDVGTVTVWSARYLN-LGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 487 ELETARRHEVPVTIVVLNNGVLGFqINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVP 566
Cdd:PRK08611 444 DFVTAVKYKLPIVVVVLNNQQLAF-IKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKP 522
|
570
....*....|...
gi 504854683 567 FVIDVKTEPSAFP 579
Cdd:PRK08611 523 VIIDVYVDPNAAP 535
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
29-579 |
1.96e-58 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 205.20 E-value: 1.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQScPTALFLAADAI---GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGF 105
Cdd:PRK06725 18 AGHVIQCLKKLGVTTVFGYP-GGAILPVYDALyesGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 106 SEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV- 184
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVq 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 ---LTTACPQARPVAQDSDEPlgrfpldrtVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVAT 261
Cdd:PRK06725 177 nekVTSFYNEVVEIPGYKPEP---------RPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 262 TNMGKGAIDETHPLSLGVIGnAMGTRSPAKHFMDyvrsADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNY 341
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGMLG-MHGTYAANMAVTE----CDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 342 GA-MRFAGDAAATLQALgdaLQERGQAVAARRMAELapafeacrQAHRAELAPYAQSDASPMRPERIMAEL-RASHGDII 419
Cdd:PRK06725 323 AVeYPVVGDVKKALHML---LHMSIHTQTDEWLQKV--------KTWKEEYPLSYKQKESELKPQHVINLVsELTNGEAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 420 WVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVT 499
Cdd:PRK06725 392 VTTEVGQHQMWAAHFYKAKNPRT-FLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 500 IVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVID--VKTEPSA 577
Cdd:PRK06725 471 VFIINNKFLGMVRQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDfcVEEGENV 550
|
..
gi 504854683 578 FP 579
Cdd:PRK06725 551 FP 552
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
62-579 |
9.80e-57 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 200.70 E-value: 9.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 62 IRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLF 141
Cdd:CHL00099 52 IKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGIT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 142 ASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVLTTACPQARPVAQDSDEPLGRFPlDRTVPVAGRLAQL 221
Cdd:CHL00099 132 LPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEKFDYYPPEPGNTIIKILGCR-PIYKPTIKRIEQA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 222 AQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaM-GTRspakhFMDY-VRS 299
Cdd:CHL00099 211 AKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGMLG--MhGTA-----YANFaVSE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 300 ADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRN-YGAMRFAGDAAATLQALGDALQERGQAVAARRMaelap 378
Cdd:CHL00099 284 CDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNrIPQVAIVGDVKKVLQELLELLKNSPNLLESEQT----- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 379 afeacrQAHRAELAPYAQS-------DASPMRPERIMAELRASHGDIIWVADASYSSIWLAQFIPCTQagTRFVTPRGIA 451
Cdd:CHL00099 359 ------QAWRERINRWRKEypllipkPSTSLSPQEVINEISQLAPDAYFTTDVGQHQMWAAQFLKCKP--RKWLSSAGLG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 452 GLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGFQINAEESRFG---THTDVCHf 528
Cdd:CHL00099 431 TMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQAFYGerySHSNMEE- 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 504854683 529 GAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVID--VKTEPSAFP 579
Cdd:CHL00099 510 GAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDcqVIEDENCYP 562
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
28-581 |
1.97e-52 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 188.30 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGqsCP--------TALFLAADAIgiRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAA 99
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFG--LPgaqlywlfDALYKAGDRI--RVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 100 LLVAGFSEATKASVPILAIVQEVPRANADKNAFQ--EL-DHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPV 176
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 177 VLLVSQDVLTTACPQARPVAQDSDEPLgrfPLDrtvpvAGRLAQLAQRLLDAKRPLVVAGGGVhlSGACDALARLQSLAG 256
Cdd:PRK08266 162 ALEMPWDVFGQRAPVAAAPPLRPAPPP---APD-----PDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 257 LPVATTNMGKGAIDETHPLSLGVIGNamgtrspakhfMDYVRSADFVLFVGTRTnENGTASWSLFPEQAQYAQIDIDSEE 336
Cdd:PRK08266 232 APVVAFRSGRGIVSDRHPLGLNFAAA-----------YELWPQTDVVIGIGSRL-ELPTFRWPWRPDGLKVIRIDIDPTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 337 VGRNYGAMRFAGDAAATLQALGDALQERGQAVAARRmAELAPAFEACRQAHRAelapyAQSDASPMRperIMAELRASHG 416
Cdd:PRK08266 300 MRRLKPDVAIVADAKAGTAALLDALSKAGSKRPSRR-AELRELKAAARQRIQA-----VQPQASYLR---AIREALPDDG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 417 diIWVADAS---YSSiWLA-------QFIPCTQAGTrfvtprgiagLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWA 486
Cdd:PRK08266 371 --IFVDELSqvgFAS-WFAfpvyaprTFVTCGYQGT----------LGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQ 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 487 ELETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVP 566
Cdd:PRK08266 438 ELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGP 517
|
570
....*....|....*....
gi 504854683 567 FVIDVK----TEPSAFPPI 581
Cdd:PRK08266 518 VLIEVPvprgSEASPWPFI 536
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
29-571 |
3.11e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 185.43 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQSCPTAL-----FLAADAIG-IRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLV 102
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMqiydaFVEDLANGeLRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 103 AGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQ 182
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 183 DVLTTACPQA----RPVAQDSDEplgrFP--LDRTvpvagRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAG 256
Cdd:PRK06456 165 DIFYEKMEEIkwpeKPLVKGYRD----FPtrIDRL-----ALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 257 LPVATTNMGKGAIDETHPLSLGvignAMGTRSPAKHFMDYVRSaDFVLFVGTRTNENGTASWSLFPE-QAQYAQIDIDSE 335
Cdd:PRK06456 236 IPIVSTFPGKTAIPHDHPLYFG----PMGYYGRAEASMAALES-DAMLVVGARFSDRTFTSYDEMVEtRKKFIMVNIDPT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 336 EVGRNYGA-MRFAGDAAATLQALGDALQE----RGQAVAARRMAELAPAFEACrqahraelapYAQSDASPMRPERIMAE 410
Cdd:PRK06456 311 DGEKAIKVdVGIYGNAKIILRELIKAITElgqkRDRSAWLKRVKEYKEYYSQF----------YYTEENGKLKPWKIMKT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 411 LRAS-HGDIIWVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELE 489
Cdd:PRK06456 381 IRQAlPRDAIVTTGVGQHQMWAEVFWEVLEPRT-FLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 490 TARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFG-AIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFV 568
Cdd:PRK06456 460 TAVDEHIPVISVIFDNRTLGLVRQVQDLFFGKRIVGVDYGpSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAV 539
|
...
gi 504854683 569 IDV 571
Cdd:PRK06456 540 IRV 542
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
82-571 |
1.36e-49 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 181.09 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 82 RVGrqltVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYT 161
Cdd:PLN02470 76 KVG----VCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 162 ERAIRIATSGRPGPVVLLVSQDVlttacpQARPVAQDSDEP------LGRFPldrTVPVAGRLAQLAQRLLDAKRPLVVA 235
Cdd:PLN02470 152 REAFFLASSGRPGPVLVDIPKDI------QQQLAVPNWNQPmklpgyLSRLP---KPPEKSQLEQIVRLISESKRPVVYV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 236 GGGVhlSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMDyvrSADFVLFVGTRTNENGT 315
Cdd:PLN02470 223 GGGC--LNSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMLG--MHGTVYANYAVD---SADLLLAFGVRFDDRVT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 316 ASWSLFPEQAQYAQIDIDSEEVGRNYGA-MRFAGDAAATLQALGDALQERGQAvaarrmaelAPAFEACR---QAHRAEL 391
Cdd:PLN02470 296 GKLEAFASRASIVHIDIDPAEIGKNKQPhVSVCADVKLALQGLNKLLEERKAK---------RPDFSAWRaelDEQKEKF 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 392 -APYAQSDAS--PMRPERIMAELraSHGDIIWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARP 468
Cdd:PLN02470 367 pLSYPTFGDAipPQYAIQVLDEL--TDGNAIISTGVGQHQMWAAQWYKYKEP-RRWLTSGGLGAMGFGLPAAIGAAAANP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 469 GARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGFQINAEEsRFG----THT---DVCHFGAI--DHVAIAKA 539
Cdd:PLN02470 444 DAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWED-RFYkanrAHTylgDPDAEAEIfpDFLKFAEG 522
|
490 500 510
....*....|....*....|....*....|..
gi 504854683 540 CGCDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PLN02470 523 CKIPAARVTRKSDLREAIQKMLDTPGPYLLDV 554
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
112-572 |
1.40e-49 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 180.17 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 112 SVPILAI--VQEVPRANADKNAFQEL-DHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVLTTa 188
Cdd:PRK07524 90 SIPMLVIssVNRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLDVLAA- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 189 cpqarPVAQDSDEPLGRfpLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVhlSGACDALARLQSLAGLPVATTNMGKGA 268
Cdd:PRK07524 169 -----PADHLLPAPPTR--PARPGPAPAALAQAAERLAAARRPLILAGGGA--LAAAAALRALAERLDAPVALTINAKGL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 269 IDETHPLSLGVIGNAMGTRspakhfmDYVRSADFVLFVGT---RTNENGTASWSlFPEQAQYAQIDIDSEEVGRNY-GAM 344
Cdd:PRK07524 240 LPAGHPLLLGASQSLPAVR-------ALIAEADVVLAVGTelgETDYDVYFDGG-FPLPGELIRIDIDPDQLARNYpPAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 345 RFAGDAAATLQALGDALQergQAVAARRMAelAPAFEACRQAHRAELAPYAQSDAspmrpeRIMAELRASHGDIIWVADa 424
Cdd:PRK07524 312 ALVGDARAALEALLARLP---GQAAAADWG--AARVAALRQALRAEWDPLTAAQV------ALLDTILAALPDAIFVGD- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 425 SYSSIWLAQFIpCTQAGTR--FVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVV 502
Cdd:PRK07524 380 STQPVYAGNLY-FDADAPRrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLL 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504854683 503 LNNGVLGfqinaEESRFGTHTDV----CHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVK 572
Cdd:PRK07524 459 WNNDGYG-----EIRRYMVARDIepvgVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVD 527
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
29-509 |
2.93e-49 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 179.69 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQscPT-ALFLAADAI---GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK08978 4 AQWVVHALRAQGVDTVFGY--PGgAIMPVYDALydgGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAK---WVRRIDvaeRAAEYTERAIRIATSGRPGPVVLLVS 181
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKhsfLVQSLE---ELPEIMAEAFEIASSGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 182 QDVLttacpqarpVAQDSDEPLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVAT 261
Cdd:PRK08978 159 KDIQ---------LAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 262 TNMGKGAIDETHPLSLGVIGnaM-GTRspAKHFMdyVRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRn 340
Cdd:PRK08978 230 TLKGLGAVEADHPYYLGMLG--MhGTK--AANLA--VQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINK- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 341 ygaMRFA-----GDAAATLQALGDALQ-ERGQAVAARRMAELAPAFEacrqaHRAEL--APYAQSDASPMRPErimaelr 412
Cdd:PRK08978 303 ---LRQAhvalqGDLNALLPALQQPLNiDAWRQHCAQLRAEHAWRYD-----HPGEAiyAPALLKQLSDRKPA------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 413 ashgDIIWVADASYSSIWLAQFIpctqagtRFVTPR------GIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWA 486
Cdd:PRK08978 368 ----DTVVTTDVGQHQMWVAQHM-------RFTRPEnfitssGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQ 436
|
490 500
....*....|....*....|...
gi 504854683 487 ELETARRHEVPVTIVVLNNGVLG 509
Cdd:PRK08978 437 ELGTIKRKQLPVKIVLLDNQRLG 459
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
31-580 |
5.33e-49 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 179.42 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 31 AIADVLKAAGVAQIFG---QSCPTALFLAADAiGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSE 107
Cdd:PRK07525 11 AFVETLQAHGITHAFGiigSAFMDASDLFPPA-GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 108 ATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGPVVLLVSQDVLTT 187
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFYG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 188 ACPQARPVAQDSDEPLGRfpldrtvpvAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKG 267
Cdd:PRK07525 169 VIDVEIPQPVRLERGAGG---------EQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 268 AIDETHPLSLGVIGnAMGTrspaKHFMDYVRSADFVLFVGTRTNENGTA---SWSLFPEQAQYAQIDIDSEEVGRNYG-A 343
Cdd:PRK07525 240 AFPGSHPLWVGPLG-YNGS----KAAMELIAKADVVLALGTRLNPFGTLpqyGIDYWPKDAKIIQVDINPDRIGLTKKvS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 344 MRFAGDAAATLQALGDALQER--GQAVAARRMAELApafeACRQAHRAELAPYAQSD---------------ASPMRPER 406
Cdd:PRK07525 315 VGICGDAKAVARELLARLAERlaGDAGREERKALIA----AEKSAWEQELSSWDHEDddpgtdwneeararkPDYMHPRQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 407 IMAEL-RASHGDIIWVAD-ASYSSIwlAQFIPCTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHC 484
Cdd:PRK07525 391 ALREIqKALPEDAIVSTDiGNNCSI--ANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGIS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 485 WAELETARRHEVPVTIVVLNNGVLGF----QINAEESRF-GTHTDvchfGAIDHVAIAKACGCDGASVSDAASLRQAMAA 559
Cdd:PRK07525 469 MNEVMTAVRHNWPVTAVVFRNYQWGAekknQVDFYNNRFvGTELD----NNVSYAGIAEAMGAEGVVVDTQEELGPALKR 544
|
570 580
....*....|....*....|....
gi 504854683 560 A---ERSPVPFVIDVKTEPSAFPP 580
Cdd:PRK07525 545 AidaQNEGKTTVIEIMCNQELGEP 568
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
36-576 |
7.22e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 178.80 E-value: 7.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 36 LKAAGVAQIFGQSCPTALFLAaDAI---GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSEATKAS 112
Cdd:PRK07710 26 LEKEGVEVIFGYPGGAVLPLY-DALydcGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLADAMIDS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 113 VPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVltTACPQA 192
Cdd:PRK07710 105 LPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDM--VVEEGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 193 RPVAQDSDEPlGRFPldRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDET 272
Cdd:PRK07710 183 FCYDVQMDLP-GYQP--NYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPAD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 273 HPLSLGVIG-NAMGTRSPAKHfmdyvrSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNY-GAMRFAGDA 350
Cdd:PRK07710 260 HPLFLGMAGmHGTYTANMALY------ECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVpTEIPIVADA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 351 AATLQALgdALQERGQAVAARRMAELApafeacrqAHRAELAPYAQSDASPMRPERIMAEL-RASHGDIIWVADASYSSI 429
Cdd:PRK07710 334 KQALQVL--LQQEGKKENHHEWLSLLK--------NWKEKYPLSYKRNSESIKPQKAIEMLyEITKGEAIVTTDVGQHQM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 430 WLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLG 509
Cdd:PRK07710 404 WAAQYYPFKTP-DKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504854683 510 ----FQINAEESRFGTHTDVCHfgaIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPS 576
Cdd:PRK07710 483 mvrqWQEEFYNQRYSHSLLSCQ---PDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQS 550
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
29-560 |
1.36e-48 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 178.09 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIY-DALheksGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV 184
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTTAC--PQARP--VAQDSDEPlgrfpldRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVA 260
Cdd:PRK08979 166 LNPAIlhPYEYPesIKMRSYNP-------TTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 261 TTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRN 340
Cdd:PRK08979 239 STLMGLGAFPGTHKNSLGMLG--MHGRYEANMAM---HNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 341 YGA-MRFAGDAAATLQALGDALQERGQAVAARRMAELAPAFEACRQahRAELAPYAQSDAspMRPERIMAEL-RASHGDI 418
Cdd:PRK08979 314 VRVdIPIVGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRS--RNCLAYDKSSER--IKPQQVIETLyKLTNGDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 419 IWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPV 498
Cdd:PRK08979 390 YVASDVGQHQMFAALYYPFDKP-RRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504854683 499 TIVVLNNGVLGFQINAEESRF-GTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:PRK08979 469 KIINLNNRFLGMVKQWQDMIYqGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKA 531
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-570 |
3.92e-48 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 177.48 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 1 MQAHTESPPGARTSTGSWARQDLSAYQAANAIADVLKAAGVAQIFGqsCPTALFLAA-----DAIGIRQIGYRTENAGAA 75
Cdd:PRK07789 6 PAAAASAAPPPAAPAARPRIVAPERMTGAQAVVRSLEELGVDVVFG--IPGGAILPVydplfDSTKVRHVLVRHEQGAGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 76 MADGAARVGRQLTVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAK---WVRR-I 151
Cdd:PRK07789 84 AAEGYAQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKhnfLVTDaD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 152 DVAERAAEyterAIRIATSGRPGPVVLLVSQDVLTTACPQARPvaQDSDEPlGRFPLdrTVPVAGRLAQLAQRLLDAKRP 231
Cdd:PRK07789 164 DIPRVIAE----AFHIASTGRPGPVLVDIPKDALQAQTTFSWP--PRMDLP-GYRPV--TKPHGKQIREAAKLIAAARRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 232 LVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAkhfMDYVRSADFVLFVGTRTN 311
Cdd:PRK07789 235 VLYVGGGVIRAEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMPG--MHGTVAA---VAALQRSDLLIALGARFD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 312 ENGTASWSLFPEQAQYAQIDIDSEEVGRNygamRFA-----GDAAATLQALGDALQERGqavAARRMAELAPAFEACRQA 386
Cdd:PRK07789 310 DRVTGKLDSFAPDAKVIHADIDPAEIGKN----RHAdvpivGDVKEVIAELIAALRAEH---AAGGKPDLTAWWAYLDGW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 387 HRAELAPYAQSDASPMRPERIMAELRASHG-DIIWVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKI 465
Cdd:PRK07789 383 RETYPLGYDEPSDGSLAPQYVIERLGEIAGpDAIYVAGVGQHQMWAAQFIDYEKPRT-WLNSGGLGTMGYAVPAAMGAKV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 466 ARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLG----FQINAEESRFgTHTDV-CHFGAI-DHVAIAKA 539
Cdd:PRK07789 462 GRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGmvrqWQTLFYEERY-SNTDLhTHSHRIpDFVKLAEA 540
|
570 580 590
....*....|....*....|....*....|....*
gi 504854683 540 CGCDGASVSDA----ASLRQAMAAAERspvPFVID 570
Cdd:PRK07789 541 YGCVGLRCEREedvdAVIEKARAINDR---PVVID 572
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
28-579 |
7.58e-48 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 175.68 E-value: 7.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIF----GQSCPtaLFLAADAIGIRQIGYRTENAGAAMADGAARVGRQ--LTVITAqnGPAAALL 101
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFtlsgGHLFP--LYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVpgVAVLTA--GPGVTNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 102 VAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVS 181
Cdd:PRK05858 83 MSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 182 QDVL-TTACPQARPVAqDSDEPLGRFPLDRTVPVAGRLaqlaqrLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVA 260
Cdd:PRK05858 163 MDHAfSMADDDGRPGA-LTELPAGPTPDPDALARAAGL------LAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 261 TTNMGKGAIDETHPLSLgvignamgTRSPAKHFmdyvRSADFVLFVGT----RTNengtasWSLFPEQAQYAQI-DIDSE 335
Cdd:PRK05858 236 MNGMGRGVVPADHPLAF--------SRARGKAL----GEADVVLVVGVpmdfRLG------FGVFGGTAQLVHVdDAPPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 336 EVGRNYGAMRFAGDAAATLQALGDALQERGQavAARRMAELAPAFEACRQAHRAELApyaqSDASPMRPERIMAELRAS- 414
Cdd:PRK05858 298 RAHHRPVAAGLYGDLSAILSALAGAGGDRTD--HQGWIEELRTAETAARARDAAELA----DDRDPIHPMRVYGELAPLl 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 415 HGDIIWVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRH 494
Cdd:PRK05858 372 DRDAIVIGDGGDFVSYAGRYIDPYRPGC-WLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 495 EVPVTIVVLNNGVLGFQINAEESRFG--THTDVCHFGAIDHVaiAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVK 572
Cdd:PRK05858 451 NLPVVSVIGNNGIWGLEKHPMEALYGydVAADLRPGTRYDEV--VRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
....*...
gi 504854683 573 TEPS-AFP 579
Cdd:PRK05858 529 TDPSvAYP 536
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
26-583 |
1.19e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 175.28 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 26 YQAANAIADVLKAAGVAQIFGQSCPTALFLAaDAIG----IRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALL 101
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLY-DALSqstqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 102 VAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAK---WVRRIdvaERAAEYTERAIRIATSGRPGPVVL 178
Cdd:PRK08155 92 VTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKhnyLVRDI---EELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 179 LVSQDVLTTACpqarpvaqDSDEPLGRFPLDRTVPVAGRLAQLAQRLLD-AKRPLVVAGGGVHLSGACDALARLQSLAGL 257
Cdd:PRK08155 169 DIPKDVQTAVI--------ELEALPAPAEKDAAPAFDEESIRDAAAMINaAKRPVLYLGGGVINSGAPARARELAEKAQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 258 PVATTNMGKGAIDETHPLSLGVIGnaM-GTRSpakhfMDYV-RSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSE 335
Cdd:PRK08155 241 PTTMTLMALGMLPKAHPLSLGMLG--MhGARS-----TNYIlQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 336 EVGRNYGA-MRFAGDAAATLQALGDALQERGQAVAARRMAELAPAFeacrqahraelaPYAQSDAS-PMRPE-RIMAELR 412
Cdd:PRK08155 314 ELGKIKQPhVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREF------------PCPIPKADdPLSHYgLINAVAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 413 ASHGDIIWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETAR 492
Cdd:PRK08155 382 CVDDNAIITTDVGQHQMWTAQAYPLNRP-RQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 493 RHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHF-GAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PRK08155 461 ENQLDVKIILMNNEALGLVHQQQSLFYGQRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHV 540
|
570
....*....|....*..
gi 504854683 572 KTEPSAF-----PPISA 583
Cdd:PRK08155 541 RIDAEEKvypmvPPGAA 557
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
406-573 |
2.03e-47 |
|
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: 163.58 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 406 RIMAELRASHG-DIIWVADASYSSIWLAQFIPcTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHC 484
Cdd:cd00568 1 RVLAALRAALPeDAIVVNDAGNSAYWAYRYLP-LRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 485 WAELETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSP 564
Cdd:cd00568 80 GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAG 159
|
....*....
gi 504854683 565 VPFVIDVKT 573
Cdd:cd00568 160 GPALIEVKT 168
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
36-560 |
6.68e-47 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 173.39 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 36 LKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSEATKA 111
Cdd:PRK06466 14 LRDEGVEYIYGYPGGAVLHIY-DALfkqdKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGIATAYMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 112 SVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVLTTACPQ 191
Cdd:PRK06466 93 SIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDMTNPAEKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 192 A----RPVAQDSDEPLGRfpldrtvPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKG 267
Cdd:PRK06466 173 EyeypKKVKLRSYSPAVR-------GHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 268 AIDETHPLSLGVIGnaMGTRSPAKHFMDYvrsADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNYGA-MRF 346
Cdd:PRK06466 246 GFPGTDRQFLGMLG--MHGTYEANMAMHH---ADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKAdIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 347 AGDAAATLQALGDALQERGQAVAARRMAELAPAFEACRQAHRaeLAPYAQSDASPMRPERIMAEL-RASHGDIIWVADAS 425
Cdd:PRK06466 321 VGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHG--LFPYDKGDGGIIKPQQVVETLyEVTNGDAYVTSDVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 426 YSSIWLAQFIpctqagtRFVTPR------GIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVT 499
Cdd:PRK06466 399 QHQMFAAQYY-------KFNKPNrwinsgGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVK 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504854683 500 IVVLNNGVLG----FQINAEESRfgtHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:PRK06466 472 IINLNNGALGmvrqWQDMQYEGR---HSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEA 533
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
11-583 |
9.82e-47 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 173.07 E-value: 9.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 11 ARTSTGSWARQDLsayQAANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQ 86
Cdd:PRK06965 9 STAESLSPPAADS---IGAEILMKALAAEGVEFIWGYPGGAVLYIY-DELykqdKIQHVLVRHEQAAVHAADGYARATGK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 87 LTVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIR 166
Cdd:PRK06965 85 VGVALVTSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 167 IATSGRPGPVVLLVSQDVLTTACPQARP--VAQDSDEPLGRFPldrtvpvAGRLAQLAQRLLDAKRPLVVAGGGVHLSGA 244
Cdd:PRK06965 165 IARTGRPGPVVVDIPKDVSKTPCEYEYPksVEMRSYNPVTKGH-------SGQIRKAVSLLLSAKRPYIYTGGGVILANA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 245 CDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSLFPEQ 324
Cdd:PRK06965 238 SRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGMLG--MHGTYEANMAM---QHCDVLIAIGARFDDRVIGNPAHFASR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 325 A-QYAQIDIDSEEVGRNYGA-MRFAGDAAATLQALGDALQERGQAVAArrmAELAPAFEACRQAHRAELAPYAQSDaSPM 402
Cdd:PRK06965 313 PrKIIHIDIDPSSISKRVKVdIPIVGDVKEVLKELIEQLQTAEHGPDA---DALAQWWKQIEGWRSRDCLKYDRES-EII 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 403 RPERIMAEL-RASHGDIIWVADASYSSIWLAQFIpctqagtRFVTPR------GIAGLGWGVPMAIGAKIARPGARVICL 475
Cdd:PRK06965 389 KPQYVVEKLwELTDGDAFVCSDVGQHQMWAAQFY-------RFNEPRrwinsgGLGTMGVGLPYAMGIKMAHPDDDVVCI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 476 TGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAI-DHVAIAKACGCDGASVSDAA--- 551
Cdd:PRK06965 462 TGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVRQWQEIEYSKRYSHSYMDALpDFVKLAEAYGHVGMRIEKTSdve 541
|
570 580 590
....*....|....*....|....*....|....*
gi 504854683 552 -SLRQAMAAAERSpvpFVIDVKTEPS--AFPPISA 583
Cdd:PRK06965 542 pALREALRLKDRT---VFLDFQTDPTenVWPMVQA 573
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
29-580 |
2.48e-45 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 169.01 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQScPTALFLAADAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVT-GDSLNGLSDSLrrmgTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGPVVLLVSQDV 184
Cdd:PRK09124 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVAVVVLPGDV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTTACPQARPVAqdsdePLgRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVhlSGACDALARLQSLAGLPVATTNM 264
Cdd:PRK09124 164 ALKPAPERATPH-----WY-HAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 265 GKGAIDETHPLSLGVIGnAMGTRSpAKHFMdyvRSADFVLFVGT----RtnengtaswSLFPEQAQYAQIDIDSEEVGRN 340
Cdd:PRK09124 236 GKEHVEYDNPYDVGMTG-LIGFSS-GYHAM---MNCDTLLMLGTdfpyR---------QFYPTDAKIIQIDINPGSLGRR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 341 YG-AMRFAGDAAATLQALGDALQERGQavaaRRMaeLAPAFEACRQAhRAELAPYAQSDAS--PMRPE---RIMAELRAS 414
Cdd:PRK09124 302 SPvDLGLVGDVKATLAALLPLLEEKTD----RKF--LDKALEHYRKA-RKGLDDLAVPSDGgkPIHPQylaRQISEFAAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 415 hgDIIWVADASYSSIWLAQFIpcTQAGTRfvtpRGIAGLGWG-----VPMAIGAKIARPGARVICLTGDGGFAHCWAELE 489
Cdd:PRK09124 375 --DAIFTCDVGTPTVWAARYL--KMNGKR----RLLGSFNHGsmanaMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 490 TARRHEVPVTIVVLNNGVLGFqINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVI 569
Cdd:PRK09124 447 SLVQLKLPVKIVVFNNSVLGF-VAMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALV 525
|
570
....*....|...
gi 504854683 570 DVKTEPS--AFPP 580
Cdd:PRK09124 526 DVVTAKQelAMPP 538
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
31-560 |
1.88e-44 |
|
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: 166.58 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 31 AIADVLKAAGVAQIFG---QSCPTALFLAADAiGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSE 107
Cdd:TIGR03457 7 AFVEVLVANGVTHAFGimgSAFMDAMDLFPPA-GIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 108 ATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGPVVLLVSQDVLT- 186
Cdd:TIGR03457 86 AYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYFYg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 187 -TACPQARPVaqdsdeplgrfPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMG 265
Cdd:TIGR03457 165 eIDVEIPRPV-----------RLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 266 KGAIDETHPLSLGVIGnAMGTRSPakhfMDYVRSADFVLFVGTRTNENGTA---SWSLFPEQAQYAQIDIDSEEVGRNYG 342
Cdd:TIGR03457 234 NDSFPASHPLWVGPLG-YQGSKAA----MKLISDADVVLALGTRLGPFGTLpqyGIDYWPKNAKIIQVDANAKMIGLVKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 343 -AMRFAGDAAATLQAL--------GDALQ-ERGQAVAARRMA---ELAPAFEACRQAHRAELAPYAQSDASPMRPERIMA 409
Cdd:TIGR03457 309 vTVGICGDAKAAAAEIlqrlagkaGDANRaERKAKIQAERSAweqELSEMTHERDPFSLDMIVEQRQEEGNWLHPRQVLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 410 EL-RASHGDIIWVAD-ASYSSIwlAQFIPCTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAE 487
Cdd:TIGR03457 389 ELeKAMPEDAIVSTDiGNINSV--ANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504854683 488 LETARRHEVPVTIVVLNNGVLGF----QINAEESRF-GTHTDvchfGAIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:TIGR03457 467 IMTAVRHDIPVTAVVFRNRQWGAekknQVDFYNNRFvGTELE----SELSFAGIADAMGAKGVVVDKPEDVGPALKKA 540
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
26-571 |
2.07e-44 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 166.18 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 26 YQAANAIADVLKAAGVAQIFGqsCPTA----LFLAADAIGIRQIGYRTE-NAGAAMADgaarVGRqLT----VITAQNGP 96
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFG--IPGAkidrVFDALEDSGPELIVTRHEqNAAFMAAA----IGR-LTgkpgVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 97 AAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPV 176
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 177 VLLVSQDVlTTACPQARPVAQDSDEPLGRFPLDrtvpvagRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAG 256
Cdd:PRK08617 158 FVSLPQDV-VDAPVTSKAIAPLSKPKLGPASPE-------DINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 257 LPVATTNMGKGAIDETH-PLSLGVIG---NAMGTRspakhfmdYVRSADFVLFVGTRTNENGTASWSlFPEQAQYAQIDI 332
Cdd:PRK08617 230 LPVVETFQAAGVISRELeDHFFGRVGlfrNQPGDE--------LLKKADLVITIGYDPIEYEPRNWN-SEGDATIIHIDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 333 DSEEVGRNYG-AMRFAGDAAATLQALGDALQErgqavaaRRMAELAPAFEACRQAHRAELA-PYAQSDASPMRPERIMAE 410
Cdd:PRK08617 301 LPAEIDNYYQpERELIGDIAATLDLLAEKLDG-------LSLSPQSLEILEELRAQLEELAeRPARLEEGAVHPLRIIRA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 411 LRASHGDIIWVA-DASYSSIWLAQFIPCTQAGTRFVTpRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELE 489
Cdd:PRK08617 374 LQDIVTDDTTVTvDVGSHYIWMARYFRSYEPRHLLFS-NGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 490 TARRHEVPVTIVVLNNG---VLGFQinaEESRFGTHTDVcHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVP 566
Cdd:PRK08617 453 TAVRLKLNIVHIIWNDGhynMVEFQ---EEMKYGRSSGV-DFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGP 528
|
....*
gi 504854683 567 FVIDV 571
Cdd:PRK08617 529 VVIDI 533
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
29-574 |
5.26e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 165.27 E-value: 5.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK08527 6 SQMVCEALKEEGVKVVFGYPGGAILNIY-DEIykqnYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV 184
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTTacpqarpvaqdsdepLGRF--PLDRTVPV--------AGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSL 254
Cdd:PRK08527 165 TAT---------------LGEFeyPKEISLKTykptykgnSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 255 AGLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMDyvrSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDS 334
Cdd:PRK08527 230 TGIPAVETLMARGVLRSDDPLLLGMLG--MHGSYAANMAMS---ECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 335 EEVGR----NYgamRFAGDAAATLQALGDALQErgqavaarrmaELAPAFEACRQAHR--AELAP--YAQSDASpMRPER 406
Cdd:PRK08527 305 SSISKivnaDY---PIVGDLKNVLKEMLEELKE-----------ENPTTYKEWREILKryNELHPlsYEDSDEV-LKPQW 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 407 IMAELRASHGD-IIWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCW 485
Cdd:PRK08527 370 VIERVGELLGDdAIISTDVGQHQMWVAQFYPFNYP-RQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 486 AELETARRHEVPVTIVVLNNGVLG----FQINAEESRFgTHTDVChfGAIDHVAIAKACGCDGASVSDAASLRQAMAAAE 561
Cdd:PRK08527 449 QELMTAVEYKIPVINIILNNNFLGmvrqWQTFFYEERY-SETDLS--TQPDFVKLAESFGGIGFRVTTKEEFDKALKEAL 525
|
570
....*....|...
gi 504854683 562 RSPVPFVIDVKTE 574
Cdd:PRK08527 526 ESDKVALIDVKID 538
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
29-560 |
9.70e-44 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 164.70 E-value: 9.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK06882 7 AEMVVQSLRDEGVEYVFGYPGGSVLDIY-DAIhtlgGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDV 184
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTtacpqarPVAQDSDEPLGRFPLDRTVPVA----GRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVA 260
Cdd:PRK06882 166 VN-------PANKFTYEYPEEVSLRSYNPTVqghkGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 261 TTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRN 340
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLG--MHGTYEANNAM---HESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 341 YGA-MRFAGDAAATLQALGDALQERGqavAARRMAELAPAFEACRQAHRAELAPYAQSDASpMRPERIMAEL-RASHGDI 418
Cdd:PRK06882 314 VPAyIPIVGSAKNVLEEFLSLLEEEN---LAKSQTDLTAWWQQINEWKAKKCLEFDRTSDV-IKPQQVVEAIyRLTNGDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 419 IWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPV 498
Cdd:PRK06882 390 YVASDVGQHQMFAALHYPFDKP-RRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPV 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504854683 499 TIVVLNNGVLGFQINAEESRF-GTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:PRK06882 469 VIVSLNNRFLGMVKQWQDLIYsGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQA 531
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
19-581 |
9.55e-43 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 162.18 E-value: 9.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 19 ARQDLSAYQAANAIADVLKAAGVAQIFGQscPTALFLAA-DAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQ 93
Cdd:PRK09107 4 KSHMPRQMTGAEMVVQALKDQGVEHIFGY--PGGAVLPIyDEIfqqdDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 94 NGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKW---VRRIDvaeRAAEYTERAIRIATS 170
Cdd:PRK09107 82 SGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHnwlVKDVN---DLARVIHEAFHVATS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 171 GRPGPVVLLVSQDV---LTTACPQARPVAQDSDEPLGRFPldrtvpvAGRLAQLAQRLLDAKRPLVVAGGGVHLSG--AC 245
Cdd:PRK09107 159 GRPGPVVVDIPKDVqfaTGTYTPPQKAPVHVSYQPKVKGD-------AEAITEAVELLANAKRPVIYSGGGVINSGpeAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 246 DALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnaMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSLFPEQA 325
Cdd:PRK09107 232 RLLRELVELTGFPITSTLMGLGAYPASGKNWLGMLG--MHGTYEANMAM---HDCDVMLCVGARFDDRITGRLDAFSPNS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 326 QYAQIDIDSEEVGRNYGA-MRFAGDAAATLQALGDALQERGQAVAARRMAELAPAFEACRQahRAELApYAQSDASPMrP 404
Cdd:PRK09107 307 KKIHIDIDPSSINKNVRVdVPIIGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRA--RNSLA-YTPSDDVIM-P 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 405 ERIMAELRA--SHGDIIWVADASYSSIWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFA 482
Cdd:PRK09107 383 QYAIQRLYEltKGRDTYITTEVGQHQMWAAQFFGFEEP-NRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 483 HCWAELETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGAI-DHVAIAKACGCDGASVSDAASLRQA---MA 558
Cdd:PRK09107 462 MCIQEMSTAVQYNLPVKIFILNNQYMGMVRQWQQLLHGNRLSHSYTEAMpDFVKLAEAYGAVGIRCEKPGDLDDAiqeMI 541
|
570 580
....*....|....*....|...
gi 504854683 559 AAERsPVPFVIDVKTEPSAFPPI 581
Cdd:PRK09107 542 DVDK-PVIFDCRVANLENCFPMI 563
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
423-571 |
1.32e-42 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 150.04 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 423 DASYSSIWLAQFIPCTQaGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVV 502
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRP-PRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504854683 503 LNNGVLGFqINAEESRFG----THTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:pfam02775 80 LNNGGYGM-TRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
40-560 |
5.72e-42 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 159.63 E-value: 5.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 40 GVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSEATKASVPI 115
Cdd:PRK07979 18 GVKQVFGYPGGAVLDIY-DALhtvgGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 116 LAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVLTTA--CPQAR 193
Cdd:PRK07979 97 VVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPAnkLPYVW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 194 P--VAQDSDEPlgrfpldRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVhLSGACDA-LARLQSLAGLPVATTNMGKGAID 270
Cdd:PRK07979 177 PesVSMRSYNP-------TTQGHKGQIKRALQTLVAAKKPVVYVGGGA-INAACHQqLKELVEKLNLPVVSSLMGLGAFP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 271 ETHPLSLGVIGnaMGTRSPAKHFMdyvRSADFVLFVGTRTNENGTASWSLFPEQAQYAQIDIDSEEVGRNYGA-MRFAGD 349
Cdd:PRK07979 249 ATHRQSLGMLG--MHGTYEANMTM---HNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAdIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 350 AaatLQALGDALQERGQAVAARRMAELAPAFEACRQAHRAELAPYAQSDASpMRPERIMAEL-RASHGDIIWVADASYSS 428
Cdd:PRK07979 324 A---RQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEK-IKPQAVIETLwRLTKGDAYVTSDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 429 IWLAQFIPCTQAgTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVL 508
Cdd:PRK07979 400 MFAALYYPFDKP-RRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 504854683 509 GFQINAEESRF-GTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:PRK07979 479 GMVKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEA 531
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
218-357 |
2.45e-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: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 218 LAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGNAmGTRSPAKHfmdyV 297
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMH-GTPAANEA----L 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504854683 298 RSADFVLFVGTRTNE-NGTASWSLFPEQAQYAQIDIDSEEVGRNYGA-MRFAGDAAATLQAL 357
Cdd:pfam00205 76 EEADLVLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVdVPIVGDAKETLEAL 137
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
29-583 |
1.58e-39 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 152.45 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGqSCPTALFLAADAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYG-IVGDSLNPIVDAVrrtgGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLING 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATsGRPGPVVLLVSQDV 184
Cdd:PRK06546 85 LYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTLPGDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTtacpqaRPVAQDSDEPLGRFPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVhlSGACDALARLQSLAGLPVATTNM 264
Cdd:PRK06546 164 AD------EPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVGHSLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 265 GKGAIDETHPLSLGVIGnAMGTRSPAKHFMDyvrsADFVLFVGTrtnengTASWSLFPEQAQYAQIDIDSEEVGRNyGAM 344
Cdd:PRK06546 236 GKEWIQYDNPFDVGMSG-LLGYGAAHEAMHE----ADLLILLGT------DFPYDQFLPDVRTAQVDIDPEHLGRR-TRV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 345 RFA--GDAAATLQALGDALQER------GQAVA--ARRMAELAPAFEACRQAHRaelapyaqsdasPMRPE---RIMAEL 411
Cdd:PRK06546 304 DLAvhGDVAETIRALLPLVKEKtdrrflDRMLKkhARKLEKVVGAYTRKVEKHT------------PIHPEyvaSILDEL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 412 RAShgDIIWVADASYSSIWLAQFIpcTQAGTRfvtpRGIAGLGWG-----VPMAIGAKIARPGARVICLTGDGGFAHCWA 486
Cdd:PRK06546 372 AAD--DAVFTVDTGMCNVWAARYI--TPNGRR----RVIGSFRHGsmanaLPHAIGAQLADPGRQVISMSGDGGLSMLLG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 487 ELETARRHEVPVTIVVLNNGVLGF----QINAEESRFGthTDVCHFgaiDHVAIAKACGCDGASVSDAASLRQAMAAAER 562
Cdd:PRK06546 444 ELLTVKLYDLPVKVVVFNNSTLGMvkleMLVDGLPDFG--TDHPPV---DYAAIAAALGIHAVRVEDPKDVRGALREAFA 518
|
570 580
....*....|....*....|....
gi 504854683 563 SPVPFVIDVKTEPSAF---PPISA 583
Cdd:PRK06546 519 HPGPALVDVVTDPNALsipPTITG 542
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
163-574 |
4.68e-37 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 144.71 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 163 RAIRIATSGRPGPVVLLVSQDvlttacpqarpvaqDSDEPLGRFPlDRTVPVAGR-----LAQLAQRLLDAKRPLVVAGG 237
Cdd:PRK07092 151 RAYHIAMQPPRGPVFVSIPYD--------------DWDQPAEPLP-ARTVSSAVRpdpaaLARLGDALDAARRPALVVGP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 238 GVHLSGACDALARLQSLAGLPVATTNM-GKGAIDETHPLSLGVIGNAMGTRSPAkhfmdyVRSADFVLFVGT---RTNEN 313
Cdd:PRK07092 216 AVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPEDHPLFAGFLPASREKISAL------LDGHDLVLVIGApvfTYHVE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 314 GTASWslFPEQAQYAQIDIDSEEVGRNYGAMRFAGDAAATLQALGDALQERGQAVAARRmaelapafeacrqahraELAP 393
Cdd:PRK07092 290 GPGPH--LPEGAELVQLTDDPGEAAWAPMGDAIVGDIRLALRDLLALLPPSARPAPPAR-----------------PMPP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 394 YAQSDASPMRPERIMAELRASHG-DIIWVADASYSSIWLAQFIPCTQAGTRFVTPRGiaGLGWGVPMAIGAKIARPGARV 472
Cdd:PRK07092 351 PAPAPGEPLSVAFVLQTLAALRPaDAIVVEEAPSTRPAMQEHLPMRRQGSFYTMASG--GLGYGLPAAVGVALAQPGRRV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 473 ICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGfqinAEESrFGTHTDVCH-----FGAIDHVAIAKACGCDGASV 547
Cdd:PRK07092 429 IGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYG----ALRW-FAPVFGVRDvpgldLPGLDFVALARGYGCEAVRV 503
|
410 420
....*....|....*....|....*..
gi 504854683 548 SDAASLRQAMAAAERSPVPFVIDVKTE 574
Cdd:PRK07092 504 SDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
32-577 |
1.26e-36 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 143.97 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 32 IADVLKAAGVAQIFG-QSCP-TALFLAADAIGIRQIGYRTE----NAGAAMADGAARVGRQLTViTAQ---NGPAAALlv 102
Cdd:PRK09259 16 VIDALKLNGIDTIYGvVGIPiTDLARLAQAEGIRYIGFRHEqsagNAAAAAGFLTQKPGVCLTV-SAPgflNGLTALA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 103 agfsEATKASVPILAIVQEVPRANAD--KNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLV 180
Cdd:PRK09259 93 ----NATTNCFPMIMISGSSEREIVDlqQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 181 SQDVLTTACPqarpvAQDSDEPLGRF--PLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSLAGLP 258
Cdd:PRK09259 169 PAKVLAQTMD-----ADEALTSLVKVvdPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 259 VATTNMGKGAIDETHPLSlgvignAMGTRSPAkhfmdyVRSADFVLFVGTRTN---ENGTA-SWSlfpEQAQYAQIDIDS 334
Cdd:PRK09259 244 FLPMSMAKGLLPDTHPQS------AAAARSLA------LANADVVLLVGARLNwllSHGKGkTWG---ADKKFIQIDIEP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 335 EEVGRNYG-AMRFAGDAAATLQALGDALQERGQAVAARRMAELApafeACRQAHRAELAPYAQSDASPMRPERIMAELRA 413
Cdd:PRK09259 309 QEIDSNRPiAAPVVGDIGSVMQALLAGLKQNTFKAPAEWLDALA----ERKEKNAAKMAEKLSTDTQPMNFYNALGAIRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 414 ---SHGDIIWVADASYSSIWLAQFIPCTQAGTRF-VTPRGIAGLGWGvpMAIGAKIArPGARVICLTGDGGFAHCWAELE 489
Cdd:PRK09259 385 vlkENPDIYLVNEGANTLDLARNIIDMYKPRHRLdCGTWGVMGIGMG--YAIAAAVE-TGKPVVAIEGDSAFGFSGMEVE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 490 TARRHEVPVTIVVLNNGvlGFQINAEESRFGTH---TDVCHFGAiDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVP 566
Cdd:PRK09259 462 TICRYNLPVTVVIFNNG--GIYRGDDVNLSGAGdpsPTVLVHHA-RYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKP 538
|
570
....*....|.
gi 504854683 567 FVIDVKTEPSA 577
Cdd:PRK09259 539 TLINVVIDPAA 549
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
29-579 |
1.04e-35 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 141.12 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 29 ANAIADVLKAAGVAQIFGqsCP-TALFLAADAIGIRQIGY---RTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYG--IPgDSIDPLVDAIRKSKVKYvqvRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGPVVLLVSQDV 184
Cdd:PRK06457 83 LYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 185 LTTAcPQARPVaQDSDEPLGRFPLDrtvpvAGRLAQLAQRlldAKRPLVVAGGGVHlsGACDALARLQSLAGLPVATTNM 264
Cdd:PRK06457 162 LRKS-SEYKGS-KNTEVGKVKYSID-----FSRAKELIKE---SEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 265 GKGAIDETHPLSLGVIGnAMGTRsPAKHFMDyvrSADFVLFVGTrtnengTASWSLF-PEQAQYAQIDIDSEEVGRnyga 343
Cdd:PRK06457 230 GKGILPDLDPKVMGGIG-LLGTK-PSIEAMD---KADLLIMLGT------SFPYVNFlNKSAKVIQVDIDNSNIGK---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 344 mRFAGDAAATLQAlGDALQERGQAVAARRMAELapafEACRQAHRAELAPYAQSDASPMRPERIMAEL-RASHGDIIWVA 422
Cdd:PRK06457 295 -RLDVDLSYPIPV-AEFLNIDIEEKSDKFYEEL----KGKKEDWLDSISKQENSLDKPMKPQRVAYIVsQKCKKDAVIVT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 423 DASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGAR-VICLTGDGGFAHCWAELETARRHEVPVTIV 501
Cdd:PRK06457 369 DTGNVTMWTARHFRASGEQT-FIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKII 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504854683 502 VLNNGVLGFqINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPSAFP 579
Cdd:PRK06457 448 IYNNSKLGM-IKFEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERP 524
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
401-579 |
2.30e-35 |
|
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: 131.11 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 401 PMRPERIMAEL-RASHGDIIWVADASYSSIWLAQFIPCTqAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDG 479
Cdd:cd02014 1 PIHPERVAAELnKRAPDDAIFTIDVGNVTVWAARHLRMN-GKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 480 GFAHCWAELETARRHEVPVTIVVLNNGVLGFqINAEESRFGTHTDVCHFGAIDHVAIAKACGCDGASVSDAASLRQAMAA 559
Cdd:cd02014 80 GFAMLMGDLITAVKYNLPVIVVVFNNSDLGF-IKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDE 158
|
170 180
....*....|....*....|
gi 504854683 560 AERSPVPFVIDVKTEPSAFP 579
Cdd:cd02014 159 ALAADGPVVIDVVTDPNEPP 178
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
24-580 |
7.64e-35 |
|
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: 138.37 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 24 SAYQAANAIADVLKAAGVAQIFGqsCP---TALFLaaDAI----GIRQIGYRTENAGAAMADGAARVgrqltvitaqNGP 96
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFG--VPgdyNLPFL--DAIeahpGIRWVGCCNELNAGYAADGYARV----------NGL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 97 AAALL------------VAG-FSEatkaSVPILAIV----QEVPRANA---------DKNAFQEL-DHVqlfaSCAKWVr 149
Cdd:COG3961 69 GALVTtygvgelsaingIAGaYAE----RVPVVHIVgapgTRAQRRGPllhhtlgdgDFDHFLRMfEEV----TVAQAV- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 150 rIDvAERAAEYTERAIRIATSGRPgPVVLLVSQDVLTTACPQARPVAQDSDEPLGRFPLDRTVpvagrlAQLAQRLLDAK 229
Cdd:COG3961 140 -LT-PENAAAEIDRVLAAALREKR-PVYIELPRDVADAPIEPPEAPLPLPPPASDPAALAAAV------AAAAERLAKAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 230 RPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGNAMGtRSPAKhfmDYVRSADFVLFVGTR 309
Cdd:COG3961 211 RPVILAGVEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTYAGAAS-SPEVR---EYVENADCVLCLGVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 310 TNENGTASWSLFPEQAQyaQIDIDSEEVgrnygamRFAGDAAATLqALGDALqergqavaaRRMAELAPAFEACRQAHRA 389
Cdd:COG3961 287 FTDTNTGGFTAQLDPER--TIDIQPDSV-------RVGGHIYPGV-SLADFL---------EALAELLKKRSAPLPAPAP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 390 ELAPYAQSDASPMRPERIMAELRA--SHGDIIwVADASySSIWLAQFIPcTQAGTRFVTPRGIAGLGWGVPMAIGAKIAR 467
Cdd:COG3961 348 PPPPPPAAPDAPLTQDRLWQRLQAflDPGDIV-VADTG-TSLFGAADLR-LPEGATFIAQPLWGSIGYTLPAALGAALAA 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 468 PGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLGFQ--INAEESRFgthTDVchfGAIDHVAIAKACGCD-- 543
Cdd:COG3961 425 PDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIEraIHGPDGPY---NDI---ANWDYAKLPEAFGGGna 498
|
570 580 590
....*....|....*....|....*....|....*....
gi 504854683 544 -GASVSDAASLRQAMAAAERSP-VPFVIDVKTEPSAFPP 580
Cdd:COG3961 499 lGFRVTTEGELEEALAAAEANTdRLTLIEVVLDKMDAPP 537
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
86-581 |
8.02e-34 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 136.19 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 86 QLTVITAQNGPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCA-KWVRRIDVAERAAEYTERA 164
Cdd:PRK08273 67 EVGVCLATSGPGAIHLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAgAFVQMVTVPEQLRHLVDRA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 165 IRIATSGRpGPVVLLVSQDVlttacpqarpvaQDSD-EPLGR----------FPLDRTVPVAGRLAQLAQRLLDAKRPLV 233
Cdd:PRK08273 147 VRTALAER-TVTAVILPNDV------------QELEyEPPPHahgtvhsgvgYTRPRVVPYDEDLRRAAEVLNAGRKVAI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 234 VAGGGVHlsGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGnAMGTRsPAKHFMdyvRSADFVLFVGTrtnen 313
Cdd:PRK08273 214 LVGAGAL--GATDEVIAVAERLGAGVAKALLGKAALPDDLPWVTGSIG-LLGTK-PSYELM---RECDTLLMVGS----- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 314 gTASWSLF-PE--QAQYAQIDIDseevGRNYGaMRF------AGDAAATLQALGDALQERgQAVAARRMAElapafEACR 384
Cdd:PRK08273 282 -SFPYSEFlPKegQARGVQIDID----GRMLG-LRYpmevnlVGDAAETLRALLPLLERK-KDRSWRERIE-----KWVA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 385 QAHRaELAPYAQSDASPMRPERIMAEL--RASHGDIIwVADASYSSIWLAQFI------PCTQAGTrfvtprgIAGLGWG 456
Cdd:PRK08273 350 RWWE-TLEARAMVPADPVNPQRVFWELspRLPDNAIL-TADSGSCANWYARDLrmrrgmMASLSGT-------LATMGPA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 457 VPMAIGAKIARPGARVICLTGDGGF-----------AHCWAELETARrhevpVTIVVLNNGVLGfQINAE------ESRF 519
Cdd:PRK08273 421 VPYAIAAKFAHPDRPVIALVGDGAMqmngmaelitvAKYWRQWSDPR-----LIVLVLNNRDLN-QVTWEqrvmegDPKF 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504854683 520 GTHTDVCHFgaiDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPsAFPPI 581
Cdd:PRK08273 495 EASQDLPDV---PYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDP-NVPPL 552
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
146-560 |
5.20e-33 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 133.59 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 146 KWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQDVLTTACPQARPvaqdsdePLGRF-PLDRTVPVAGRLAQLAQR 224
Cdd:PRK08327 144 KWDYEIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKA-------DAGRQmAPAPPAPDPEDIARAAEM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 225 LLDAKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGNAMgtrspakhfmdyVRSADFVL 304
Cdd:PRK08327 217 LAAAERPVIITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRAD------------LAEADLVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 305 FVGTRtnengtASWS----LFPEQAQYAQIDID---SEEVGRNYGA-MRFAGDAAATLQALGDALQERGQAVAARRMAEL 376
Cdd:PRK08327 285 VVDSD------VPWIpkkiRPDADARVIQIDVDplkSRIPLWGFPCdLCIQADTSTALDQLEERLKSLASAERRRARRRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 377 APAFEACRQAHRAEL-APYAQSDASPMRPERIMA---ELRASHGDIIwvadASYSSIWlaQFIPCTQAGTRFVTPRGiAG 452
Cdd:PRK08327 359 AAVRELRIRQEAAKRaEIERLKDRGPITPAYLSYclgEVADEYDAIV----TEYPFVP--RQARLNKPGSYFGDGSA-GG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 453 LGWGVPMAIGAKIARPGARVICLTGDGG--FAHCWAELETARRHEVPVTIVVLNNG--------VLGFQINAEESRFGTH 522
Cdd:PRK08327 432 LGWALGAALGAKLATPDRLVIATVGDGSfiFGVPEAAHWVAERYGLPVLVVVFNNGgwlavkeaVLEVYPEGYAARKGTF 511
|
410 420 430
....*....|....*....|....*....|....*....
gi 504854683 523 TDVcHFG-AIDHVAIAKACGCDGASVSDAASLRQAMAAA 560
Cdd:PRK08327 512 PGT-DFDpRPDFAKIAEAFGGYGERVEDPEELKGALRRA 549
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
31-182 |
1.59e-31 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 119.56 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 31 AIADVLKAAGVAQIFGQSCPTALFL--AADAIGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAGFSEA 108
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLldALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLANA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504854683 109 TKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQ 182
Cdd:cd07035 82 YLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
404-581 |
1.59e-31 |
|
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: 120.68 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 404 PERIMAEL-RASHGDIIWVADASYSSIWLAQFIPCTQAGTrFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFA 482
Cdd:cd02015 3 PQEVIKELsELTPGDAIVTTDVGQHQMWAAQYYRFKKPRS-WLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 483 HCWAELETARRHEVPVTIVVLNNGVLG----FQ-INAEESRFGTHTDVChfgaIDHVAIAKACGCDGASVSDAASLRQAM 557
Cdd:cd02015 82 MNIQELATAAQYNLPVKIVILNNGSLGmvrqWQeLFYEGRYSHTTLDSN----PDFVKLAEAYGIKGLRVEKPEELEAAL 157
|
170 180
....*....|....*....|....*.
gi 504854683 558 AAAERSPVPFVIDVKTEPSA--FPPI 581
Cdd:cd02015 158 KEALASDGPVLLDVLVDPEEnvLPMV 183
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
28-190 |
4.01e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 118.88 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQSCPTALFL---AADAIGIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVAG 104
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLldaLAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 105 FSEATKASVPILAIVQEVPRANADKNAFQ-ELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPGPVVLLVSQD 183
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*..
gi 504854683 184 VLTTACP 190
Cdd:pfam02776 161 VLLEEVD 167
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
417-574 |
3.36e-29 |
|
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: 113.78 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 417 DIIWVADASYSSIWLAQFIPCTQAGTRfVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEV 496
Cdd:cd02004 15 DAIIVSDGGNTMDWARYILRPRKPRHR-LDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGMELETAVRYNL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504854683 497 PVTIVVLNNGVLGFQINAEESRFGTHTDVCHFGA-IDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTE 574
Cdd:cd02004 94 PIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPdTRYDLVAEAFGGKGELVTTPEELKPALKRALASGKPALINVIID 172
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
402-573 |
1.67e-28 |
|
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: 111.92 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 402 MRPERIMAELRAS-HGDIIWVADASYSSIWLAQFIPCTQAGTRFvTPRGiAGLGWGVPMAIGAKIARPGARVICLTGDGG 480
Cdd:cd02002 1 LTPEYLAAALAAAlPEDAIIVDEAVTNGLPLRDQLPLTRPGSYF-TLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 481 FAHCWAELETARRHEVPVTIVVLNNGvlGFQI-NAEESRFGTHTDVC--------HFGAIDHVAIAKACGCDGASVSDAA 551
Cdd:cd02002 79 FMYTIQALWTAARYGLPVTVVILNNR--GYGAlRSFLKRVGPEGPGEnapdgldlLDPGIDFAAIAKAFGVEAERVETPE 156
|
170 180
....*....|....*....|..
gi 504854683 552 SLRQAMAAAERSPVPFVIDVKT 573
Cdd:cd02002 157 ELDEALREALAEGGPALIEVVV 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
404-571 |
3.87e-27 |
|
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: 108.14 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 404 PERIMAELRASHG-DIIWVADASYSSIWLAQFIPCTQAGTRFVTpRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFA 482
Cdd:cd02010 1 PQRIVHDLRAVMGdDDIVLLDVGAHKIWMARYYRTYAPNTCLIS-NGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 483 HCWAELETARRHEVPVTIVVLNNGVLGFQINAEESRFGTHTDVcHFGAIDHVAIAKACGCDGASVSDAASLRQAMAAAER 562
Cdd:cd02010 80 MNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGV-DFGNPDFVKYAESFGAKGYRIESADDLLPVLERALA 158
|
....*....
gi 504854683 563 SPVPFVIDV 571
Cdd:cd02010 159 ADGVHVIDC 167
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
398-574 |
1.48e-20 |
|
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: 90.03 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 398 DASPMRPERIMAELRASHG-DIIWVADASYSSIWLAQF---------IPCTQAGTrfvtprgiagLGWGVPMAIGAKIAR 467
Cdd:cd02006 4 DDVPIKPQRVYEEMNKAFGrDVRYVTTIGLSQIAGAQMlhvykprhwINCGQAGP----------LGWTVPAALGVAAAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 468 PGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGVLG------------FQINAEESRFGThTDVCHFGaIDHVA 535
Cdd:cd02006 74 PDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGlirqaqrafdmdYQVNLAFENINS-SELGGYG-VDHVK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504854683 536 IAKACGCDGASVSD----AASLRQAMAAAERSPVPFVIDVKTE 574
Cdd:cd02006 152 VAEGLGCKAIRVTKpeelAAAFEQAKKLMAEHRVPVVVEAILE 194
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
28-184 |
1.56e-18 |
|
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: 82.98 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 28 AANAIADVLKAAGVAQIFGQSCPTALFLAaDAI----GIRQIGYRTENAGAAMADGAARVGRQLTVITAQNGPAAALLVA 103
Cdd:cd07039 2 VADVIVETLENWGVKRVYGIPGDSINGLM-DALrregKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 104 GFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRpGPVVLLVSQD 183
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
.
gi 504854683 184 V 184
Cdd:cd07039 160 V 160
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
453-575 |
8.23e-17 |
|
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: 79.27 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 453 LGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGvlGFQ-INA-EES----RFGTHTDVC 526
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNH--GFGcINNlQEStgsgSFGTEFRDR 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504854683 527 HFGA---------IDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKTEP 575
Cdd:cd02003 128 DQESgqldgallpVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTDP 185
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
96-571 |
2.46e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 82.20 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 96 PAAALL---------VAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIR 166
Cdd:PRK07586 65 PAATLLhlgpglangLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 167 IATSGRPGPVVLLVSQDVLTTACPQARPVAQdsdeplgrfPLDRTVPVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACD 246
Cdd:PRK07586 145 AARGAPGQVATLILPADVAWSEGGPPAPPPP---------APAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 247 ALARLQSLAGLPVATtnmgkgaidETHPLSLgvignAMGTRSPAKHFMDYV--------RSADFVLFVGTRtnengtasw 318
Cdd:PRK07586 216 AAARIAAATGARLLA---------ETFPARM-----ERGAGRPAVERLPYFaeqalaqlAGVRHLVLVGAK--------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 319 slfPEQAQYAQIDIDSEEVGRNYGAMRFAG---DAAATLQALGDALQERGQAVAARRMAELAPAfeacrqahRAELAPYA 395
Cdd:PRK07586 273 ---APVAFFAYPGKPSRLVPEGCEVHTLAGpgeDAAAALEALADALGAKPAAPPLAAPARPPLP--------TGALTPEA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 396 QSDAspmrperIMAELRAshGDIiwVADASYSSIWLaqFIPCTQAGTR--FVTPRGIAgLGWGVPMAIGAKIARPGARVI 473
Cdd:PRK07586 342 IAQV-------IAALLPE--NAI--VVDESITSGRG--FFPATAGAAPhdWLTLTGGA-IGQGLPLATGAAVACPDRKVL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 474 CLTGDGGFAHCWAELETARRHEVPVTIVVLNNGvlGFQI-NAEESRFG------THTDVCHFG--AIDHVAIAKACGCDG 544
Cdd:PRK07586 408 ALQGDGSAMYTIQALWTQARENLDVTTVIFANR--AYAIlRGELARVGagnpgpRALDMLDLDdpDLDWVALAEGMGVPA 485
|
490 500
....*....|....*....|....*..
gi 504854683 545 ASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:PRK07586 486 RRVTTAEEFADALAAALAEPGPHLIEA 512
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
416-580 |
2.08e-13 |
|
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: 68.71 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 416 GDIIwVADA--SYSSIWLAQFIPctqaGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELETARR 493
Cdd:cd02005 18 NDIL-VAETgtSWFGALDLKLPK----GTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 494 HEVPVTIVVLNNGvlGF----QINAEESRFgthTDVCHFgaiDHVAIAKACGCDGAS----VSDAASLRQAMAAAERSP- 564
Cdd:cd02005 93 YGLNPIIFLINND--GYtierAIHGPEASY---NDIANW---NYTKLPEVFGGGGGGlsfrVKTEGELDEALKDALFNRd 164
|
170
....*....|....*.
gi 504854683 565 VPFVIDVKTEPSAFPP 580
Cdd:cd02005 165 KLSLIEVILPKDDAPE 180
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
400-580 |
2.49e-13 |
|
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: 69.08 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 400 SPMRPERIMAELRASHGDIIWVADASYSSIWLAQFIPCTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGARVICLTGDG 479
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 480 GFAHCWAELETARRHEVPVTIVVLNNGVLG----FQINAEESRF-GTHTDVCHFgaidhVAIAKACGCDGASVSDAASLR 554
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGaekkNQVDFYNNRFvGTELESESF-----AKIAEACGAKGITVDKPEDVG 156
|
170 180
....*....|....*....|....*....
gi 504854683 555 QAMA---AAERSPVPFVIDVKTEPSAFPP 580
Cdd:cd02013 157 PALQkaiAMMAEGKTTVIEIVCDQELGDP 185
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
95-570 |
4.58e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 62.20 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 95 GPAAALLVAGFSEATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGRPG 174
Cdd:PRK12474 77 GPGLANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 175 PVVLLVSQDVLTTACPQARPVAQDsdepLGRFPLdrtvpVAGRLAQLAQRLLDAKRPLVVAGGGVHLSGACDALARLQSL 254
Cdd:PRK12474 157 IATLIMPADVAWNEAAYAAQPLRG----IGPAPV-----AAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 255 AGLPVattnMGKGAIDETHplsLGViGNAMGTRSPAKH--FMDYVRSADFVLFVGTRTNEN-----GTASWsLFPEQAQY 327
Cdd:PRK12474 228 TGVRL----YCDTFAPRIE---RGA-GRVPIERIPYFHeqITAFLKDVEQLVLVGAKPPVSffaypGKPSW-GAPPGCEI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 328 AQIDIDSEevgrnygamrfagDAAATLQALGDALQERGQAVAARRMAELAPAFEACRQAHRAelapyaqsdaspmrpeRI 407
Cdd:PRK12474 299 VYLAQPDE-------------DLAQALQDLADAVDAPAEPAARTPLALPALPKGALNSLGVA----------------QL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 408 MAELRASHGdiIWVADASYSSIwlaqFIPCTQAGTRFVTPRGIAG--LGWGVPMAIGAKIARPGARVICLTGDGGFAHCW 485
Cdd:PRK12474 350 IAHRTPDQA--IYADEALTSGL----FFDMSYDRARPHTHLPLTGgsIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTM 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 486 AELETARRHEVPVTIVVLNNGVLGFqINAEESRFGTHTD--------VCHFGAIDHVAIAKACGCDGASVSDAASLRQAM 557
Cdd:PRK12474 424 QALWTMARENLDVTVVIFANRSYAI-LNGELQRVGAQGAgrnalsmlDLHNPELNWMKIAEGLGVEASRATTAEEFSAQY 502
|
490
....*....|...
gi 504854683 558 AAAERSPVPFVID 570
Cdd:PRK12474 503 AAAMAQRGPRLIE 515
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
427-573 |
2.15e-09 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 56.83 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 427 SSIWLAQ-FIPCTQAGTRFVTPRGIAGLGWGVPMAIGAKIARPGaRVICLTGDGGFAHCWAELETARRHEVPVTIVVLNN 505
Cdd:cd02009 26 MPIRDLDlFALPSDKTVRVFANRGASGIDGTLSTALGIALATDK-PTVLLTGDLSFLHDLNGLLLGKQEPLNLTIVVINN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504854683 506 GvlGFQI------NAEESRFGThtdvcHFGA---IDHVAIAKACGCDGASVSDAASLRQAMAAAERSPVPFVIDVKT 573
Cdd:cd02009 105 N--GGGIfsllpqASFEDEFER-----LFGTpqgLDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
228-515 |
7.28e-09 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 58.56 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 228 AKRPLVVAGGGVHLSGACDALARLQSLAGLPVATTNMGKGAIDETHPLSLGVIGNAMGTRSPAkhfmDYVRSADFVLFVG 307
Cdd:PLN02573 224 AVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCA----EIVESADAYLFAG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 308 TRTNENGTASWSLF--PEQAqyaqIDIDSEEV----GRNYGAMRFAGdaaaTLQALgdalqergqavaARRMAELAPAFE 381
Cdd:PLN02573 300 PIFNDYSSVGYSLLlkKEKA----IIVQPDRVtignGPAFGCVLMKD----FLEAL------------AKRVKKNTTAYE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 382 ACRQAHRAELAPYAQSDASPMRP----ERIMAELRASHGDIIWVADASYSSIWLAQFIPCtqaGTRFVTPRGiaGLGWGV 457
Cdd:PLN02573 360 NYKRIFVPEGEPLKSEPGEPLRVnvlfKHIQKMLSGDTAVIAETGDSWFNCQKLKLPEGC---GYEFQMQYG--SIGWSV 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 504854683 458 PMAIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTIVVLNNGvlGFQINAE 515
Cdd:PLN02573 435 GATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNG--GYTIEVE 490
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
453-574 |
4.01e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 53.68 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 453 LGWGVPMAIGAKIARPGARVICLTGDGGFAHCWAELET-ARRHEVPVTIVVLNNGVlgFQINAEESRFGTHTdvchfgaI 531
Cdd:PRK06163 59 MGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGV--YQITGGQPTLTSQT-------V 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504854683 532 DHVAIAKACGC-DGASVSDAASLRQAMAAAERSPVPFVIDVKTE 574
Cdd:PRK06163 130 DVVAIARGAGLeNSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
460-580 |
8.86e-07 |
|
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: 49.62 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 460 AIGAKIARPGARVICLTGDGGFAHCWAELETARRHEVPVTI-VVLNNGV---LGFQINAeesrfGTHTDVChfgaidhvA 535
Cdd:cd03371 57 ALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIhIVLNNGAhdsVGGQPTV-----SFDVSLP--------A 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504854683 536 IAKACG-CDGASVSDAASLRQAMAAAERSPVPFVIDVKTEPSAFPP 580
Cdd:cd03371 124 IAKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKVRPGSRSD 169
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
458-575 |
1.66e-06 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 48.44 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 458 PMAIGAKIARPgARVICLTGDGGFAHCWAELETARRHEVP-VTIVVLNNGVLGFQINAEesrfgTHTDVChfgaIDHVAI 536
Cdd:cd03372 49 SIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIAAEKPKnLIIVVLDNGAYGSTGNQP-----THAGKK----TDLEAV 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 504854683 537 AKACGCDGAS-VSDAASLRQAMaaAERSPVPFVIDVKTEP 575
Cdd:cd03372 119 AKACGLDNVAtVASEEAFEKAV--EQALDGPSFIHVKIKP 156
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
31-179 |
1.91e-06 |
|
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: 48.11 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 31 AIADVLKAAGVAQIFG----QSCPTALFLAADAiGIRQIGYRTENAGAAMADGAARVGRQLTVITAqNGPAAALLVAGFS 106
Cdd:cd06586 2 AFAEVLTAWGVRHVFGypgdEISSLLDALREGD-KRIIDTVIHELGAAGAAAGYARAGGPPVVIVT-SGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504854683 107 EATKASVPILAIVQEVPRANADKNAFQELDHVQLFASCAKWVRRIDVAERAAEYTERAIRIATSGrPGPVVLL 179
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVR 151
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
454-571 |
2.66e-06 |
|
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: 48.29 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 454 GWGVPMAIGAKIARPGARVICLTGDG-----GFAHCwaeLETARRHeVPVTIVVLNNGVLGF---QInAEESRFGTHTDV 525
Cdd:cd03375 54 GRALAVATGVKLANPDLTVIVVSGDGdlaaiGGNHF---IHAARRN-IDITVIVHNNQIYGLtkgQA-SPTTPEGFKTKT 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 504854683 526 CHFGAIDH----VAIAKACGCD---GASVSDAASLRQAMAAAERSPVPFVIDV 571
Cdd:cd03375 129 TPYGNIEEpfnpLALALAAGATfvaRGFSGDIKQLKEIIKKAIQHKGFSFVEV 181
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
458-560 |
1.62e-05 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 47.14 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 458 PMAIGAKIARPGARVICLTGDG-GFA-------HcwaeleTARRHeVPVTIVVLNN---GVLGFQINAeESRFGTHTDVC 526
Cdd:PRK11867 76 AIATGLKLANPDLTVIVVTGDGdALAiggnhfiH------ALRRN-IDITYILFNNqiyGLTKGQYSP-TSPVGFVTKTT 147
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 504854683 527 HFGAIDH----VAIAKACGCDG---ASVSDAASLRQAMAAA 560
Cdd:PRK11867 148 PYGSIEPpfnpVELALGAGATFvarGFDSDVKQLTELIKAA 188
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
453-569 |
1.90e-05 |
|
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: 45.35 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 453 LGWGVPMAIGAKIARPGARVICLTGDGGFAHCW--AELETARRHeVPVTIVVLNNGVL---GFQINAEESRFGTHTDvch 527
Cdd:cd02008 53 MGASIGVAIGMAKASEDKKVVAVIGDSTFFHSGilGLINAVYNK-ANITVVILDNRTTamtGGQPHPGTGKTLTEPT--- 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504854683 528 fGAIDHVAIAKACGCDGASVSDAASL---RQAMAAAERSPVPFVI 569
Cdd:cd02008 129 -TVIDIEALVRAIGVKRVVVVDPYDLkaiREELKEALAVPGVSVI 172
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
435-541 |
2.49e-05 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 46.29 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 435 IPCTQAGTRFVTPRGIAGL-GWGVPMAIGAKIARPGARVICLTGDG-GFAHCWAELETARRHEVPVTIVVLNNGVLGF-- 510
Cdd:PRK11866 42 IGCSSNLPEFLNTYGIHGIhGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYGLtt 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 504854683 511 -QINAEESRfGTHTDVCHFGAIDH----VAIAKACG 541
Cdd:PRK11866 122 gQASPTTPR-GVKTKTTPDGNIEEpfnpIALALAAG 156
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
458-542 |
4.66e-05 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 45.64 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 458 PMAIGAKIARPGARVICLTGDG-----G---FAHcwaeletARRHEVPVTIVVLNNGVLGF---QINAeESRFGTHT--- 523
Cdd:PRK05778 77 AFATGAKLANPDLEVIVVGGDGdlasiGgghFIH-------AGRRNIDITVIVENNGIYGLtkgQASP-TTPEGSKTkta 148
|
90 100
....*....|....*....|
gi 504854683 524 -DVCHFGAIDHVAIAKACGC 542
Cdd:PRK05778 149 pYGNIEPPIDPCALALAAGA 168
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
452-573 |
1.59e-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: 40.57 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504854683 452 GLGWGVPMAIGAKIARPGARVICLTGDGgfahCWAE------LETARRHEV-PVTIVVLNNgvlGFQInaeesrFGTHTD 524
Cdd:cd02012 110 GLSVAVGMALAEKLLGFDYRVYVLLGDG----ELQEgsvweaASFAGHYKLdNLIAIVDSN---RIQI------DGPTDD 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504854683 525 VCHFGaiDHVAIAKACG-----CDGasvSDAASLRQAMAAAERSP-VPFVIDVKT 573
Cdd:cd02012 177 ILFTE--DLAKKFEAFGwnvieVDG---HDVEEILAALEEAKKSKgKPTLIIAKT 226
|
|
| |
