|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
3-544 |
0e+00 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 854.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGgLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADTGFIHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIQGAKIPLSLVTAPVKPAsVSPVDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADAGITVISSTHARG 241
Cdd:PRK07064 161 VEIPIDIQAAEIELPDDLAPVHVA-VPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLGFGVVTSTQGRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 242 VLPDSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRVQIDIDPAAASRNYLMDNTLVADCSALL 321
Cdd:PRK07064 240 VVPEDHPASLGAFNNSAAVEALYKTCDLLLVVGSRLRGNETLKYSLALPRPLIRVDADAAADGRGYPNDLFVHGDAARVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 322 SALAEKAQGREWGNAQWDGLVQEAVTQAERGLREQCGVYAQLNDAIEKALPEDGLLVRDITVSGSLWGSRLFRARGPLMN 401
Cdd:PRK07064 320 ARLADRLEGRLSVDPAFAADLRAAREAAVADLRKGLGPYAKLVDALRAALPRDGNWVRDVTISNSTWGNRLLPIFEPRAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 402 IHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYY 481
Cdd:PRK07064 400 VHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRYY 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863665 482 NELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRMGQIGALK--FAGPPQKT 544
Cdd:PRK07064 480 VELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLSIGPFAaaFAGPPVKK 544
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
3-529 |
2.03e-135 |
|
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: 404.16 E-value: 2.03e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDadTGFIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIG--RGAFQEV-DQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIQGAKIPLSLVTAPVKPASVSPV-DVGSVNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISST 237
Cdd:COG0028 158 LDIPKDVQAAEAEEEPAPPELRGYRPRPApDPEAIEEAAELLAAAKRPVilAGGGARRAGAAEELRALAERlGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HARGVLPDSHRASLRAF--HNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPR-VQIDIDPAAASRNYLMDNTLV 314
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLgmHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKiIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 315 ADCSALLSALAEKAQGREWGNAQWDGLVQEAVTQAERGLREQCGV--YAQLNDAIEKALPEDGLLVRDITvSGSLWGSRL 392
Cdd:COG0028 318 GDAKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAAYAADDGPikPQRVIAALREALPDDAIVVTDVG-QHQMWAARY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 393 FRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQ 471
Cdd:COG0028 397 LRFRRPRRFLTSGGlGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQ 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863665 472 DKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:COG0028 477 ELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRV 534
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-530 |
2.88e-74 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 245.31 E-value: 2.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMiTVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGN-IRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAG 78
Cdd:PRK08266 1 MTTM-TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGrPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 79 AGNAVGALVEAMNACTPLLHLTGQVEKAWLDADTGFIHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCG 158
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 159 PVSVEIPIDIQGAKIPLSLVTaPVKPASVSPVDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADA-GITVISST 237
Cdd:PRK08266 160 PVALEMPWDVFGQRAPVAAAP-PLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMlQAPVVAFR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HARGVLPDSHRASLrafhNSPSVEALIAQCDFTLIAGSRLrsnetrswtlELPSPR----------VQIDIDPAAASRnY 307
Cdd:PRK08266 239 SGRGIVSDRHPLGL----NFAAAYELWPQTDVVIGIGSRL----------ELPTFRwpwrpdglkvIRIDIDPTEMRR-L 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 308 LMDNTLVADCSALLSALAE-------KAQGREWG----NAQWDGLVQEAVTQAErglreqcgvYAQlndAIEKALPEDGL 376
Cdd:PRK08266 304 KPDVAIVADAKAGTAALLDalskagsKRPSRRAElrelKAAARQRIQAVQPQAS---------YLR---AIREALPDDGI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 377 LVRDITVSGslWGSRL-FRARGPLMNIHS-LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANV 454
Cdd:PRK08266 372 FVDELSQVG--FASWFaFPVYAPRTFVTCgYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863665 455 TLLIMNDGGYGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRMG 530
Cdd:PRK08266 450 VTVVFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVP 525
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-531 |
1.05e-59 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 206.36 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVISIHNLPIadavgQRG----NIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAG 78
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVEL-----YRGlagsGIRHVTPRHEQGAGFMADGYARVSGKpGVCFIITGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 79 AGNAVGALVEAMNACTPLLHLTGQVEKAWLDADTGFIHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCG 158
Cdd:PRK07524 76 MTNIATAMGQAYADSIPMLVISSVNRRASLGKGRGKLHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 159 PVSVEIPIDIQGAKIPlSLVTAPVKPASVSPVDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADA-GITVISST 237
Cdd:PRK07524 156 PVHIEIPLDVLAAPAD-HLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERlDAPVALTI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HARGVLPDSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNE---TRSWTLELPSPRVQIDIDPAAASRNYLMDNTLV 314
Cdd:PRK07524 235 NAKGLLPAGHPLLLGASQSLPAVRALIAEADVVLAVGTELGETDydvYFDGGFPLPGELIRIDIDPDQLARNYPPALALV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 315 ADC----SALLSALAEKAQGREWGNAQwdglvQEAVTQAER-GLREQCGVYAQLNDAIEKALPeDGLLVRDIT---VSGS 386
Cdd:PRK07524 315 GDAraalEALLARLPGQAAAADWGAAR-----VAALRQALRaEWDPLTAAQVALLDTILAALP-DAIFVGDSTqpvYAGN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 387 LwgsrLFRARGP--LMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGY 464
Cdd:PRK07524 389 L----YFDADAPrrWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 465 GVMRgiqdKYFGGRQYYNE---LHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRMGQ 531
Cdd:PRK07524 465 GEIR----RYMVARDIEPVgvdPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
365-529 |
2.29e-51 |
|
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: 173.21 E-value: 2.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 365 DAIEKALPEDGLLVRDITVSGSLWGSRLFRARGPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGEL 444
Cdd:cd00568 4 AALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 445 ATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSV 524
Cdd:cd00568 84 ATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGPAL 163
|
....*
gi 502863665 525 VEVRM 529
Cdd:cd00568 164 IEVKT 168
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-526 |
9.47e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 169.38 E-value: 9.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGnIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADtGFihETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKD-GF--QEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIQGAKIPL---SLVTAPVKPASVSPvDVGSVNALWAQLKQAKQPLLWLG--GGALGCADAVKKLA-DAGITVIS 235
Cdd:PRK06725 169 IDIPKDVQNEKVTSfynEVVEIPGYKPEPRP-DSMKLREVAKAISKAKRPLLYIGggVIHSGGSEELIEFArENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 236 STHARGVLP--DSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSwtLELPSP---RVQIDIDPAAASRNYLMD 310
Cdd:PRK06725 248 TLMGLGAYPpgDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGK--LELFSPhskKVHIDIDPSEFHKNVAVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 311 NTLVADCSALLSALAEKA---QGREWGNA--QWDGLVQEAVTQAERGLREQcgvyaQLNDAIEKALPEDGLLVRDITvSG 385
Cdd:PRK06725 326 YPVVGDVKKALHMLLHMSihtQTDEWLQKvkTWKEEYPLSYKQKESELKPQ-----HVINLVSELTNGEAIVTTEVG-QH 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 386 SLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGY 464
Cdd:PRK06725 400 QMWAAHFYKAKNPRTFLTSGGlGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863665 465 GVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVE 526
Cdd:PRK06725 480 GMVRQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVD 541
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-529 |
9.78e-46 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 168.90 E-value: 9.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGA 79
Cdd:PRK08199 4 TPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRpGICFVTRGPGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQVEKAWLDADtGFihETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGP 159
Cdd:PRK08199 84 TNASIGVHTAFQDSTPMILFVGQVARDFRERE-AF--QEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 160 VSVEIPIDI--QGAKIPLSLVTAPVKPAsVSPVDVGSVNALwaqLKQAKQPLLWLGGGALGcADAVKKLAD----AGITV 233
Cdd:PRK08199 161 VVLALPEDVlsETAEVPDAPPYRRVAAA-PGAADLARLAEL---LARAERPLVILGGSGWT-EAAVADLRAfaerWGLPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 234 ISSTHARGVLPdsHRASLRAFH----NSPSVEALIAQCDFTLIAGSRLRSNETRSWTL-ELPSPR---VQIDIDPAAASR 305
Cdd:PRK08199 236 ACAFRRQDLFD--NRHPNYAGDlglgINPALAARIREADLVLAVGTRLGEVTTQGYTLlDIPVPRqtlVHVHPDAEELGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 306 NYLMDNTLVADCSALLSALAEKAQG-----REWGNAQWDGLVQEAVTQAERGLREQCGVYAQLNDAiekaLPEDGLLVRD 380
Cdd:PRK08199 314 VYRPDLAIVADPAAFAAALAALEPPaspawAEWTAAAHADYLAWSAPLPGPGAVQLGEVMAWLRER----LPADAIITNG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 381 itvSG--SLWGSRLFRARGPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLI 458
Cdd:PRK08199 390 ---AGnyATWLHRFFRFRRYRTQLAPTSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863665 459 MNDGGYGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:PRK08199 467 VNNGMYGTIRMHQEREYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRI 537
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
6-529 |
3.40e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 164.88 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 6 TVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGAGNAVG 84
Cdd:PRK08155 14 TGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKpAVCMACSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 85 ALVEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEI 164
Cdd:PRK08155 94 AIADARLDSIPLVCITGQVPASMIGTDA---FQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 165 PIDIQGAKIPLSLVTAPVKPASVSPVDVGSVNALWAQLKQAKQPLLWL--GGGALGCADAVKKLAD-AGITVISSTHARG 241
Cdd:PRK08155 171 PKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLggGVINSGAPARARELAEkAQLPTTMTLMALG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 242 VLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPR-VQIDIDPAAASRNYLMDNTLVADCS 318
Cdd:PRK08155 251 MLPKAHPLSLgmLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKiIHVDIDRAELGKIKQPHVAIQADVD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 319 ALLSALAEKAQGREwgNAQWDGLVQEavTQAERGL--------REQCGvyaqLNDAIEKALPEDGLLVRDITvSGSLWGS 390
Cdd:PRK08155 331 DVLAQLLPLVEAQP--RAEWHQLVAD--LQREFPCpipkaddpLSHYG----LINAVAACVDDNAIITTDVG-QHQMWTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 391 RLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRG 469
Cdd:PRK08155 402 QAYPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863665 470 IQDKYFGGRQYYNEL-HTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:PRK08155 482 QQSLFYGQRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRI 542
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
9-527 |
4.15e-43 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 161.53 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVgQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALV 87
Cdd:PRK08322 5 DLFVKCLENEGVEYIFGIPGEENLDLLEAL-RDSSIKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 88 EAMNACTPLLHLTGQVekawldaDTGFIHETRDQLTFLKAS----SKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVE 163
Cdd:PRK08322 84 YAQLGGMPMVAITGQK-------PIKRSKQGSFQIVDVVAMmaplTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 164 IPIDIqgAKIPLSLVTAPVKPASVSPVDVGSVNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHAR 240
Cdd:PRK08322 157 LPEDI--AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLilIGAGANRKTASKALTEFVDKtGIPFFTTQMGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 241 GVLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRVQIDIDPAAASRNYLMDNTLVADCS 318
Cdd:PRK08322 235 GVIPETHPLSLgtAGLSQGDYVHCAIEHADLIINVGHDVIEKPPFFMNPNGDKKVIHINFLPAEVDPVYFPQVEVVGDIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 319 ALLSALAEKAQGREWGNAQWDGLVQEAVTQ--AERGLREQCGVYAQ--LNDaIEKALPEDGLLVRDITVSgSLWGSRLFR 394
Cdd:PRK08322 315 NSLWQLKERLADQPHWDFPRFLKIREAIEAhlEEGADDDRFPMKPQriVAD-LRKVMPDDDIVILDNGAY-KIWFARNYR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 395 ARGP----LMNihSLAgAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGI 470
Cdd:PRK08322 393 AYEPntclLDN--ALA-TMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWK 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863665 471 QDKYFgGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK08322 470 QENMG-FEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDC 525
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-519 |
2.42e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 156.91 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALV 87
Cdd:PRK07282 14 DLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVTSGPGATNAITGIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 88 EAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPID 167
Cdd:PRK07282 94 DAMSDSVPLLVFTGQVARAGIGKDA---FQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 168 IQGAKIPL---SLVTAPVKPASVSPVDVgSVNALWAQLKQAKQPLLWLGGGALGcADAVKKLADAG----ITVISSTHAR 240
Cdd:PRK07282 171 VSALETDFiydPEVNLPSYQPTLEPNDM-QIKKILKQLSKAKKPVILAGGGINY-AEAATELNAFAeryqIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 241 GVLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAASRNYLMDNTLVADC 317
Cdd:PRK07282 249 GTIATSHPLFLgmGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVaHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 318 SALLSALAEKAQGREwGNAQWDGLVQEAVTQA------ERGLREQCGVyaqlnDAIEKALPEDGLLVRDITvSGSLWGSR 391
Cdd:PRK07282 329 KKALQMLLAEPTVHN-NTEKWIEKVTKDKNRVrsydkkERVVQPQAVI-----ERIGELTNGDAIVVTDVG-QHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 392 LFrargPLMNIHSLA-----GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGV 466
Cdd:PRK07282 402 YY----PYQNERQLVtsgglGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGM 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863665 467 MRGIQDKYFGGRQYYNELHT-PDFTLLAQAIGLQSWSVER----AEDFDaVMTEALAM 519
Cdd:PRK07282 478 VRQWQESFYEGRTSESVFDTlPDFQLMAQAYGIKHYKFDNpetlAQDLE-VITEDVPM 534
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
6-527 |
2.57e-41 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 156.84 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 6 TVGDAIARTLEQYQVEAIYGvisiHNLP-----IADAVGqrgnIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGA 79
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFG----QSLPsalflAAEAIG----IRQIAYRTENAGGAMADGYARVSGkVAVVTAQNGPAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGP 159
Cdd:PRK06112 87 TLLVAPLAEALKASVPIVALVQDVNRDQTDRNA---FQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 160 VSVEIPIDIQGAKIPLSlvtAPVKPASVS--PVD-VGSVNALWAQ----LKQAKQPLLWLGGGALgCADAVKKLA----D 228
Cdd:PRK06112 164 VVLLLPADLLTAAAAAP---AAPRSNSLGhfPLDrTVPAPQRLAEaaslLAQAQRPVVVAGGGVH-ISGASAALAalqsL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 229 AGITVISSTHARGVLPDSHRASLRAFHN-----SPS--VEALIAQCDFTLIAGSRLRSNETRSWTLELPSPR-VQIDIDP 300
Cdd:PRK06112 240 AGLPVATTNMGKGAVDETHPLSLGVVGSlmgprSPGrhLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQyIHIDVDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 301 AAASRNYlMDNTLVADCSALLSALAEKAQGREWGNAQWD-GLVQEAVTQAERGLREQCGVYAQLNDAI---EKALPE-DG 375
Cdd:PRK06112 320 EEVGRNY-EALRLVGDARLTLAALTDALRGRDLAARAGRrAALEPAIAAGREAHREDSAPVALSDASPirpERIMAElQA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 376 LLVRDITVSG-----SLWGSRLFRARGPLMNI---HSLAGaIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATL 447
Cdd:PRK06112 399 VLTGDTIVVAdasysSIWVANFLTARRAGMRFltpRGLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 448 AQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK06112 478 RRMGVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEV 557
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-529 |
7.38e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 146.84 E-value: 7.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVgQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGA 79
Cdd:PRK06048 4 STEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDEL-YDSDLRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGP 159
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDA---FQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 160 VSVEIPIDIQGAKIPLSLvtapvkPASVS-----PVDVGSVNAL---WAQLKQAKQPLLWLGGGALGcADAVKKLADAGI 231
Cdd:PRK06048 160 VLIDLPKDVTTAEIDFDY------PDKVElrgykPTYKGNPQQIkraAELIMKAERPIIYAGGGVIS-SNASEELVELAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 232 T----VISSTHARGVLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAAS 304
Cdd:PRK06048 233 TipapVTTTLMGIGAIPTEHPLSLgmLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIiHIDIDPAEIS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 305 RNYLMDNTLVADCSALLSALAEKAQGREWGN-----AQWDGLVQEAVTQAERGLREQCgVYAQLNDAIEkalpeDGLLVR 379
Cdd:PRK06048 313 KNVKVDVPIVGDAKQVLKSLIKYVQYCDRKEwldkiNQWKKEYPLKYKEREDVIKPQY-VIEQIYELCP-----DAIIVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 380 DITvSGSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLI 458
Cdd:PRK06048 387 EVG-QHQMWAAQYFKYKYPRTFITSGGlGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAI 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863665 459 MNDGGYGVMRGIQDKYFGGRQYYNELH-TPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:PRK06048 466 LNNGYLGMVRQWQELFYDKRYSHTCIKgSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIV 537
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-531 |
1.16e-37 |
|
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: 146.07 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSGLGVALT------- 73
Cdd:COG3961 1 MPMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTtygvgel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 74 StgagagnavgalveAMNA-------CTPLLHLTG------QVEKAwldadtgFIHET---RDQLTFLKASSK--RAYRI 135
Cdd:COG3961 81 S--------------AINGiagayaeRVPVVHIVGapgtraQRRGP-------LLHHTlgdGDFDHFLRMFEEvtVAQAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 136 SNASQAIAILHKAIQEAQTPpCGPVSVEIPIDIQGAKIPLSLVTAPVKPASVSPVDVGS-VNALWAQLKQAKQPL--LWL 212
Cdd:COG3961 140 LTPENAAAEIDRVLAAALRE-KRPVYIELPRDVADAPIEPPEAPLPLPPPASDPAALAAaVAAAAERLAKAKRPVilAGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 213 GGGALGCADAVKKLADA-GITVISSTHARGVLPDSHR---------ASlrafhnSPSVEALIAQCDFTLIAGSRLRSNET 282
Cdd:COG3961 219 EVHRFGLQEELLALAEKtGIPVATTLLGKSVLDESHPqfigtyagaAS------SPEVREYVENADCVLCLGVVFTDTNT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 283 RSWTLELPSPRVqIDIDPAAAS-RNYLMDNTLVADcsaLLSALAEKAQGREWGNAQWDGLVQEAVTQAERGLReqcgvYA 361
Cdd:COG3961 293 GGFTAQLDPERT-IDIQPDSVRvGGHIYPGVSLAD---FLEALAELLKKRSAPLPAPAPPPPPPPAAPDAPLT-----QD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 362 QLNDAIEKALPEDGLLVRDItvsgslwGSRLFRARGplMNIHS--------LAGAIGMGLPMAIGTAIANPQRKVVGLVG 433
Cdd:COG3961 364 RLWQRLQAFLDPGDIVVADT-------GTSLFGAAD--LRLPEgatfiaqpLWGSIGYTLPAALGAALAAPDRRVILLVG 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 434 DGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYfggrQYYNELHTPDFTLLAQAIG---LQSWSVERAEDFD 510
Cdd:COG3961 435 DGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPD----GPYNDIANWDYAKLPEAFGggnALGFRVTTEGELE 510
|
570 580
....*....|....*....|..
gi 502863665 511 AVMTEALAMP-GPSVVEVRMGQ 531
Cdd:COG3961 511 EALAAAEANTdRLTLIEVVLDK 532
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
5-527 |
1.94e-37 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 145.91 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 5 ITVGDAIARTLEQYQVEAIYGVI--SIHNlpIADAV-GQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAG 80
Cdd:PRK08611 4 IKAGEALVKLLQDWGIDHVYGIPgdSIDA--VVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 81 NAVGALVEAMNACTPLLHLTGQVEKAWLDadTGFIHETRDQLTFLKASskrAY--RISNASQAIAILHKAIQEAQTPPcG 158
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLG--TDFFQEVNLEKMFEDVA---VYnhQIMSAENLPEIVNQAIRTAYEKK-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 159 PVSVEIPIDIQGAKIPLSLVTAPVK--PASVSPvDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLAD-AGITVIS 235
Cdd:PRK08611 156 VAVLTIPDDLPAQKIKDTTNKTVDTfrPTVPSP-KPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEkAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 236 STHARGVLPDSHRASLR---AFHNSPSVEAlIAQCDFTLIAGSRLrsnetrSWTLELP--SPRVQIDIDPAAASRNYLMD 310
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGnlgKIGTKPAYEA-MQEADLLIMVGTNY------PYVDYLPkkAKAIQIDTDPANIGKRYPVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 311 NTLVADCSALLSALAEKAQGREWGN---------AQWDGLVQEAVTQAERGLREQcgvyaQLNDAIEKALPEDGLLVRDI 381
Cdd:PRK08611 308 VGLVGDAKKALHQLTENIKHVEDRRfleacqenmAKWWKWMEEDENNASTPIKPE-----RVMAAIQKIADDDAVLSVDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 382 TVSgSLWGSRLFRargplMN------IHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVT 455
Cdd:PRK08611 383 GTV-TVWSARYLN-----LGtnqkfiISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863665 456 LLIMNDGGYGVMrgiqdKY----FGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK08611 457 VVVLNNQQLAFI-----KYeqqaAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDV 527
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
8-527 |
1.15e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 143.74 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 8 GDAIARTLEQYQVEAIYGVISIHNLPIADAVGQrGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGAL 86
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 87 VEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPI 166
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDA---FQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 167 DIQGAK-------IPLSLVTAPVKPASVS-PVDVGSVNALwaqLKQAKQPLLWLGGGALGcADA---VKKLAD-AGITVI 234
Cdd:PRK06276 160 DVQEGEldlekypIPAKIDLPGYKPTTFGhPLQIKKAAEL---IAEAERPVILAGGGVII-SGAseeLIELSElVKIPVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 235 SSTHARGVLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAASRNYLMDN 311
Cdd:PRK06276 236 TTLMGKGAFPEDHPLALgmVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIiHIDIDPAEIGKNVRVDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 312 TLVADCSALLSALAEKAQGREWGNA-QWDGLVQE-------AVTQAERGLREQcGVYAQLNDAIEKALP-EDGLLVRDIT 382
Cdd:PRK06276 316 PIVGDAKNVLRDLLAELMKKEIKNKsEWLERVKKlkkesipRMDFDDKPIKPQ-RVIKELMEVLREIDPsKNTIITTDVG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 383 VSgSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMND 461
Cdd:PRK06276 395 QN-QMWMAHFFKTSAPRSFISSGGlGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDN 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863665 462 GGYGVMRGIQDKYFGGRQYYNEL-HTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK06276 474 RTLGMVYQWQNLYYGKRQSEVHLgETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDI 540
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
7-174 |
1.41e-36 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 133.51 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 7 VGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGA 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 86 LVEAMNACTPLLHLTGQVEKAwlDADTGFIHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIP 165
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRS--LVGRGALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIP 158
|
....*....
gi 502863665 166 IDIQGAKIP 174
Cdd:pfam02776 159 LDVLLEEVD 167
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
9-527 |
1.46e-36 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 143.07 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGnIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALV 87
Cdd:PRK08617 9 DLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLTGkPGVVLVTSGPGVSNLATGLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 88 EAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPID 167
Cdd:PRK08617 88 TATAEGDPVVAIGGQVKRADRLKRT---HQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 168 IQGAKIPLSLVtAPVKPASVSPVDVGSVNALWAQLKQAKQPLLW--LGGGALGCADAVKKL-ADAGITVISSTHARGVLP 244
Cdd:PRK08617 165 VVDAPVTSKAI-APLSKPKLGPASPEDINYLAELIKNAKLPVLLlgMRASSPEVTAAIRRLlERTNLPVVETFQAAGVIS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 245 DSH------RASLraFHNSPSvEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRVQIDIDPAAASRNYLMDNTLVADCS 318
Cdd:PRK08617 244 RELedhffgRVGL--FRNQPG-DELLKKADLVITIGYDPIEYEPRNWNSEGDATIIHIDVLPAEIDNYYQPERELIGDIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 319 ALLSALAEKAQGREW---GNAQWDGLVQEAVTQAERGLREQCGVYAQLN--DAIEKALPEDGLLVRDItvsGS--LWGSR 391
Cdd:PRK08617 321 ATLDLLAEKLDGLSLspqSLEILEELRAQLEELAERPARLEEGAVHPLRiiRALQDIVTDDTTVTVDV---GShyIWMAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 392 LFR---ARGPLM-NIHSlagAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGvM 467
Cdd:PRK08617 398 YFRsyePRHLLFsNGMQ---TLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYN-M 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863665 468 RGIQD--KYfgGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK08617 474 VEFQEemKY--GRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDI 533
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
386-527 |
1.69e-35 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 130.01 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 386 SLWGSRLFRARGPLMNIHS-LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGY 464
Cdd:pfam02775 6 QMWAAQYYRFRPPRRYLTSgGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGY 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863665 465 GVMRGIQDKYFGGR---QYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:pfam02775 86 GMTRGQQTPFGGGRysgPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-527 |
1.28e-33 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 134.57 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVgQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNA 82
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 83 VGALVEAMNACTPLLHLTGQVEKAWLDADtgFIHETRDQLTFLKASSKRAyRISNASQAIAILHKAIQEAQTPPcGPVSV 162
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHD--YFQEVNLTKLFDDVAVFNQ-ILINPENAEYIIRRAIREAISKR-GVAHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 163 EIPIDI--QGAKIPLSLVTApvKPASVSPVDVGSVNALwaqLKQAKQPLLWLGGGALGCADAVKKLADA-GITVISSTHA 239
Cdd:PRK06457 156 NLPVDIlrKSSEYKGSKNTE--VGKVKYSIDFSRAKEL---IKESEKPVLLIGGGTRGLGKEINRFAEKiGAPIIYTLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 240 RGVLPDSHR---ASLRAFHNSPSVEALiAQCDFTLIAGSRLrsneTRSWTLELPSPRVQIDIDPAAASRNYLMDNTLVAD 316
Cdd:PRK06457 231 KGILPDLDPkvmGGIGLLGTKPSIEAM-DKADLLIMLGTSF----PYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 317 CSALLSALAEKAQGREWGN-----AQWDGLVQEAVTQAERGLREQCGVYaqlndAIEKALPEDGLLVRDiTVSGSLWGSR 391
Cdd:PRK06457 306 VAEFLNIDIEEKSDKFYEElkgkkEDWLDSISKQENSLDKPMKPQRVAY-----IVSQKCKKDAVIVTD-TGNVTMWTAR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 392 LFRARGPLMNIHS-LAGAIGMGLPMAIGTAIA-NPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRg 469
Cdd:PRK06457 380 HFRASGEQTFIFSaWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIK- 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863665 470 IQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK06457 459 FEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDA 516
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-528 |
1.30e-32 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 131.75 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGA 79
Cdd:PRK09107 7 MPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQV------EKAWLDADTGFIheTRdqltflkASSKRAYRISNASQAIAILHKAIQEAQ 153
Cdd:PRK09107 87 TNAVTPLQDALMDSIPLVCITGQVpthligSDAFQECDTVGI--TR-------PCTKHNWLVKDVNDLARVIHEAFHVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 154 TPPCGPVSVEIPIDIQGAKiplSLVTAPVKPA---SVSPV---DVGSVNALWAQLKQAKQPLLWL----GGGALGCADAV 223
Cdd:PRK09107 158 SGRPGPVVVDIPKDVQFAT---GTYTPPQKAPvhvSYQPKvkgDAEAITEAVELLANAKRPVIYSgggvINSGPEASRLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 224 KKLADAGITVISST-HARGVLPDSHRASLRAFHNSPSVEALIAQ--CDFTLIAGSRLRSNET-RSWTLELPSPRVQIDID 299
Cdd:PRK09107 235 RELVELTGFPITSTlMGLGAYPASGKNWLGMLGMHGTYEANMAMhdCDVMLCVGARFDDRITgRLDAFSPNSKKIHIDID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 300 PAAASRNYLMDNTLVADCSALLSAL--AEKAQGREWGNAQwdglVQEAVTQAERGLREQCGVYAQLNDAIekaLPEDGL- 376
Cdd:PRK09107 315 PSSINKNVRVDVPIIGDVGHVLEDMlrLWKARGKKPDKEA----LADWWGQIARWRARNSLAYTPSDDVI---MPQYAIq 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 377 ----LVRD----ITV---SGSLWGSRLFRARGP--LMNIHSLaGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGE 443
Cdd:PRK09107 388 rlyeLTKGrdtyITTevgQHQMWAAQFFGFEEPnrWMTSGGL-GTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 444 LATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGR--QYYNElHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPG 521
Cdd:PRK09107 467 MSTAVQYNLPVKIFILNNQYMGMVRQWQQLLHGNRlsHSYTE-AMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDK 545
|
....*..
gi 502863665 522 PSVVEVR 528
Cdd:PRK09107 546 PVIFDCR 552
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
388-529 |
8.90e-32 |
|
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: 121.07 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 388 WGSRLFRARGP--LMNIHSLaGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYG 465
Cdd:cd02015 30 WAAQYYRFKKPrsWLTSGGL-GTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGSLG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863665 466 VMRGIQDKYFGGR-QYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:cd02015 109 MVRQWQELFYEGRySHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDGPVLLDVLV 173
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
15-531 |
3.43e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 127.57 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 15 LEQYQVEAIYGVISIHNLPIADAVGQRGnIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGAGNAVGALVEAMNAC 93
Cdd:PRK07710 26 LEKEGVEVIFGYPGGAVLPLYDALYDCG-IPHILTRHEQGAIHAAEGYARISGKpGVVIATSGPGATNVVTGLADAMIDS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 94 TPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPIDIQGAKI 173
Cdd:PRK07710 105 LPLVVFTGQVATSVIGSDA---FQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDMVVEEG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 174 PLSL---VTAPVKPASVSPvDVGSVNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHARGVLPDSH 247
Cdd:PRK07710 182 EFCYdvqMDLPGYQPNYEP-NLLQIRKLVQAVSVAKKPVilAGAGVLHAKASKELTSYAEQqEIPVVHTLLGLGGFPADH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 248 RASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAASRNYLMDNTLVADCSALLSAL 324
Cdd:PRK07710 261 PLFLgmAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVaHIDIDPAEIGKNVPTEIPIVADAKQALQVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 325 AEKaQGREWGNAQWDGLVQEAVTQ-------AERGLREQcgvyaQLNDAIEKALPEDGLLVRDITvSGSLWGSRLFRARG 397
Cdd:PRK07710 341 LQQ-EGKKENHHEWLSLLKNWKEKyplsykrNSESIKPQ-----KAIEMLYEITKGEAIVTTDVG-QHQMWAAQYYPFKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 398 PLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFG 476
Cdd:PRK07710 414 PDKWVTSGGlGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEEFYN 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863665 477 GRQYYNEL-HTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRMGQ 531
Cdd:PRK07710 494 QRYSHSLLsCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQ 549
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-528 |
6.32e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 127.09 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 2 SEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAV---GQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGA 77
Cdd:PRK07418 16 PQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELykaEAEGWLKHILVRHEQGAAHAADGYARATGkVGVCFGTSGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 78 GAGNAVGALVEAMNACTPLLHLTGQVEKAWLDADtGFiHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPC 157
Cdd:PRK07418 96 GATNLVTGIATAQMDSVPMVVITGQVPRPAIGTD-AF-QET-DIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 158 GPVSVEIPIDIqGAKiplSLVTAPVKPASVSP--------VDVGSVNALWAQLKQAKQPLLWLG--GGALGCADAVKKLA 227
Cdd:PRK07418 173 GPVLIDIPKDV-GQE---EFDYVPVEPGSVKPpgyrptvkGNPRQINAALKLIEEAERPLLYVGggAISAGAHAELKELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 228 DAG-ITVISSTHARGVLPDSHRASL--RAFHNSPSVEALIAQCDFtLIA-GSRLRSNETRSwtLELPSPR---VQIDIDP 300
Cdd:PRK07418 249 ERFqIPVTTTLMGKGAFDEHHPLSVgmLGMHGTAYANFAVTECDL-LIAvGARFDDRVTGK--LDEFASRakvIHIDIDP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 301 AAASRNYLMDNTLVADCSALLSALAEKAQGR--EWGNAQWDGLVQE-------AVTQAERGLREQcgvyaQLNDAIEKAL 371
Cdd:PRK07418 326 AEVGKNRRPDVPIVGDVRKVLVKLLERSLEPttPPRTQAWLERINRwkqdyplVVPPYEGEIYPQ-----EVLLAVRDLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 372 PeDGLLVRDITvSGSLWGSRLFRaRGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQE 450
Cdd:PRK07418 401 P-DAYYTTDVG-QHQMWAAQFLR-NGPRRWISSAGlGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 451 KANVTLLIMNDGGYGVMRGIQDKYFGGRqYYN---ELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK07418 478 GINVKTVIINNGWQGMVRQWQESFYGER-YSAsnmEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDV 556
|
.
gi 502863665 528 R 528
Cdd:PRK07418 557 H 557
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
4-527 |
9.42e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 126.11 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVISIHNLPIADAV---GQRGNIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGA 79
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQVEK------AWLDADTGFIHETrdqltflkaSSKRAYRISNASQAIAILHKAIQEAQ 153
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRsvmgkmAFQEADAMGVFEN---------VTKYVIGIKRIDEIPQWIKNAFYIAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 154 TPPCGPVSVEIPIDIQGAKIplSLVTAPVKP---------ASVSPVDVGSVNALwaqLKQAKQPLLWLGGGA--LGCADA 222
Cdd:PRK06456 152 TGRPGPVVIDIPRDIFYEKM--EEIKWPEKPlvkgyrdfpTRIDRLALKKAAEI---LINAERPIILVGTGVvwSNATPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 223 VKKLADA-GITVISSTHARGVLPDSHRASLRAFHNSPSVEALIA--QCDFTLIAGSRLrSNETRSWTLELPSPR---VQI 296
Cdd:PRK06456 227 VLELAELlHIPIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAalESDAMLVVGARF-SDRTFTSYDEMVETRkkfIMV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 297 DIDPAAASRNYLMDNTLVADCSALLSAL--AEKAQGREWGNAQWDGLVQEavtqaergLREqcgVYAQLN---------- 364
Cdd:PRK06456 306 NIDPTDGEKAIKVDVGIYGNAKIILRELikAITELGQKRDRSAWLKRVKE--------YKE---YYSQFYyteengklkp 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 365 ----DAIEKALPEDGLLVRDITvSGSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSL 439
Cdd:PRK06456 375 wkimKTIRQALPRDAIVTTGVG-QHQMWAEVFWEVLEPRTFLTSSGmGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 440 NLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGR----QYYNelhTPDFTLLAQAIGLQSWSVERAEDFDAVMTE 515
Cdd:PRK06456 454 TGTNLATAVDEHIPVISVIFDNRTLGLVRQVQDLFFGKRivgvDYGP---SPDFVKLAEAFGALGFNVTTYEDIEKSLKS 530
|
570
....*....|..
gi 502863665 516 ALAMPGPSVVEV 527
Cdd:PRK06456 531 AIKEDIPAVIRV 542
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
3-519 |
1.64e-30 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 125.70 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK08979 2 EMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:PRK08979 82 TITGIATAYMDSIPMVVLSGQVPSNLIGNDA---FQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIQGAKIPLSLV-TAPVKPASVSPVDVGSVNALWAQLK---QAKQPL--LWLGGGALGCADAVKKLADA-GITVI 234
Cdd:PRK08979 159 IDLPKDCLNPAILHPYEyPESIKMRSYNPTTSGHKGQIKRGLQallAAKKPVlyVGGGAIISGADKQILQLAEKlNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 235 SSTHARGVLPDSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPR---VQIDIDPAAASRNYLMDN 311
Cdd:PRK08979 239 STLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNatiLHIDIDPSSISKTVRVDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 312 TLV--AD--CSALLSALAEKAQGREWG--NAQWDGLVQeavtQAERglreQCGVYAQLNDAIEkalPED------GLLVR 379
Cdd:PRK08979 319 PIVgsADkvLDSMLALLDESGETNDEAaiASWWNEIEV----WRSR----NCLAYDKSSERIK---PQQvietlyKLTNG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 380 DITVSGSLWGSRLFRA-----RGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKAN 453
Cdd:PRK08979 388 DAYVASDVGQHQMFAAlyypfDKPRRWINSGGlGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863665 454 VTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHT-PDFTLLAQAIGLQSWSVERAEDFDAVMTEALAM 519
Cdd:PRK08979 468 VKIINLNNRFLGMVKQWQDMIYQGRHSHSYMDSvPDFAKIAEAYGHVGIRISDPDELESGLEKALAM 534
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
2-527 |
3.21e-30 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 124.30 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 2 SEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADavGQRGNIRFVPARGEAGSVTMADAHGRFS------------GLG 69
Cdd:PRK07092 9 AAMTTVRDATIDLLRRFGITTVFGNPGSTELPFLR--DFPDDFRYVLGLQEAVVVGMADGYAQATgnaafvnlhsaaGVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 70 VALTStgagagnavgaLVEAMNACTPLLHLTGQVEKAWLDADTgFIHETRDQlTFLKASSKRAYRISNASQAIAILHKAI 149
Cdd:PRK07092 87 NAMGN-----------LFTAFKNHTPLVITAGQQARSILPFEP-FLAAVQAA-ELPKPYVKWSIEPARAEDVPAAIARAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 150 QEAQTPPCGPVSVEIPIDIQGAKIPlslvtaPVKPASVSPV---DVGSVNALWAQLKQAKQPLLW--LGGGALGCADAVK 224
Cdd:PRK07092 154 HIAMQPPRGPVFVSIPYDDWDQPAE------PLPARTVSSAvrpDPAALARLGDALDAARRPALVvgPAVDRAGAWDDAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 225 KLAD---AGITVISSThARGVLPDSHRaSLRAF-HNSP-SVEALIAQCDFTLIAGSRLRSnetrsWTLELPSPR------ 293
Cdd:PRK07092 228 RLAErhrAPVWVAPMS-GRCSFPEDHP-LFAGFlPASReKISALLDGHDLVLVIGAPVFT-----YHVEGPGPHlpegae 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 294 -VQIDIDPAAASRNyLMDNTLVADCSALLSALAEKAqgREWGNAQWDGLVQ-EAVTQAERGLREqcgvyAQLNDAIEKAL 371
Cdd:PRK07092 301 lVQLTDDPGEAAWA-PMGDAIVGDIRLALRDLLALL--PPSARPAPPARPMpPPAPAPGEPLSV-----AFVLQTLAALR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 372 PEDGLLVRDITVSGSLWGSRL-FRARGPLMNIHSlaGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQE 450
Cdd:PRK07092 373 PADAIVVEEAPSTRPAMQEHLpMRRQGSFYTMAS--GGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863665 451 KANVTLLIMNDGGYGVMRGIQdKYFGGRQYYN-ELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:PRK07092 451 KLPVTFVILNNGRYGALRWFA-PVFGVRDVPGlDLPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEV 527
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
3-518 |
6.10e-30 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 123.81 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK07979 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:PRK07979 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDA---FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIQGAKIPLSLV-TAPVKPASVSPV---DVGSVNALWAQLKQAKQPLLWLG--GGALGCADAVKKLADA-GITVI 234
Cdd:PRK07979 159 VDLPKDILNPANKLPYVwPESVSMRSYNPTtqgHKGQIKRALQTLVAAKKPVVYVGggAINAACHQQLKELVEKlNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 235 SSTHARGVLPDSHRASLRAFHNSPSVEALIA--QCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAASRNYLMDN 311
Cdd:PRK07979 239 SSLMGLGAFPATHRQSLGMLGMHGTYEANMTmhNADVIFAVGVRFDDRTTNNLAKYCPNATVlHIDIDPTSISKTVTADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 312 TLVADCSALLSALAEKaqgrewgnaqwdgLVQEAVTQAERGLRE-----------QCGVYAQLNDAIE-KALPED--GLL 377
Cdd:PRK07979 319 PIVGDARQVLEQMLEL-------------LSQESAHQPLDEIRDwwqqieqwrarQCLKYDTHSEKIKpQAVIETlwRLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 378 VRDITVSGSLWGSRLFRA-----RGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEK 451
Cdd:PRK07979 386 KGDAYVTSDVGQHQMFAAlyypfDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYE 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863665 452 ANVTLLIMNDGGYGVMRGIQDKYFGGR--QYYNElHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALA 518
Cdd:PRK07979 466 LPVLVLNLNNRYLGMVKQWQDMIYSGRhsQSYMQ-SLPDFVRLAEAYGHVGIQISHPDELESKLSEALE 533
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
11-519 |
7.57e-30 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 123.49 E-value: 7.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 11 IARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALVEA 89
Cdd:PRK06882 10 VVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 90 MNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPIDIQ 169
Cdd:PRK06882 90 YTDSVPLVILSGQVPSNLIGTDA---FQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDMV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 170 GAKIPLSL-VTAPVKPASVSPVDVGSVNALWAQLKQ---AKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHARGV 242
Cdd:PRK06882 167 NPANKFTYeYPEEVSLRSYNPTVQGHKGQIKKALKAllvAKKPVlfVGGGVITAECSEQLTQFAQKlNLPVTSSLMGLGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 243 LPDSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPR---VQIDIDPAAASRNYLMDNTLVADCSA 319
Cdd:PRK06882 247 YPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNakvIHIDIDPTSISKNVPAYIPIVGSAKN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 320 LLSALAEKAQGREWGNAQWDglVQEAVTQAERGLREQCGVYAQLNDAIEkalPEDGL-LVRDIT-----VSGSLWGSRLF 393
Cdd:PRK06882 327 VLEEFLSLLEEENLAKSQTD--LTAWWQQINEWKAKKCLEFDRTSDVIK---PQQVVeAIYRLTngdayVASDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 394 RA-----RGPLMNIHS-LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVM 467
Cdd:PRK06882 402 AAlhypfDKPRRWINSgGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502863665 468 RGIQDKYFGGRQ---YYNELhtPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAM 519
Cdd:PRK06882 482 KQWQDLIYSGRHsqvYMNSL--PDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSI 534
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
365-527 |
8.43e-30 |
|
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: 115.32 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 365 DAIEKALPEDGLLVRDiTVSGSLWGSRLFRARGPLMNIHS-LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGE 443
Cdd:cd02014 9 AELNKRAPDDAIFTID-VGNVTVWAARHLRMNGKQRFILSgLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 444 LATLAQEKANVTLLIMNDGGYGVMRGIQdKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPS 523
Cdd:cd02014 88 LITAVKYNLPVIVVVFNNSDLGFIKWEQ-EVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALAADGPV 166
|
....
gi 502863665 524 VVEV 527
Cdd:cd02014 167 VIDV 170
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
360-529 |
1.68e-29 |
|
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: 114.23 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 360 YAQLNDAIEKALPEDGLLVRD-ITVSGSLWgsRLFRARGPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLS 438
Cdd:cd02002 3 PEYLAAALAAALPEDAIIVDEaVTNGLPLR--DQLPLTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 439 LNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGR-----QYYNELHTP--DFTLLAQAIGLQSWSVERAEDFDA 511
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenaPDGLDLLDPgiDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 502863665 512 VMTEALAMPGPSVVEVRM 529
Cdd:cd02002 161 ALREALAEGGPALIEVVV 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
366-527 |
3.17e-29 |
|
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: 113.54 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 366 AIEKALPEDGLLVRDItvsGS--LWGSRLFRARGPLMNIHSLAGA-IGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLG 442
Cdd:cd02010 7 DLRAVMGDDDIVLLDV---GAhkIWMARYYRTYAPNTCLISNGLAtMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 443 ELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFgGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGP 522
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEY-GRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAADGV 162
|
....*
gi 502863665 523 SVVEV 527
Cdd:cd02010 163 HVIDC 167
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
4-528 |
1.54e-28 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 119.71 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVI--SIHNLpiADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAG 80
Cdd:PRK09124 2 KQTVADYIAKTLEQAGVKRIWGVTgdSLNGL--SDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 81 NAVGALVEAMNACTPLLHLTGQVEKAwlDADTGFIHETRDQLTFlKASSKRAYRISNASQAIAILHKAIQEAQTPPcGPV 160
Cdd:PRK09124 80 HLINGLFDCHRNHVPVLAIAAHIPSS--EIGSGYFQETHPQELF-RECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 161 SVEIPIDIQGAKIPLSLVTAPVKPAS--VSPVDvGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADA-GITVIsst 237
Cdd:PRK09124 156 VVVLPGDVALKPAPERATPHWYHAPQpvVTPAE-EELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETlKAPIV--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HA-RGVL------P-DSHRASLRAFhnSPSVEALIAqCDFTLIAGSRLrsnETRSWtleLPSPR--VQIDIDPAAASRNY 307
Cdd:PRK09124 232 HAlRGKEhveydnPyDVGMTGLIGF--SSGYHAMMN-CDTLLMLGTDF---PYRQF---YPTDAkiIQIDINPGSLGRRS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 308 LMDNTLVADCSALLSALAEKAQGREwgnaqwDGLVQEAVTQAERGLREQCGVYAQLNDA------------IEKALPEDG 375
Cdd:PRK09124 303 PVDLGLVGDVKATLAALLPLLEEKT------DRKFLDKALEHYRKARKGLDDLAVPSDGgkpihpqylarqISEFAADDA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 376 LLVRDITvSGSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANV 454
Cdd:PRK09124 377 IFTCDVG-TPTVWAARYLKMNGKRRLLGSFNhGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPV 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863665 455 TLLIMNDGGYGVMrGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVR 528
Cdd:PRK09124 456 KIVVFNNSVLGFV-AMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVV 528
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
9-166 |
2.78e-28 |
|
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: 110.31 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVgQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALV 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDAL-ARSGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863665 88 EAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPI 166
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGA---FQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
9-527 |
5.61e-28 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 117.92 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALV 87
Cdd:PLN02470 17 DILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGkVGVCIATSGPGATNLVTGLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 88 EAMNACTPLLHLTGQVEKAWLDAD----TGFIHETRdQLTflkassKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVE 163
Cdd:PLN02470 97 DALLDSVPLVAITGQVPRRMIGTDafqeTPIVEVTR-SIT------KHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 164 IPIDIQgAKIPLSLVTAPVK-PASVS----PVDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADA-GITVISST 237
Cdd:PLN02470 170 IPKDIQ-QQLAVPNWNQPMKlPGYLSrlpkPPEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELtGIPVASTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HARGVLPDSHRASLR--AFHNSPSVEALIAQCDFTLIAGSRLRSNETRSwtLELPSPR---VQIDIDPAAASRNYLMDNT 312
Cdd:PLN02470 249 MGLGAFPASDELSLQmlGMHGTVYANYAVDSADLLLAFGVRFDDRVTGK--LEAFASRasiVHIDIDPAEIGKNKQPHVS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 313 LVADCSALLSAL-----AEKAQGREWGnaQWDGLVQEavTQAERGLReqcgvYAQLNDAIekaLPEDGLLVRD------- 380
Cdd:PLN02470 327 VCADVKLALQGLnklleERKAKRPDFS--AWRAELDE--QKEKFPLS-----YPTFGDAI---PPQYAIQVLDeltdgna 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 381 ITVSG----SLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVT 455
Cdd:PLN02470 395 IISTGvgqhQMWAAQWYKYKEPRRWLTSGGlGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 456 LLIMNDGGYGVMRGIQDKYFGGrqyyNELHT------------PDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPS 523
Cdd:PLN02470 475 IMVLNNQHLGMVVQWEDRFYKA----NRAHTylgdpdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPY 550
|
....
gi 502863665 524 VVEV 527
Cdd:PLN02470 551 LLDV 554
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
3-519 |
1.98e-27 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 116.38 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 3 EMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK06466 2 ELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADTgfIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVS 161
Cdd:PRK06466 82 AITGIATAYMDSIPMVVLSGQVPSTLIGEDA--FQET-DMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 162 VEIPIDIqgakiplslvTAP-----------VKPASVSPV---DVGSVNALWAQLKQAKQPLLWL--GGGALGCADAVKK 225
Cdd:PRK06466 159 VDIPKDM----------TNPaekfeyeypkkVKLRSYSPAvrgHSGQIRKAVEMLLAAKRPVIYSggGVVLGNASALLTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 226 LADA-GITVISSTHARGVLPDSHRASLRAFHNSPSVEALIA--QCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPA 301
Cdd:PRK06466 229 LAHLlNLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAmhHADVILAVGARFDDRVTNGPAKFCPNAKIiHIDIDPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 302 AASRNYLMDNTLVADCS-------ALLSALAEK----------AQGREWGNAQwdGLVQEAVTQAErGLREQcgvyaQLN 364
Cdd:PRK06466 309 SISKTIKADIPIVGPVEsvltemlAILKEIGEKpdkealaawwKQIDEWRGRH--GLFPYDKGDGG-IIKPQ-----QVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 365 DAIEKALPEDGLLVRDITvSGSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGE 443
Cdd:PRK06466 381 ETLYEVTNGDAYVTSDVG-QHQMFAAQYYKFNKPNRWINSGGlGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQE 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863665 444 LATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQ---YYNELhtPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAM 519
Cdd:PRK06466 460 LSTCLQYGLPVKIINLNNGALGMVRQWQDMQYEGRHshsYMESL--PDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAM 536
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
8-517 |
8.43e-27 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 114.51 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 8 GDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGAL 86
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 87 VEAMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPI 166
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDA---FQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 167 DIQGAKIPLSLVTApVKPASVSPVD---VGSVNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHAR 240
Cdd:PRK06965 181 DVSKTPCEYEYPKS-VEMRSYNPVTkghSGQIRKAVSLLLSAKRPYiyTGGGVILANASRELRQLADLlGYPVTNTLMGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 241 GVLPDSHRASLRAFHNSPSVEALIA--QCDFTLIAGSRLRSNETRSWTLELPSPR--VQIDIDPAAASRNYLMDNTLVAD 316
Cdd:PRK06965 260 GAYPASDKKFLGMLGMHGTYEANMAmqHCDVLIAIGARFDDRVIGNPAHFASRPRkiIHIDIDPSSISKRVKVDIPIVGD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 317 CSALLSALAekAQGREWGNAQWDGLVQEAVTQAERGLREQCGVYAQLNDAIE---------KALPEDGLLVRDITvSGSL 387
Cdd:PRK06965 340 VKEVLKELI--EQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKpqyvveklwELTDGDAFVCSDVG-QHQM 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 388 WGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGV 466
Cdd:PRK06965 417 WAAQFYRFNEPRRWINSGGlGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGM 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502863665 467 MRGIQDKYFGGR---QYYNELhtPDFTLLAQAIGLQSWSVERAEDFDAVMTEAL 517
Cdd:PRK06965 497 VRQWQEIEYSKRyshSYMDAL--PDFVKLAEAYGHVGMRIEKTSDVEPALREAL 548
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
4-527 |
1.40e-26 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 113.54 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNA 82
Cdd:PRK06546 2 AKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGkLAVCAGSCGPGNLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 83 VGALVEAMNACTPLLHLTGQVEKAwlDADTGFIHETRDQLTFLKASSkraYR--ISNASQAIAILHKAIQEAQTPPcGPV 160
Cdd:PRK06546 82 INGLYDAHRSGAPVLAIASHIPSA--QIGSGFFQETHPDRLFVECSG---YCemVSSAEQAPRVLHSAIQHAVAGG-GVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 161 SVEIPIDI--QGAKIPLSLVTAPVKPASVSPvDVGSVNALWAQLKQAKQPLLWLGGGALGCADAVKKLADAgitvissTH 238
Cdd:PRK06546 156 VVTLPGDIadEPAPEGFAPSVISPRRPTVVP-DPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEK-------IK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 239 ArgvlPDSHraSLRA-----FHNSPSV------------EAlIAQCDFTLIAGSRLRSNETrswtleLPSPR-VQIDIDP 300
Cdd:PRK06546 228 A----PVGH--SLRGkewiqYDNPFDVgmsgllgygaahEA-MHEADLLILLGTDFPYDQF------LPDVRtAQVDIDP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 301 AAASRNYLMDNTLVAD----CSALLSALAEKAQGRewgnaqwdgLVQEAVTQAERGLREQCGVYAqlnDAIEKALP---- 372
Cdd:PRK06546 295 EHLGRRTRVDLAVHGDvaetIRALLPLVKEKTDRR---------FLDRMLKKHARKLEKVVGAYT---RKVEKHTPihpe 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 373 -----------EDGLLVRDiTVSGSLWGSRLFRARGPLMNIHS-LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLN 440
Cdd:PRK06546 363 yvasildelaaDDAVFTVD-TGMCNVWAARYITPNGRRRVIGSfRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSML 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 441 LGELATLAQEKANVTLLIMNDGGYGVMR------GIQDkyFGgrqyyNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMT 514
Cdd:PRK06546 442 LGELLTVKLYDLPVKVVVFNNSTLGMVKlemlvdGLPD--FG-----TDHPPVDYAAIAAALGIHAVRVEDPKDVRGALR 514
|
570
....*....|...
gi 502863665 515 EALAMPGPSVVEV 527
Cdd:PRK06546 515 EAFAHPGPALVDV 527
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
11-529 |
3.31e-26 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 112.50 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 11 IARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALVEA 89
Cdd:PRK08527 9 VCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 90 MNACTPLLHLTGQVEKAWLDADtGFihETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPIDIQ 169
Cdd:PRK08527 89 YMDSIPLVLISGQVPNSLIGTD-AF--QEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDVT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 170 GAkipLSLVTAP--VKPASVSPVDVGSVNAL---WAQLKQAKQPL--LWLGGGALGCADAVKKLAD-AGITVISSTHARG 241
Cdd:PRK08527 166 AT---LGEFEYPkeISLKTYKPTYKGNSRQIkkaAEAIKEAKKPLfyLGGGAILSNASEEIRELVKkTGIPAVETLMARG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 242 VL--PDSHRASLRAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSwTLELPSPR--VQIDIDPAAASRNYLMDNTLVADC 317
Cdd:PRK08527 243 VLrsDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGK-LSEFAKHAkiIHVDIDPSSISKIVNADYPIVGDL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 318 SALLSALAEKAQGREWGN-AQWdglvqeavtqaerglREQCGVYAQLND--------------AIE---KALPEDGLLVR 379
Cdd:PRK08527 322 KNVLKEMLEELKEENPTTyKEW---------------REILKRYNELHPlsyedsdevlkpqwVIErvgELLGDDAIIST 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 380 DITvSGSLWGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLI 458
Cdd:PRK08527 387 DVG-QHQMWVAQFYPFNYPRQLATSGGlGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINII 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863665 459 MNDGGYGVMRGIQDKYFGGRQYYNELHT-PDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVRM 529
Cdd:PRK08527 466 LNNNFLGMVRQWQTFFYEERYSETDLSTqPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKI 537
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
9-528 |
4.27e-26 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 111.90 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYG----VIsihnLPIADAVgQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAV 83
Cdd:PRK08978 5 QWVVHALRAQGVDTVFGypggAI----MPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGkVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 84 GALVEAMNACTPLLHLTGQVEKAWLDADTgfIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVE 163
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIGTDA--FQEI-DVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 164 IPIDIQGAKIPLS-LVTAPVKPASVSPVDVGSVNALwaqLKQAKQPLLWLGGGALGcADAVKKLAD----AGITVISSTH 238
Cdd:PRK08978 157 IPKDIQLAEGELEpHLTTVENEPAFPAAELEQARAL---LAQAKKPVLYVGGGVGM-AGAVPALREflaaTGMPAVATLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 239 ARGVLPDSHRASL--RAFHNSPSVEALIAQCDFTLIAGSRLRSNETRSWTLELPSPRV-QIDIDPAAASRNYLMDNTLVA 315
Cdd:PRK08978 233 GLGAVEADHPYYLgmLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKViHLDIDPAEINKLRQAHVALQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 316 DCSALLSALAEKAQGREWgnaqwdglvQEAVTQ--AERGLR-EQCG--VYA-QLNDAIEKALPEDGLLVRDItvsG--SL 387
Cdd:PRK08978 313 DLNALLPALQQPLNIDAW---------RQHCAQlrAEHAWRyDHPGeaIYApALLKQLSDRKPADTVVTTDV---GqhQM 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 388 WGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGV 466
Cdd:PRK08978 381 WVAQHMRFTRPENFITSSGlGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGM 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863665 467 MRGIQDKYFGGRqyYNEL---HTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVR 528
Cdd:PRK08978 461 VRQWQQLFFDER--YSETdlsDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVS 523
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-518 |
9.64e-26 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 111.23 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGA 79
Cdd:PRK07789 27 APERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrVGVCMATSGPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 80 GNAVGALVEAMNACTPLLHLTGQVEKAWLDADTgfihetrdqltFLKAS--------SKRAYRISNASQAIAILHKAIQE 151
Cdd:PRK07789 107 TNLVTPIADANMDSVPVVAITGQVGRGLIGTDA-----------FQEADivgitmpiTKHNFLVTDADDIPRVIAEAFHI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 152 AQTPPCGPVSVEIPIDIQGAKIPLSL-----------VTAP----VKPAsvspvdvgsvnalwAQL-KQAKQPLLWLGGG 215
Cdd:PRK07789 176 ASTGRPGPVLVDIPKDALQAQTTFSWpprmdlpgyrpVTKPhgkqIREA--------------AKLiAAARRPVLYVGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 216 ALGcADA---VKKLADA-GITVISSTHARGVLPDSHRASL--RAFHNS-PSVEALiAQCDFtLIA-GSRLRSNETRSWTL 287
Cdd:PRK07789 242 VIR-AEAsaeLRELAELtGIPVVTTLMARGAFPDSHPQHLgmPGMHGTvAAVAAL-QRSDL-LIAlGARFDDRVTGKLDS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 288 ELPSPRV-QIDIDPAAASRNYLMDNTLVADCSALLSALAEkAQGREwgnaqwdglvqeavtQAERGLREQCGVYAQLNDA 366
Cdd:PRK07789 319 FAPDAKViHADIDPAEIGKNRHADVPIVGDVKEVIAELIA-ALRAE---------------HAAGGKPDLTAWWAYLDGW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 367 IEK-----ALPEDGLLVRD--------------ITVSG----SLWGSRLFRARGPLMNIHSL-AGAIGMGLPMAIGTAIA 422
Cdd:PRK07789 383 RETyplgyDEPSDGSLAPQyvierlgeiagpdaIYVAGvgqhQMWAAQFIDYEKPRTWLNSGgLGTMGYAVPAAMGAKVG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 423 NPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHT-----PDFTLLAQAIG 497
Cdd:PRK07789 463 RPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVRQWQTLFYEERYSNTDLHThshriPDFVKLAEAYG 542
|
570 580
....*....|....*....|.
gi 502863665 498 LQSWSVERAEDFDAVMTEALA 518
Cdd:PRK07789 543 CVGLRCEREEDVDAVIEKARA 563
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
114-531 |
8.30e-25 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 108.16 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 114 FIH---ETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPIDIQGAKIPLSLVTAPVKPASVSP- 189
Cdd:PRK08327 125 RIHwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPa 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 190 VDVGSVNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHARGVLPDSHraslrAFHNSPSVEALIAQ 266
Cdd:PRK08327 205 PDPEDIARAAEMLAAAERPViiTWRAGRTAEGFASLRRLAEElAIPVVEYAGEVVNYPSDH-----PLHLGPDPRADLAE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 267 CDFTLIAGS-------RLRSNETRSWtlelpsprVQIDIDPAAAS---RNYLMDNTLVADCSALLSALAEKAQGREWGNA 336
Cdd:PRK08327 280 ADLVLVVDSdvpwipkKIRPDADARV--------IQIDVDPLKSRiplWGFPCDLCIQADTSTALDQLEERLKSLASAER 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 337 QWDGLVQEAVTQAERglREQCGVYAQLNDA--------------IEKALPEDGLLVRDITV---------SGSLWGSrlf 393
Cdd:PRK08327 352 RRARRRRAAVRELRI--RQEAAKRAEIERLkdrgpitpaylsycLGEVADEYDAIVTEYPFvprqarlnkPGSYFGD--- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 394 rargplmnihSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGglSLNLGE----LATLAQEKANVTLLIMNDGGYG-VMR 468
Cdd:PRK08327 427 ----------GSAGGLGWALGAALGAKLATPDRLVIATVGDG--SFIFGVpeaaHWVAERYGLPVLVVVFNNGGWLaVKE 494
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863665 469 GIQDKYFGG----RQYYNELH---TPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMP----GPSVVEVRMGQ 531
Cdd:PRK08327 495 AVLEVYPEGyaarKGTFPGTDfdpRPDFAKIAEAFGGYGERVEDPEELKGALRRALAAVrkgrRSAVLDVIVDR 568
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-531 |
2.10e-24 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 107.01 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEM-ITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGnIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAG 78
Cdd:PRK07525 1 MGKMkMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 79 AGNAVGALVEAMNACTPLLHLTGQVEKAWLDADtGFihETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTpPCG 158
Cdd:PRK07525 80 ITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQG-GF--QEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKR-ESG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 159 PVSVEIP-------IDIQgakIPlslvtapvKPASV--SPVDVGSVNALWAQLKQAKQPLLWLGG--GALGCADAVKKLA 227
Cdd:PRK07525 156 PAQINIPrdyfygvIDVE---IP--------QPVRLerGAGGEQSLAEAAELLSEAKFPVILSGAgvVLSDAIEECKALA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 228 DA-GITVISSTHARGVLPDSHRASLR--AFHNSPSVEALIAQCDFTLIAGSRLRSNETrswtleLPS------PR----V 294
Cdd:PRK07525 225 ERlDAPVACGYLHNDAFPGSHPLWVGplGYNGSKAAMELIAKADVVLALGTRLNPFGT------LPQygidywPKdakiI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 295 QIDIDPAAASRNYLMDNTLVADCSA----LLSALAEKAQGRE---------------WGN--AQWDGLVQEAVTQAERGL 353
Cdd:PRK07525 299 QVDINPDRIGLTKKVSVGICGDAKAvareLLARLAERLAGDAgreerkaliaaeksaWEQelSSWDHEDDDPGTDWNEEA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 354 REQCGVYA---QLNDAIEKALPEDGLLVRDITVSGSLwGSRLFRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVV 429
Cdd:PRK07525 379 RARKPDYMhprQALREIQKALPEDAIVSTDIGNNCSI-ANSYLRFEKGRKYLAPGSfGNCGYAFPAIIGAKIACPDRPVV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 430 GLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHT-PDFTLLAQAIGLQSWSVERAED 508
Cdd:PRK07525 458 GFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNnVSYAGIAEAMGAEGVVVDTQEE 537
|
570 580
....*....|....*....|....*.
gi 502863665 509 FDAVMTEALAMPG---PSVVEVRMGQ 531
Cdd:PRK07525 538 LGPALKRAIDAQNegkTTVIEIMCNQ 563
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
366-527 |
2.77e-23 |
|
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: 96.83 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 366 AIEKALPEDGLLVRD--ITVSgslWGSRLFRARGPLmniHSL-AGA---IGMGLPMAIGTAIANPQRKVVGLVGDGGLSL 439
Cdd:cd02004 7 ELQEALPDDAIIVSDggNTMD---WARYILRPRKPR---HRLdAGTfgtLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 440 NLGELATLAQEKANVTLLIMNDGG-YGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALA 518
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGwYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
....*....
gi 502863665 519 MPGPSVVEV 527
Cdd:cd02004 161 SGKPALINV 169
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
4-528 |
1.67e-22 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 101.14 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 4 MITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGN-IRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGN 81
Cdd:PRK08273 2 SQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGAIH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 AVGALVEAMNACTPLLHLTGQVEKAWLDADtgFIHETrDQLTFLK-ASSKRAYRISNASQAIAILHKAIQEAQTPPcGPV 160
Cdd:PRK08273 82 LLNGLYDAKLDHVPVVAIVGQQARAALGGH--YQQEV-DLQSLFKdVAGAFVQMVTVPEQLRHLVDRAVRTALAER-TVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 161 SVEIPIDIQGA---KIPLSLVTAPVKPASVSPVDVGSVNALWAQ---LKQAKQPLLWLGGGALGCADAVKKLAD---AGI 231
Cdd:PRK08273 158 AVILPNDVQELeyePPPHAHGTVHSGVGYTRPRVVPYDEDLRRAaevLNAGRKVAILVGAGALGATDEVIAVAErlgAGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 232 TviSSTHARGVLPDSHR---ASLRAFHNSPSVEaLIAQCDFTLIAGSRLrsnetrSWTLELPSP---R-VQIDIDPAAAS 304
Cdd:PRK08273 238 A--KALLGKAALPDDLPwvtGSIGLLGTKPSYE-LMRECDTLLMVGSSF------PYSEFLPKEgqaRgVQIDIDGRMLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 305 RNYLMDNTLVADCSALLSALAEKAQGREwgNAQWDGLVQEAVTQAERGLREQCGVYAQ-LND-----AIEKALPEDGLLV 378
Cdd:PRK08273 309 LRYPMEVNLVGDAAETLRALLPLLERKK--DRSWRERIEKWVARWWETLEARAMVPADpVNPqrvfwELSPRLPDNAILT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 379 RDitvSGSL--WGSRLFRARGPLMNihSLAG---AIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLN-LGELATLA---Q 449
Cdd:PRK08273 387 AD---SGSCanWYARDLRMRRGMMA--SLSGtlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 450 EKANVTLLIM--NDGGYG-------VMRGiqDKYFGGRQyynelHTPDF--TLLAQAIGLQSWSVERAEDFDAVMTEALA 518
Cdd:PRK08273 462 QWSDPRLIVLvlNNRDLNqvtweqrVMEG--DPKFEASQ-----DLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEALA 534
|
570
....*....|
gi 502863665 519 MPGPSVVEVR 528
Cdd:PRK08273 535 ADRPVVLEVK 544
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-527 |
2.31e-22 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 100.82 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 1 MSEMiTVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFS--GLGVALTSTGAG 78
Cdd:PRK11269 1 MAKM-RAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATagNIGVCIGTSGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 79 AGNAVGALVEAMNACTPLLHLTGQVEKAWLDADtGFihETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCG 158
Cdd:PRK11269 80 GTDMITGLYSASADSIPILCITGQAPRARLHKE-DF--QAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 159 PVSVEIPIDIQGAKIPLSLVT-APVKPASVSPVDVGSVNALwAQLKQAKQPLLWLGGGALGcADAVKKLAD----AGITV 233
Cdd:PRK11269 157 PVLIDLPFDVQVAEIEFDPDTyEPLPVYKPAATRAQIEKAL-EMLNAAERPLIVAGGGVIN-ADASDLLVEfaelTGVPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 234 ISSTHARGVLPDSHR-----ASLRAFH---NspsveALIAQCDFTLIAGSRLRSNETRSwtLELPSPR---VQIDIDPAA 302
Cdd:PRK11269 235 IPTLMGWGAIPDDHPlmagmVGLQTSHrygN-----ATLLASDFVLGIGNRWANRHTGS--VEVYTKGrkfVHVDIEPTQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 303 ASRNYLMDNTLVADCSALLSALAEKAqgREWGNA-------QWDGLVQEAVTQAERG-------LREQcGVYAQLNdaie 368
Cdd:PRK11269 308 IGRVFGPDLGIVSDAKAALELLVEVA--REWKAAgrlpdrsAWVADCQERKRTLLRKthfdnvpIKPQ-RVYEEMN---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 369 KALPEDGLLVRDITVSgSLWGSRLFRARGPLMNIH-SLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATL 447
Cdd:PRK11269 381 KAFGRDTCYVSTIGLS-QIAAAQFLHVYKPRHWINcGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 448 AQEKANVTLLIMNDGGYGVMRGIQDKY---FGGRQYYNELHTP-------DFTLLAQAIGLQSWSVERAEDFDAVMTEAL 517
Cdd:PRK11269 460 AQFNLPYIHVLVNNAYLGLIRQAQRAFdmdYCVQLAFENINSPelngygvDHVKVAEGLGCKAIRVFKPEDIAPALEQAK 539
|
570
....*....|....
gi 502863665 518 AMPG----PSVVEV 527
Cdd:PRK11269 540 ALMAefrvPVVVEV 553
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
32-528 |
4.68e-22 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 99.77 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 32 LPIAD---AVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVGALVEAMNACTPLLHLTGQVEKAW 107
Cdd:CHL00099 37 LPIYDelyAWEKKGLIKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 108 LDADTgfIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIPIDIQGAKIPL-------SLVTA 180
Cdd:CHL00099 117 IGTDA--FQEV-DIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEKFDYyppepgnTIIKI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 181 PVKPASVSPVDVGSVNALwAQLKQAKQPLLWLG--GGALGCADAVKKLADA-GITVISSTHARGVLPDSHRASL--RAFH 255
Cdd:CHL00099 194 LGCRPIYKPTIKRIEQAA-KLILQSSQPLLYVGggAIISDAHQEITELAELyKIPVTTTLMGKGIFDEDHPLCLgmLGMH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 256 NSPSVEALIAQCDFTLIAGSRLRSNETRSWTlELPSPR--VQIDIDPAAASRNYLMDNTLVADCSALLSAL--------- 324
Cdd:CHL00099 273 GTAYANFAVSECDLLIALGARFDDRVTGKLD-EFACNAqvIHIDIDPAEIGKNRIPQVAIVGDVKKVLQELlellknspn 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 325 -AEKAQGREWGN--AQWDGLVQEAVTQAERGLREQcgvyaQLNDAIEKALPeDGLLVRDITvSGSLWGSRLFRArGPLMN 401
Cdd:CHL00099 352 lLESEQTQAWREriNRWRKEYPLLIPKPSTSLSPQ-----EVINEISQLAP-DAYFTTDVG-QHQMWAAQFLKC-KPRKW 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 402 IHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQY 480
Cdd:CHL00099 424 LSSAGlGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQAFYGERYS 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502863665 481 YNELH--TPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVR 528
Cdd:CHL00099 504 HSNMEegAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQ 553
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
407-531 |
1.34e-20 |
|
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: 89.52 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 407 GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQdkyfGGRQYYNELHT 486
Cdd:cd02005 50 GSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIH----GPEASYNDIAN 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 502863665 487 PDFTLLAQAIGL----QSWSVERAEDFDAVMTEALAMP-GPSVVEVRMGQ 531
Cdd:cd02005 126 WNYTKLPEVFGGggggLSFRVKTEGELDEALKDALFNRdKLSLIEVILPK 175
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
8-465 |
2.37e-20 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 94.40 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 8 GDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGnIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGAGNAVGAL 86
Cdd:PRK05858 8 GRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVpGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 87 VEAMNACTPLLHLTGQVEKA-WldaDTGFIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPCGPVSVEIP 165
Cdd:PRK05858 87 AAAQFNQSPLVVLGGRAPALrW---GMGSLQEI-DHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 166 IDI-----QGAKIPLSLVTAPVKPASvSPVDVGSVNALwaqLKQAKQPLLWLGGG--ALGCADAVKKLADA-GITVISST 237
Cdd:PRK05858 163 MDHafsmaDDDGRPGALTELPAGPTP-DPDALARAAGL---LAEAQRPVIMAGTDvwWGHAEAALLRLAEElGIPVLMNG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 238 HARGVLPDSH-----RASLRAFHNSPSVEALIAQCDFTLIAGsrLRSNETRSWTLELPSPRVQIDIDPAAAsrnylmdnt 312
Cdd:PRK05858 239 MGRGVVPADHplafsRARGKALGEADVVLVVGVPMDFRLGFG--VFGGTAQLVHVDDAPPQRAHHRPVAAG--------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 313 LVADCSALLSALAEKA-QGREWgnAQWDGLVQEAVTQAERGLREQCG----------VYAQLNdaieKALPEDGLLVRDI 381
Cdd:PRK05858 308 LYGDLSAILSALAGAGgDRTDH--QGWIEELRTAETAARARDAAELAddrdpihpmrVYGELA----PLLDRDAIVIGDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 382 TVSGSLWGSRLFRAR-------GPLmnihslaGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANV 454
Cdd:PRK05858 382 GDFVSYAGRYIDPYRpgcwldpGPF-------GCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPV 454
|
490
....*....|.
gi 502863665 455 TLLIMNDGGYG 465
Cdd:PRK05858 455 VSVIGNNGIWG 465
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
363-529 |
3.30e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 93.76 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 363 LNDAIEKALPEDGLLVRDITVSGSLWGSRLFRARgPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLG 442
Cdd:PRK07586 342 IAQVIAALLPENAIVVDESITSGRGFFPATAGAA-PHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 443 ELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGR-----QYYNELHTP--DFTLLAQAIGLQSWSVERAEDFDAVMTE 515
Cdd:PRK07586 421 ALWTQARENLDVTTVIFANRAYAILRGELARVGAGNpgpraLDMLDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAA 500
|
170
....*....|....
gi 502863665 516 ALAMPGPSVVEVRM 529
Cdd:PRK07586 501 ALAEPGPHLIEAVV 514
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
366-531 |
7.98e-19 |
|
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: 84.87 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 366 AIEKALPEDGLLVRDITVSGSLWGSRLfRARGPLMNIHSLA-GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGEL 444
Cdd:cd02013 12 ELEKAMPEDAIVSTDIGNICSVANSYL-RFEKPRSFIAPLSfGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMMEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 445 ATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEALAMPG--- 521
Cdd:cd02013 91 MTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQKAIAMMAegk 170
|
170
....*....|
gi 502863665 522 PSVVEVRMGQ 531
Cdd:cd02013 171 TTVIEIVCDQ 180
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
407-528 |
4.62e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 82.57 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 407 GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEK-ANVTLLIMNDGGYGVMrgiqdkyfgGRQYYNELH 485
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALApKNLTIIVMDNGVYQIT---------GGQPTLTSQ 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 502863665 486 TPDFTLLAQAIGLQS--WSVERAeDFDAVMTEALAMPGPSVVEVR 528
Cdd:PRK06163 128 TVDVVAIARGAGLENshWAADEA-HFEALVDQALSGPGPSFIAVR 171
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
6-172 |
1.80e-17 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 79.90 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 6 TVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSG-LGVALTSTGAGAGNAVG 84
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 85 ALVEAMNACTPLLHLTGQVEKAWLdaDTGFIHETrDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPcGPVSVEI 164
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDEL--GTDYFQEV-DLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLIL 156
|
....*...
gi 502863665 165 PIDIQGAK 172
Cdd:cd07039 157 PGDVQDAP 164
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
11-535 |
3.42e-17 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 84.65 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 11 IARTLEQYQVEAIYGVISIhnlPIAD--AVGQRGNIRFVPARGEAGSVTMADAHGRFSGL-GVALTSTGAGAGNAVGALV 87
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGI---PITDlaRLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKpGVCLTVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 88 EAMNACTPLLHLTGQVEKAWLDADTGfIHETRDQLTFLKASSKRAYRISNAsQAIAI-LHKAIQEAQTPPCGPVSVEIPI 166
Cdd:PRK09259 93 NATTNCFPMIMISGSSEREIVDLQQG-DYEELDQLNAAKPFCKAAFRVNRA-EDIGIgVARAIRTAVSGRPGGVYLDLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 167 DIQGAKIP-----LSLVTaPVKPASVSPVDVGSVNALWAQLKQAKQPLLWL--GGGALGCADAVKKLAD-AGITVISSTH 238
Cdd:PRK09259 171 KVLAQTMDadealTSLVK-VVDPAPAQLPAPEAVDRALDLLKKAKRPLIILgkGAAYAQADEQIREFVEkTGIPFLPMSM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 239 ARGVLPDSHR---ASLRAFhnspsveaLIAQCDFTLIAGSRLR----SNETRSWTleLPSPRVQIDIDPAAASRNYLMDN 311
Cdd:PRK09259 250 AKGLLPDTHPqsaAAARSL--------ALANADVVLLVGARLNwllsHGKGKTWG--ADKKFIQIDIEPQEIDSNRPIAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 312 TLVADCSALLSALAEKAQGREWG-NAQWDGLVQEAVTQ-----AERGLREQ--CGVYAQLNdAIEKALPE--DGLLV--- 378
Cdd:PRK09259 320 PVVGDIGSVMQALLAGLKQNTFKaPAEWLDALAERKEKnaakmAEKLSTDTqpMNFYNALG-AIRDVLKEnpDIYLVneg 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 379 -------RDIT---------VSGSlWGsrlfrargpLMnihslagAIGMGLpmAIGTAIANpQRKVVGLVGDGGLSLNLG 442
Cdd:PRK09259 399 antldlaRNIIdmykprhrlDCGT-WG---------VM-------GIGMGY--AIAAAVET-GKPVVAIEGDSAFGFSGM 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 443 ELATLAQEKANVTLLIMNDGgyGVMRGIQDKYFGGRQYYNELHTPD--FTLLAQAIGLQSWSVERAEDFDAVMTEALAMP 520
Cdd:PRK09259 459 EVETICRYNLPVTVVIFNNG--GIYRGDDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNVTTPDELRHALTEAIASG 536
|
570 580
....*....|....*....|...
gi 502863665 521 GPSVVEVRM--------GQIGAL 535
Cdd:PRK09259 537 KPTLINVVIdpaagtesGHITNL 559
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-517 |
3.55e-17 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 84.48 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 2 SEMITVGDAIARTLEQYQVEAIYGVISIHNLPIADAVGqrgnIRFVPARGEAGSVTMADAHGRFSG---LGVALTSTGAG 78
Cdd:PRK06154 17 AKTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAAG----IRPVIARTERVAVHMADGYARATSgerVGVFAVQYGPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 79 AGNAVGALVEAMNACTPLLHLTGQVEKAWLDADTGFihetrdqltflkaSSKRAYR-ISNASQAIA-------ILHKAIQ 150
Cdd:PRK06154 93 AENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPNF-------------ESLRNYRhITKWCEQVTlpdevpeLMRRAFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 151 EAQTPPCGPVSVEIPIDIQGAKIP-LSLVTAPVkPASVSPVDVGSVNALWAQLKQAKQPLLWLGG--GALGCADAVKKLA 227
Cdd:PRK06154 160 RLRNGRPGPVVLELPVDVLAEELDeLPLDHRPS-RRSRPGADPVEVVEAAALLLAAERPVIYAGQgvLYAQATPELKELA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 228 DA-GITVISSTHARGVLPDSHRASLRAFHNS--PSVEALIAQCDFTLIAGSRLrsneTRS-WTLELPSPR--VQIDIDPA 301
Cdd:PRK06154 239 ELlEIPVMTTLNGKSAFPEDHPLALGSGGRArpATVAHFLREADVLFGIGCSL----TRSyYGLPMPEGKtiIHSTLDDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 302 AASRNYLMDNTLVADCSALLSAL-------------------AEKAQGREWGNAQWdglvQEAVTQAERGLREqcgvYAQ 362
Cdd:PRK06154 315 DLNKDYPIDHGLVGDAALVLKQMieelrrrvgpdrgraqqvaAEIEAVRAAWLAKW----MPKLTSDSTPINP----YRV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 363 LNDAIEKALPEDGLLVRDitvSGSLWG--SRLFRARGPLMNIH-SLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSL 439
Cdd:PRK06154 387 VWELQHAVDIKTVIITHD---AGSPRDqlSPFYVASRPGSYLGwGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 440 NLGELATLAQEKANVTLLIMNDggyGVMrGIQDKYF--GGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAVMTEAL 517
Cdd:PRK06154 464 TGMDFETAVRERIPILTILLNN---FSM-GGYDKVMpvSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRAL 539
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
363-526 |
7.05e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 83.38 E-value: 7.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 363 LNDAIEKALPEDGLLVRDITVSGSLWGSRLFRARgPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLG 442
Cdd:PRK12474 346 VAQLIAHRTPDQAIYADEALTSGLFFDMSYDRAR-PHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 443 ELATLAQEKANVTLLIMNDGGYGVMRGIQDKYFGGRQYYN-----ELHTP--DFTLLAQAIGLQSWSVERAEDFDAVMTE 515
Cdd:PRK12474 425 ALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRNalsmlDLHNPelNWMKIAEGLGVEASRATTAEEFSAQYAA 504
|
170
....*....|.
gi 502863665 516 ALAMPGPSVVE 526
Cdd:PRK12474 505 AMAQRGPRLIE 515
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
195-324 |
4.59e-15 |
|
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: 72.21 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 195 VNALWAQLKQAKQPL--LWLGGGALGCADAVKKLADA-GITVISSTHARGVLPDSHRASL--RAFHNSPSVEALIAQCDF 269
Cdd:pfam00205 1 IEKAAELLKKAKRPVilAGGGVRRSGASEELRELAEKlGIPVVTTLMGKGAFPEDHPLYLgmLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863665 270 TLIAGSRL-RSNETRSWTLELPSPR-VQIDIDPAAASRNYLMDNTLVADCSALLSAL 324
Cdd:pfam00205 81 VLAVGARFdDIRTTGKLPEFAPDAKiIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
366-527 |
6.38e-15 |
|
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: 73.49 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 366 AIEKALPEDGLLvrdITVSGSLWG--SRLFRARGPLmNIHSLAGAIGMG--LPMAIGTAIANPQRKVVGLVGDGGLSLNL 441
Cdd:cd02003 7 ALNEAIGDDDVV---INAAGSLPGdlHKLWRARTPG-GYHLEYGYSCMGyeIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 442 GELATLAQEKANVTLLIMNDGGYGVMRGIQDKYfGGRQYYNELHTP--------------DFTLLAQAIGLQSWSVERAE 507
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQEST-GSGSFGTEFRDRdqesgqldgallpvDFAANARSLGARVEKVKTIE 161
|
170 180
....*....|....*....|
gi 502863665 508 DFDAVMTEALAMPGPSVVEV 527
Cdd:cd02003 162 ELKAALAKAKASDRTTVIVI 181
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
364-528 |
8.19e-15 |
|
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: 72.71 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 364 NDAIEKALP--EDGLLVRDITVSgslwgSR-LFRARGPLMNIHSLaGAIGMGLPMAIGTAIANPqRKVVGLVGDGGLSLN 440
Cdd:cd03372 2 RDAIKTLIAdlKDELVVSNIGFP-----SKeLYAAGDRPLNFYML-GSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 441 LGELATLAQEKA-NVTLLIMNDGGYGVMrGIQDKYFGGRQyynelhtpDFTLLAQAIGLQS-WSVERAEDFDAVMteALA 518
Cdd:cd03372 75 LGALATIAAEKPkNLIIVVLDNGAYGST-GNQPTHAGKKT--------DLEAVAKACGLDNvATVASEEAFEKAV--EQA 143
|
170
....*....|
gi 502863665 519 MPGPSVVEVR 528
Cdd:cd03372 144 LDGPSFIHVK 153
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
365-528 |
4.56e-11 |
|
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: 61.95 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 365 DAIEKALpeDGLLVRDITVSGSLWGSR-LFRARGPLMNIHS----LAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSL 439
Cdd:cd03371 3 DAIEIVL--SRAPATAAVVSTTGMTSReLFELRDRPGGGHAqdflTVGSMGHASQIALGIALARPDRKVVCIDGDGAALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 440 NLGELATLAQEK-ANVTLLIMNDGGYGVMRGIQDKYFggrqyynelhTPDFTLLAQAIGL-QSWSVERAEDFDAVMTEAL 517
Cdd:cd03371 81 HMGGLATIGGLApANLIHIVLNNGAHDSVGGQPTVSF----------DVSLPAIAKACGYrAVYEVPSLEELVAALAKAL 150
|
170
....*....|.
gi 502863665 518 AMPGPSVVEVR 528
Cdd:cd03371 151 AADGPAFIEVK 161
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-528 |
8.95e-11 |
|
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: 60.69 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 415 MAIGTAIANPQRkVVGLVGDggLSL--NLGELATLAQEKANVTLLIMNDGGYGVMR----GIQDKYFggRQYYNELHTPD 488
Cdd:cd02009 59 TALGIALATDKP-TVLLTGD--LSFlhDLNGLLLGKQEPLNLTIVVINNNGGGIFSllpqASFEDEF--ERLFGTPQGLD 133
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 502863665 489 FTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVVEVR 528
Cdd:cd02009 134 FEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVK 173
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
357-527 |
5.92e-10 |
|
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: 58.69 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 357 CGVYAQLNdAIEKALPEDGLLVRDIT-VSGSLWGSRLFRargpLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDG 435
Cdd:cd03375 5 CGDGSILK-ALAKALAELGIDPEKVVvVSGIGCSSRLPY----YFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 436 -GLSLNLGELATLAQEKANVTLLIMNDGGYGvMRGIQ-----DKYFGGRqyynelHTPD------FTLLAQAIGLQSWSV 503
Cdd:cd03375 80 dLAAIGGNHFIHAARRNIDITVIVHNNQIYG-LTKGQaspttPEGFKTK------TTPYgnieepFNPLALALAAGATFV 152
|
170 180
....*....|....*....|....*....
gi 502863665 504 ERAEDFD-----AVMTEALAMPGPSVVEV 527
Cdd:cd03375 153 ARGFSGDikqlkEIIKKAIQHKGFSFVEV 181
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
398-525 |
8.28e-09 |
|
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: 55.36 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 398 PLMNIHSLAgAIGMGLPMAIGTAIANPQRKVVGLVGDGGL--SLNLGeLATLAQEKANVTLLIMnDGGYGVMRGIQDKYF 475
Cdd:cd02008 43 PLNAIDTCT-CMGASIGVAIGMAKASEDKKVVAVIGDSTFfhSGILG-LINAVYNKANITVVIL-DNRTTAMTGGQPHPG 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 502863665 476 GGRQYYNELHTPDFTLLAQAIGLQSWSVERAEDFDAV---MTEALAMPGPSVV 525
Cdd:cd02008 120 TGKTLTEPTTVIDIEALVRAIGVKRVVVVDPYDLKAIreeLKEALAVPGVSVI 172
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
357-469 |
9.89e-09 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 56.69 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 357 CGVYAQLnDAIEKALPEDGLLVRDITV-SGSLWGSRLfrarGPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLVGDG 435
Cdd:PRK11866 13 CGNYGIL-EALRKALAELGIPPENVVVvSGIGCSSNL----PEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDG 87
|
90 100 110
....*....|....*....|....*....|....*
gi 502863665 436 -GLSLNLGELATLAQEKANVTLLIMNDGGYGVMRG 469
Cdd:PRK11866 88 dGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTG 122
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
359-527 |
1.06e-08 |
|
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: 55.36 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 359 VYAQLNdaieKALPEDGLLVRDITVSgSLWGSRLFRARGPLMNIH-SLAGAIGMGLPMAIGTAIANPQRKVVGLVGDGGL 437
Cdd:cd02006 13 VYEEMN----KAFGRDVRYVTTIGLS-QIAGAQMLHVYKPRHWINcGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 438 SLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQ---DKYFGGRQYYNELHTP-------DFTLLAQAIGLQSWSVERAE 507
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFENINSSelggygvDHVKVAEGLGCKAIRVTKPE 167
|
170 180
....*....|....*....|....
gi 502863665 508 DFDAVMTEALAMPG----PSVVEV 527
Cdd:cd02006 168 ELAAAFEQAKKLMAehrvPVVVEA 191
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
411-525 |
2.10e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus 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. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 53.65 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 411 MGLPMAIGTAIA-NPQRKVVGLVGDGGLSLNLGELATLAQEKA-NVTLLIMNDGGYGVMrgiqdkyfGGRQYYNElhTPD 488
Cdd:cd02001 44 MGLAGSIGLGLAlGLSRKVIVVDGDGSLLMNPGVLLTAGEFTPlNLILVVLDNRAYGST--------GGQPTPSS--NVN 113
|
90 100 110
....*....|....*....|....*....|....*..
gi 502863665 489 FTLLAQAIGLQSWSVERAEDFDAVMTEALAMPGPSVV 525
Cdd:cd02001 114 LEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
357-527 |
7.74e-07 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 51.00 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 357 CGVYAQLNdAIEKALPEDGLLVRDIT-VSG---SlwgsrlfrARGP-LMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGL 431
Cdd:PRK11867 23 CGDGSILA-ALQRALAELGLDPENVAvVSGigcS--------GRLPgYINTYGFHTIHGRALAIATGLKLANPDLTVIVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 432 VGDG-GLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGiqdkyfggrQY--------------YNELHTPdFTLLAQAI 496
Cdd:PRK11867 94 TGDGdALAIGGNHFIHALRRNIDITYILFNNQIYGLTKG---------QYsptspvgfvtkttpYGSIEPP-FNPVELAL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 502863665 497 GLQSWSVERAEDFDA-----VMTEALAMPGPSVVEV 527
Cdd:PRK11867 164 GAGATFVARGFDSDVkqlteLIKAAINHKGFSFVEI 199
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-165 |
8.73e-07 |
|
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: 48.88 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSGLGVALTSTGAGAGNAVGALVE 88
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863665 89 AMNACTPLLHLTGQVEKAWLDADTgfiHETRDQLTFLKASSKRAYRISNASQAIAILHKAIQEAQTPPcGPVSVEIP 165
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQT---FQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQ-GPVVVRLP 153
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
357-527 |
1.57e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 49.88 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 357 CGVYAQLNdAIEKALPEDGLLVRDIT-VSG---SlwgSRLfrarGPLMNIHSLAGAIGMGLPMAIGTAIANPQRKVVGLV 432
Cdd:PRK05778 24 CGNFGILN-AIIQALAELGLDPDKVVvVSGigcS---SKI----PGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 433 GDG-GLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGiQ-----DKYFGGR--QYYNELhtPDFTLLAQAIGLQSWSVE 504
Cdd:PRK05778 96 GDGdLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKG-QaspttPEGSKTKtaPYGNIE--PPIDPCALALAAGATFVA 172
|
170 180
....*....|....*....|....*...
gi 502863665 505 RAEDFDA-----VMTEALAMPGPSVVEV 527
Cdd:PRK05778 173 RSFAGDVkqlveLIKKAISHKGFAFIDV 200
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
357-527 |
8.68e-05 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 44.36 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 357 CGVYAQLNdAIEKALPEdgLLVRDITV-------SGSLWGSrlfrargplMNIHSLAGAIGMGLPMAIGTAIANPQRKVV 429
Cdd:COG1013 19 CGHGIILR-LLLKALDE--LLDGDKTVvvsgigcSSVAPGY---------FNVPGFHTLHGRAAAVATGIKLANPDLTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 430 GLVGDGGL-SLNLGELATLAQEKANVTLLIMNDGGYGvMRGIQ-----DKYF------GGrqyyNELHTPDFTLLAQAIG 497
Cdd:COG1013 87 VFGGDGDTyDIGGNHLIHAARRNEDITYIVYDNEIYG-NTGGQrspttPLGAkttttpYG----KPEPPKDPAEIAAAHG 161
|
170 180 190
....*....|....*....|....*....|...
gi 502863665 498 ---LQSWSVERAEDFDAVMTEALAMPGPSVVEV 527
Cdd:COG1013 162 atyVARASVGDPKDLKKKIKKAIEHKGFSFIEV 194
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
407-496 |
2.41e-03 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 40.45 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 407 GAIGMGLPMAIGTAIANPQRKVVGLVGDGGLSLNLGELATLAQEKANVTLLIMNDGGYGVMRGIQDKyfggrqYYNELHT 486
Cdd:PLN02573 428 GSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIHDG------PYNVIKN 501
|
90
....*....|
gi 502863665 487 PDFTLLAQAI 496
Cdd:PLN02573 502 WNYTGLVDAI 511
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
9-166 |
3.02e-03 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 38.63 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 9 DAIARTLEQYQVEAIYGVISIHNLPIADAVGQRGNIRFVPARGEAGSVTMADAHGRFSGLGVALT-------Stgagagn 81
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTtygvgelS------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863665 82 avgalveAMNAC-------TPLLHLTGQ-----VEKAWLdadtgfIHET---RDQLTFLKASSK---RAYRISNASQAIA 143
Cdd:cd07038 74 -------ALNGIagayaehVPVVHIVGApstkaQASGLL------LHHTlgdGDFDVFLKMFEEitcAAARLTDPENAAE 140
|
170 180
....*....|....*....|...
gi 502863665 144 ILHKAIQEAQTpPCGPVSVEIPI 166
Cdd:cd07038 141 EIDRVLRTALR-ESRPVYIEIPR 162
|
|
| |
