|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
31-589 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 779.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 31 LNDMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGK-IKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGA 109
Cdd:PRK07282 6 LESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEgIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 110 TNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVI 189
Cdd:PRK07282 86 TNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 190 DFPKDMGVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK07282 166 DLPKDVSALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGII 349
Cdd:PRK07282 246 LGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 350 ADCKRFLECLNDKNVETIEHSDWVKHCQNNKQKHPFKlgEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFY 429
Cdd:PRK07282 326 GDAKKALQMLLAEPTVHNNTEKWIEKVTKDKNRVRSY--DKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 430 PFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQD 509
Cdd:PRK07282 404 PYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 510 KFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDaAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEMEGL 589
Cdd:PRK07282 484 SFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLE-VITEDVPMLIEVDISRKEHVLPMVPAGKSNHEMLGV 562
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
17-589 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 767.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 17 MAESLELEQLNEKTlndMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSG 96
Cdd:PRK07710 1 TNVMRTMSSKTEEK---LMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 97 KTGVVVVTSGPGATNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAF 176
Cdd:PRK07710 78 KPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 177 HVANSGRKGPVVIDFPKDMGVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQ 256
Cdd:PRK07710 158 HIATTGRPGPVLIDIPKDMVVEEGEFCYDVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 257 FVNKHQIPTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPS 336
Cdd:PRK07710 238 YAEQQEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 337 EINKVIHVDLGIIADCKRFLECLNDKNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTT 416
Cdd:PRK07710 318 EIGKNVPTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESI-KPQKAIEMLYEITKGEAIVTT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 417 DVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLI 496
Cdd:PRK07710 397 DVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVIL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 497 NNGTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPM 576
Cdd:PRK07710 477 NNEALGMVRQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPM 556
|
570
....*....|...
gi 445969956 577 VPSGKSNHEMEGL 589
Cdd:PRK07710 557 VAPGKGLHEMVGV 569
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
34-586 |
0e+00 |
|
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: 760.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNV 112
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 113 MTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFP 192
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 193 KDMGVLATNVDLcDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGL 272
Cdd:COG0028 162 KDVQAAEAEEEP-APPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 273 GAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADC 352
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 353 KRFLECLNDK-NVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPF 431
Cdd:COG0028 321 KAVLAALLEAlEPRADDRAAWLARIAAWRAEYLAAYAADDGPI-KPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 432 KNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKF 511
Cdd:COG0028 400 RRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELF 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445969956 512 FNQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEavtpmVPSGKSNHEM 586
Cdd:COG0028 480 YGGRYSGTDL-PNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEE-----NPPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
36-589 |
0e+00 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 740.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFY-DGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:TIGR00118 162 VTTAEIEYPYPEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:TIGR00118 242 FPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDARN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLNDKNVETIEHSD--WVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFK 432
Cdd:TIGR00118 322 VLEELLKKLFELKERKEsaWLEQINKWKKEYPLKMDYTEEGI-KPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 433 NHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFF 512
Cdd:TIGR00118 401 KPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELFY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 513 NQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEMEGL 589
Cdd:TIGR00118 481 EERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMIGE 557
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
17-589 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 665.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 17 MAESLELEQLNEKTLNDMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFY----DGKIKHILARHEQGAVHAAEGYA 92
Cdd:PRK07418 1 LTSSPPKIGDSTTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 93 RVSGKTGVVVVTSGPGATNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIV 172
Cdd:PRK07418 81 RATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 173 HEAFHVANSGRKGPVVIDFPKDMGvlatnVDLCD-------EINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGI 245
Cdd:PRK07418 161 AEAFHIASSGRPGPVLIDIPKDVG-----QEEFDyvpvepgSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 246 NQSKSNQLLTQFVNKHQIPTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPN 325
Cdd:PRK07418 236 ISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 326 AKIVHVDIDPSEINKVIHVDLGIIADCKRFLECLNDKNVE-TIEH--SDWVKHCQNNKQKHPFKL-GEEDQVFckPQQTI 401
Cdd:PRK07418 316 AKVIHIDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLEpTTPPrtQAWLERINRWKQDYPLVVpPYEGEIY--PQEVL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 402 EYIGKITNgEAIVTTDVGQHQMWAAQFypFKNhG--QWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQ 479
Cdd:PRK07418 394 LAVRDLAP-DAYYTTDVGQHQMWAAQF--LRN-GprRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 480 EMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHS-VFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQ 558
Cdd:PRK07418 470 ELGTLAQYGINVKTVIINNGWQGMVRQWQESFYGERYSASnMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHD 549
|
570 580 590
....*....|....*....|....*....|.
gi 445969956 559 GPVLIEVRISPTEAVTPMVPSGKSNHEMEGL 589
Cdd:PRK07418 550 GPVLIDVHVRRDENCYPMVPPGKSNAQMVGL 580
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
36-586 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 657.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGK-IKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK08527 4 SGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNyFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK08527 84 GLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:PRK08527 164 VTATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMARGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK08527 244 LRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDLKN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLND--KNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFK 432
Cdd:PRK08527 324 VLKEMLEelKEENPTTYKEWREILKRYNELHPLSYEDSDEVL-KPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 433 NHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFF 512
Cdd:PRK08527 403 YPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTFFY 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445969956 513 NQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEM 586
Cdd:PRK08527 483 EERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNM 556
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
36-586 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 648.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTG 115
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 116 ITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDM 195
Cdd:PRK06725 96 LADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 196 GVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAV 275
Cdd:PRK06725 176 QNEKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 276 PYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKRF 355
Cdd:PRK06725 256 PPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKKA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 356 LECLNDKNVETiEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHG 435
Cdd:PRK06725 336 LHMLLHMSIHT-QTDEWLQKVKTWKEEYPLSYKQKESEL-KPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 436 QWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQR 515
Cdd:PRK06725 414 TFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFYENR 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445969956 516 FSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEM 586
Cdd:PRK06725 494 LSESKI-GSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEM 563
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
35-586 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 645.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 35 RSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 mgVLATNVDLCDEINIPGYEvvTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:PRK08978 161 --IQLAEGELEPHLTTVENE--PAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK08978 237 VEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLNdknvETIEHSDWVKHCQNNKQKHPFKLGEEDQVFCKPqQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNH 434
Cdd:PRK08978 317 LLPALQ----QPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAP-ALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 435 GQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQ 514
Cdd:PRK08978 392 ENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445969956 515 RFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEM 586
Cdd:PRK08978 472 RYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEM 543
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
37-589 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 634.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDMG 196
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 197 VLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAVP 276
Cdd:PRK06048 170 TAEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGIGAIP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 277 YEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKRFL 356
Cdd:PRK06048 250 TEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVGDAKQVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 357 ECLNdKNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNgEAIVTTDVGQHQMWAAQFYPFKNHGQ 436
Cdd:PRK06048 330 KSLI-KYVQYCDRKEWLDKINQWKKEYPLKYKEREDVI-KPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKYKYPRT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 437 WVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRF 516
Cdd:PRK06048 407 FITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELFYDKRY 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445969956 517 SHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEMEGL 589
Cdd:PRK06048 487 SHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILDL 559
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
36-585 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 629.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDG-KIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:PRK07789 192 ALQAQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMARGA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK07789 272 FPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPIVGDVKE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLND------KNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQF 428
Cdd:PRK07789 352 VIAELIAalraehAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 429 YPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQ 508
Cdd:PRK07789 432 IDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVRQWQ 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 509 DKFFNQRFSHSVFNGQ----PDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQG-PVLIEVRISPTEAVTPMVPSGKSN 583
Cdd:PRK07789 512 TLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDrPVVIDFVVGKDAMVWPMVAAGTSN 591
|
..
gi 445969956 584 HE 585
Cdd:PRK07789 592 DE 593
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
36-586 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 628.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDT-FYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEiFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGvLATNVDLCDEINI--PGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQS--KSNQLLTQFVNKHQIPTVTTLL 270
Cdd:PRK09107 172 VQ-FATGTYTPPQKAPvhVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITSTLM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 271 GLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIA 350
Cdd:PRK09107 251 GLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPIIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 351 DCKRFLECL------NDKNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNG-EAIVTTDVGQHQM 423
Cdd:PRK09107 331 DVGHVLEDMlrlwkaRGKKPDKEALADWWGQIARWRARNSLAYTPSDDVI-MPQYAIQRLYELTKGrDTYITTEVGQHQM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 424 WAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGM 503
Cdd:PRK09107 410 WAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 504 VKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSN 583
Cdd:PRK09107 490 VRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIPSGKAH 569
|
...
gi 445969956 584 HEM 586
Cdd:PRK09107 570 NEM 572
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
26-589 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 624.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 26 LNEKTLNDMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFY----DGKIKHILARHEQGAVHAAEGYARVSGKTGVV 101
Cdd:CHL00099 1 MMNQLTLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 102 VVTSGPGATNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANS 181
Cdd:CHL00099 81 FATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 182 GRKGPVVIDFPKDMGVLATNVDLC----DEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQF 257
Cdd:CHL00099 161 GRPGPVLIDIPKDVGLEKFDYYPPepgnTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 258 VNKHQIPTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSE 337
Cdd:CHL00099 241 AELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 338 INKVIHVDLGIIADCKR----FLECL--NDKNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNgE 411
Cdd:CHL00099 321 IGKNRIPQVAIVGDVKKvlqeLLELLknSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSL-SPQEVINEISQLAP-D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 412 AIVTTDVGQHQMWAAQFYPFKNhGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDV 491
Cdd:CHL00099 399 AYFTTDVGQHQMWAAQFLKCKP-RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 492 KIVLINNGTLGMVKQWQDKFFNQRFSHS-VFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPT 570
Cdd:CHL00099 478 KIIIINNKWQGMVRQWQQAFYGERYSHSnMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIED 557
|
570
....*....|....*....
gi 445969956 571 EAVTPMVPSGKSNHEMEGL 589
Cdd:CHL00099 558 ENCYPMVAPGKSNSQMIGI 576
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
37-580 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 622.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDMG 196
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 197 VLATNVD---LCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLG 273
Cdd:PRK06276 163 EGELDLEkypIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 274 AVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCK 353
Cdd:PRK06276 243 AFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGDAK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 354 RFLECLNDK--NVETIEHSDWVKHCQNNKQKHPFKLgEEDQVFCKPQQTIEYI-----GKITNGEAIVTTDVGQHQMWAA 426
Cdd:PRK06276 323 NVLRDLLAElmKKEIKNKSEWLERVKKLKKESIPRM-DFDDKPIKPQRVIKELmevlrEIDPSKNTIITTDVGQNQMWMA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 427 QFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQ 506
Cdd:PRK06276 402 HFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVYQ 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445969956 507 WQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVtPMVPSG 580
Cdd:PRK06276 482 WQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPG 554
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
36-588 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 601.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTF-YDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK08155 14 TGAELIVRLLERQGIRIVTGIPGGAILPLYDALsQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK08155 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVLATNVDLCDEINIPgyEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:PRK08155 174 VQTAVIELEALPAPAEK--DAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK08155 252 LPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLNDKnVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFCkPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNH 434
Cdd:PRK08155 332 VLAQLLPL-VEAQPRAEWHQLVADLQREFPCPIPKADDPLS-HYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 435 GQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQ 514
Cdd:PRK08155 410 RQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFYGQ 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445969956 515 RFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSGKSNHEMEG 588
Cdd:PRK08155 490 RVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTEMIG 563
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
33-586 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 583.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 33 DMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDT-FYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATN 111
Cdd:PRK06466 2 ELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDAlFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 112 VMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDF 191
Cdd:PRK06466 82 AITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 192 PKDMGVLATNVDLC--DEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK06466 162 PKDMTNPAEKFEYEypKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGII 349
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 350 ADCKR-------FLECLNDK-NVETIehSDWVKHCQNNKQKH---PFKLGEEDQVfcKPQQTIEYIGKITNGEAIVTTDV 418
Cdd:PRK06466 322 GPVESvltemlaILKEIGEKpDKEAL--AAWWKQIDEWRGRHglfPYDKGDGGII--KPQQVVETLYEVTNGDAYVTSDV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 419 GQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINN 498
Cdd:PRK06466 398 GQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 499 GTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQ-GPVLIEVRISPTEAVTPMV 577
Cdd:PRK06466 478 GALGMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKdRLVFIDIYVDRSEHVYPMQ 557
|
....*....
gi 445969956 578 PSGKSNHEM 586
Cdd:PRK06466 558 IADGSMRDM 566
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
37-586 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 559.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFY-DGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTG 115
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 116 ITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDM 195
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 196 GVLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAV 275
Cdd:PRK06965 183 SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLGAY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 276 PYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNA-KIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK06965 263 PASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVGDVKE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLNDKNVETIEHSD------WVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQF 428
Cdd:PRK06965 343 VLKELIEQLQTAEHGPDadalaqWWKQIEGWRSRDCLKYDRESEII-KPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 429 YPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQ 508
Cdd:PRK06965 422 YRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVRQWQ 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445969956 509 DKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQG-PVLIEVRISPTEAVTPMVPSGKSNHEM 586
Cdd:PRK06965 502 EIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDrTVFLDFQTDPTENVWPMVQAGKGITEM 580
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
33-586 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 552.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 33 DMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATN 111
Cdd:PRK08979 2 EMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 112 VMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDF 191
Cdd:PRK08979 82 TITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 192 PKDMGVLATNVDLC--DEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK08979 162 PKDCLNPAILHPYEypESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGII 349
Cdd:PRK08979 242 MGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 350 ADCKRFLECLNDKNVETIEHSD------WVKHCQNNKQKHPFKLgEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQM 423
Cdd:PRK08979 322 GSADKVLDSMLALLDESGETNDeaaiasWWNEIEVWRSRNCLAY-DKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 424 WAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGM 503
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 504 VKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGP-VLIEVRISPTEAVTPMVPSGKS 582
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRlVFVDINVDETEHVYPMQIRGGA 560
|
....
gi 445969956 583 NHEM 586
Cdd:PRK08979 561 MNEM 564
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
36-586 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 545.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK06882 5 SGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK06882 85 GIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVLATNV--DLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGL 272
Cdd:PRK06882 165 MVNPANKFtyEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 273 GAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADC 352
Cdd:PRK06882 245 GAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVGSA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 353 KR----FLECLNDKNVETIEH--SDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMWAA 426
Cdd:PRK06882 325 KNvleeFLSLLEEENLAKSQTdlTAWWQQINEWKAKKCLEFDRTSDVI-KPQQVVEAIYRLTNGDAYVASDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 427 QFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQ 506
Cdd:PRK06882 404 LHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 507 WQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGP-VLIEVRISPTEAVTPMVPSGKSNHE 585
Cdd:PRK06882 484 WQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKlVFVDVNVDETEHVYPMQIRGGAMNE 563
|
.
gi 445969956 586 M 586
Cdd:PRK06882 564 M 564
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
35-582 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 540.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 35 RSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGK-IKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVM 113
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 114 TGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPK 193
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 194 DMGVLATNVDLCDEINIPGY--EVVTEPENKDIDTFISLLKEAKKPVVLAGAG-INQSKSnqlLTQFVNKHQIPTVTTLL 270
Cdd:PLN02470 173 DIQQQLAVPNWNQPMKLPGYlsRLPKPPEKSQLEQIVRLISESKRPVVYVGGGcLNSSEE---LREFVELTGIPVASTLM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 271 GLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEI--NKVIHVdlGI 348
Cdd:PLN02470 250 GLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIgkNKQPHV--SV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 349 IADCKRFLECLN----DKNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQHQMW 424
Cdd:PLN02470 328 CADVKLALQGLNklleERKAKRPDFSAWRAELDEQKEKFPLSYPTFGDAI-PPQYAIQVLDELTDGNAIISTGVGQHQMW 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 425 AAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMV 504
Cdd:PLN02470 407 AAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMV 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 505 KQWQDKFFNQRFSHSVFNGQ-------PDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMV 577
Cdd:PLN02470 487 VQWEDRFYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMI 566
|
....*
gi 445969956 578 PSGKS 582
Cdd:PLN02470 567 PGGGT 571
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
33-586 |
3.62e-178 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 515.94 E-value: 3.62e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 33 DMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATN 111
Cdd:PRK07979 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 112 VMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDF 191
Cdd:PRK07979 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 192 PKDMGVLATNVDLC--DEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAG-INQSKSNQLLTqFVNKHQIPTVTT 268
Cdd:PRK07979 162 PKDILNPANKLPYVwpESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGaINAACHQQLKE-LVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 269 LLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGI 348
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 349 IADCKRFLECLND--------KNVETIEhsDWVKHCQNNKQKHPFKLGEEDQVFcKPQQTIEYIGKITNGEAIVTTDVGQ 420
Cdd:PRK07979 321 VGDARQVLEQMLEllsqesahQPLDEIR--DWWQQIEQWRARQCLKYDTHSEKI-KPQAVIETLWRLTKGDAYVTSDVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 421 HQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGT 500
Cdd:PRK07979 398 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 501 LGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAY---QGPVLIEVRISPTEAVTPMV 577
Cdd:PRK07979 478 LGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQ 557
|
....*....
gi 445969956 578 PSGKSNHEM 586
Cdd:PRK07979 558 IRGGGMDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
34-586 |
9.03e-140 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 417.70 E-value: 9.03e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD----GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGA 109
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlanGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 110 TNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVI 189
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 190 DFPKDmgVLATNVDLCDEIN---IPGY-EVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPT 265
Cdd:PRK06456 161 DIPRD--IFYEKMEEIKWPEkplVKGYrDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 266 VTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDR-LASKPDAFAPNAKIVHVDIDPSEINKVIHV 344
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRtFTSYDEMVETRKKFIMVNIDPTDGEKAIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 345 DLGIIADCKRFLECLNdKNVETI----EHSDWVKHCQNNKQKHPFKLGEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQ 420
Cdd:PRK06456 319 DVGIYGNAKIILRELI-KAITELgqkrDRSAWLKRVKEYKEYYSQFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 421 HQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGT 500
Cdd:PRK06456 398 HQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 501 LGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTPMVPSG 580
Cdd:PRK06456 478 LGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPG 557
|
....*.
gi 445969956 581 KSNHEM 586
Cdd:PRK06456 558 GRLKQV 563
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
37-565 |
7.19e-126 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 381.10 E-value: 7.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDmg 196
Cdd:PRK08322 83 AYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 197 VLAtnvDLCDEINIP-GYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAV 275
Cdd:PRK08322 161 IAA---EETDGKPLPrSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 276 PYEDTLFLG-MGGMHGSYAsNMALTECDLLINLGsrFDdrLASKPDAF-APNA--KIVHVDIDPSEINKVIHVDLGIIAD 351
Cdd:PRK08322 238 PETHPLSLGtAGLSQGDYV-HCAIEHADLIINVG--HD--VIEKPPFFmNPNGdkKVIHINFLPAEVDPVYFPQVEVVGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 352 CKRFLECLNDKnVETIEHSDWV--KHCQNNKQKHpFKLGEEDQVF-CKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQF 428
Cdd:PRK08322 313 IANSLWQLKER-LADQPHWDFPrfLKIREAIEAH-LEEGADDDRFpMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 429 YPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQ 508
Cdd:PRK08322 391 YRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 445969956 509 DkffNQRFSHSVFN-GQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:PRK08322 471 E---NMGFEDFGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDC 525
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
34-575 |
3.67e-123 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 374.21 E-value: 3.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNV 112
Cdd:PRK08199 7 ARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDeTDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 113 MTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFP 192
Cdd:PRK08199 87 SIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 193 KDMgvlatnvdLCDEINIPG---YEVV-TEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTT 268
Cdd:PRK08199 167 EDV--------LSETAEVPDappYRRVaAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 269 LLGLGAVPYEDTLFLGmggmHGSYASNMALT----ECDLLINLGSRFDD------RLASKPdafAPNAKIVHVDIDPSEI 338
Cdd:PRK08199 239 FRRQDLFDNRHPNYAG----DLGLGINPALAarirEADLVLAVGTRLGEvttqgyTLLDIP---VPRQTLVHVHPDAEEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 339 NKVIHVDLGIIADCKRFLECLND-KNVETIEHSDWVkhcqnnKQKHpfklgEEDQVFCKPQ---------QTIEYIGKIT 408
Cdd:PRK08199 312 GRVYRPDLAIVADPAAFAAALAAlEPPASPAWAEWT------AAAH-----ADYLAWSAPLpgpgavqlgEVMAWLRERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 409 NGEAIVTTDVGQHQMWAAQFYPFKNHGQWV--TSgglGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPE 486
Cdd:PRK08199 381 PADAIITNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 487 YGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVR 566
Cdd:PRK08199 458 YGLPIIVIVVNNGMYGTIRMHQEREYPGRVSGTDL-TNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIR 536
|
....*....
gi 445969956 567 ISPtEAVTP 575
Cdd:PRK08199 537 IDP-EAITP 544
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
42-574 |
1.64e-115 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 355.83 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 42 VEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVS-GKTGVVVVTSGPGATNVMTGITDA 119
Cdd:PRK11269 11 VLVLEKEGVTTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGLYSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 120 HCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDMGVLA 199
Cdd:PRK11269 91 SADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQVAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 200 TNVDLCDEINIPGYEVvtEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAVPYED 279
Cdd:PRK11269 171 IEFDPDTYEPLPVYKP--AATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 280 TLFLGMGGMHGS--YAsNMALTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKRFLE 357
Cdd:PRK11269 249 PLMAGMVGLQTShrYG-NATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVSDAKAALE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 358 CLNDKNVETI------EHSDWVKHCQNNKQ----KHPFklgeeDQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQ 427
Cdd:PRK11269 328 LLVEVAREWKaagrlpDRSAWVADCQERKRtllrKTHF-----DNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 428 FYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQW 507
Cdd:PRK11269 403 FLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 508 QDKF---FNQRFSHSVFNGQP------DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFA----YQGPVLIEVRIsptEAVT 574
Cdd:PRK11269 483 QRAFdmdYCVQLAFENINSPElngygvDHVKVAEGLGCKAIRVFKPEDIAPALEQAKAlmaeFRVPVVVEVIL---ERVT 559
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
396-580 |
1.68e-111 |
|
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: 331.00 E-value: 1.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 396 KPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQ 475
Cdd:cd02015 2 KPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 476 MTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAF 555
Cdd:cd02015 82 MNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEAL 161
|
170 180
....*....|....*....|....*
gi 445969956 556 AYQGPVLIEVRISPTEAVTPMVPSG 580
Cdd:cd02015 162 ASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
37-575 |
3.93e-108 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 336.20 E-value: 3.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVlplyDTFYDG------KIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGAT 110
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSI----DAVVDAlrkeqdKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 111 NVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSgRKGPVVID 190
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 191 FPKDmgVLATNVDLCDEINIPGY-EVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKsnQLLTQFVNKHQIPTVTTL 269
Cdd:PRK08611 161 IPDD--LPAQKIKDTTNKTVDTFrPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIHTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRlaskpdAFAPN-AKIVHVDIDPSEINKVIHVDLGI 348
Cdd:PRK08611 237 PAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 349 IADCKRFLECLNDkNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFC---KPQQTIEYIGKITNGEAIVTTDVGQHQMWA 425
Cdd:PRK08611 311 VGDAKKALHQLTE-NIKHVEDRRFLEACQENMAKWWKWMEEDENNAStpiKPERVMAAIQKIADDDAVLSVDVGTVTVWS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 426 AQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVK 505
Cdd:PRK08611 390 ARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIK 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 506 QWQDKFFNQRFSHSVFNgqPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVTP 575
Cdd:PRK08611 470 YEQQAAGELEYAIDLSD--MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLP 537
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
36-575 |
4.79e-91 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 290.76 E-value: 4.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD--GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVM 113
Cdd:PRK08266 5 TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKagDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 114 TGITDAHCDSLPLVVFTGQVATPGIGKDAFQ--E-ADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVID 190
Cdd:PRK08266 85 AALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEmPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 191 FPKDmgVLATNVDlcDEINIPGYEVVTEPENKD-IDTFISLLKEAKKPVVLAGAGinQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK08266 165 MPWD--VFGQRAP--VAAAPPLRPAPPPAPDPDaIAAAAALIAAAKNPMIFVGGG--AAGAGEEIRELAEMLQAPVVAFR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMggmhgsYASNMALTECDLLINLGSRFDD---RLASKPDafapNAKIVHVDIDPSEINKVIhVDL 346
Cdd:PRK08266 239 SGRGIVSDRHPLGLNF------AAAYELWPQTDVVIGIGSRLELptfRWPWRPD----GLKVIRIDIDPTEMRRLK-PDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 347 GIIADCKRFLECLNDKNVETiehsdwvkhcqnnKQKHPFKLGE--------EDQVF-CKPQqtIEYIGKITNG---EAIV 414
Cdd:PRK08266 308 AIVADAKAGTAALLDALSKA-------------GSKRPSRRAElrelkaaaRQRIQaVQPQ--ASYLRAIREAlpdDGIF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 415 TTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIV 494
Cdd:PRK08266 373 VDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTV 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 495 LINNGTLGMVKQWQDKFFNQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEAVT 574
Cdd:PRK08266 453 VFNNNAYGNVRRDQKRRFGGRVVASDL-VNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEAS 531
|
.
gi 445969956 575 P 575
Cdd:PRK08266 532 P 532
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
37-565 |
1.47e-90 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 289.34 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDmg 196
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 197 VLATNVdlcDEINIP--GYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:TIGR02418 159 VVDSPV---SVKAIPasYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VP--YEDTlFLGMGGMHGSYASNMALTECDLLINLGsrFDdrlaskPDAFAP-------NAKIVHVDIDPSEINKVIHVD 345
Cdd:TIGR02418 236 VSreLEDH-FFGRVGLFRNQPGDRLLKQADLVITIG--YD------PIEYEPrnwnsenDATIVHIDVEPAQIDNNYQPD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 346 LGIIADCKRFLECLNDKNVET----------------IEHSDWVKHCQNNKQKHPFKLgeedqvfckpqqtIEYIGKITN 409
Cdd:TIGR02418 307 LELVGDIASTLDLLAERIPGYelppdalailedlkqqREALDRVPATLKQAHLHPLEI-------------IKAMQAIVT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 410 GEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGL 489
Cdd:TIGR02418 374 DDVTVTVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKL 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 490 DVKIVLINNGTLGMVK-QWQDKFfnQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:TIGR02418 454 NIVHIIWNDNGYNMVEfQEEMKY--QRSSGVDF-GPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDI 527
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
34-578 |
2.91e-89 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 286.34 E-value: 2.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVM 113
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 114 TGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSgRKGPVVIDFPK 193
Cdd:PRK06457 81 NGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 194 DMGVLATNVDLCDEINIPGYEVvtepeNKDIDTFISLLKEAKKPVVLAGAGInQSKSNQLLtQFVNKHQIPTVTTLLGLG 273
Cdd:PRK06457 160 DILRKSSEYKGSKNTEVGKVKY-----SIDFSRAKELIKESEKPVLLIGGGT-RGLGKEIN-RFAEKIGAPIIYTLNGKG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 274 AVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFddrlaskP-DAFAP-NAKIVHVDIDPSEINKVIHVDLGIIAD 351
Cdd:PRK06457 233 ILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSF-------PyVNFLNkSAKVIQVDIDNSNIGKRLDVDLSYPIP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 352 CKRFL----ECLNDKNVETI--EHSDWVKHC--QNNKQKHPFklgeedqvfcKPQQTIEYIGKITNGEAIVTTDVGQHQM 423
Cdd:PRK06457 306 VAEFLnidiEEKSDKFYEELkgKKEDWLDSIskQENSLDKPM----------KPQRVAYIVSQKCKKDAVIVTDTGNVTM 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 424 WAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLA-NPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLG 502
Cdd:PRK06457 376 WTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLG 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 503 MVKQWQDKFFNQRFSHSVFNgqPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEavTPMVP 578
Cdd:PRK06457 456 MIKFEQEVMGYPEWGVDLYN--PDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNE--RPMPP 527
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
38-567 |
4.37e-88 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 284.20 E-value: 4.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 38 SEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGIT 117
Cdd:PRK07525 9 SEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 118 DAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKqnYQVkRVED---IPKIVHEAFHVANSGRkGPVVIDFPKD 194
Cdd:PRK07525 89 TAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTK--YQE-EVRDpsrMAEVLNRVFDKAKRES-GPAQINIPRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 M--GVLatnvdlcdEINIP---GYEVVTEPENKdIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK07525 165 YfyGVI--------DVEIPqpvRLERGAGGEQS-LAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDrLASKP----DAFAPNAKIVHVDIDPSEINKVIHVD 345
Cdd:PRK07525 236 LHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNP-FGTLPqygiDYWPKDAKIIQVDINPDRIGLTKKVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 346 LGIIADCKRFLECL-------------NDKNVETI--EHSDWVK------HCQNNKQKHPFKLG-EEDQVFCKPQQTIEY 403
Cdd:PRK07525 315 VGICGDAKAVARELlarlaerlagdagREERKALIaaEKSAWEQelsswdHEDDDPGTDWNEEArARKPDYMHPRQALRE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 404 IGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMAL 483
Cdd:PRK07525 395 IQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 484 LPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQG---P 560
Cdd:PRK07525 475 AVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQNegkT 554
|
....*..
gi 445969956 561 VLIEVRI 567
Cdd:PRK07525 555 TVIEIMC 561
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
38-565 |
1.92e-86 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 279.82 E-value: 1.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 38 SEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGIT 117
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 118 DAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRkGPVVIDFPKDM-- 195
Cdd:TIGR03457 85 AAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYfy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 196 GVLATNVDLCDEINI-PGYEvvtepenKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGA 274
Cdd:TIGR03457 164 GEIDVEIPRPVRLDRgAGGA-------TSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDrLASKP----DAFAPNAKIVHVDIDPSEINKVIHVDLGIIA 350
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGP-FGTLPqygiDYWPKNAKIIQVDANAKMIGLVKKVTVGICG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 351 DCK----RFLECL--------NDKNVETI--EHSDWVKHCQN-NKQKHPFKL------GEEDQVFCKPQQTIEYIGKITN 409
Cdd:TIGR03457 316 DAKaaaaEILQRLagkagdanRAERKAKIqaERSAWEQELSEmTHERDPFSLdmiveqRQEEGNWLHPRQVLRELEKAMP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 410 GEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGL 489
Cdd:TIGR03457 396 EDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDI 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445969956 490 DVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQG---PVLIEV 565
Cdd:TIGR03457 476 PVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAegkTTVIEI 554
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
35-565 |
3.19e-86 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 278.28 E-value: 3.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 35 RSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MgvlatnvdLCDEINIPGYEVVTEPEN-----KDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTL 269
Cdd:PRK08617 165 V--------VDAPVTSKAIAPLSKPKLgpaspEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAV--PYEDTlFLGMGGMHGSYASNMALTECDLLINLGS---RFDDRLASKPdafaPNAKIVHVDIDPSEINKVIHV 344
Cdd:PRK08617 237 QAAGVIsrELEDH-FFGRVGLFRNQPGDELLKKADLVITIGYdpiEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 345 DLGIIADCKRFLECLNDKNVETI---EHSDWVKHCQNNKQKHPFKLGEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQH 421
Cdd:PRK08617 312 ERELIGDIAATLDLLAEKLDGLSlspQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 422 QMWAAQ-FYPFKNHgQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGT 500
Cdd:PRK08617 392 YIWMARyFRSYEPR-HLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGH 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 501 LGMVK-QWQDKFfnQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:PRK08617 471 YNMVEfQEEMKY--GRSSGVDF-GPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDI 533
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
37-571 |
2.90e-84 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 274.02 E-value: 2.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGK--IKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMT 114
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERdrIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 115 GITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSgRKGPVVIDFPKD 194
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 MGVlaTNVDLCDEINIPGYEVVT---EPENKDIDTFISLLKEAKKPVVLAGAGinQSKSNQLLTQFVNKHQIPTVTTLLG 271
Cdd:TIGR02720 160 FGW--QEIPDNDYYASSVSYQTPllpAPDVEAVTRAVQTLKAAERPVIYYGIG--ARKAGEELEALSEKLKIPLISTGLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 272 LGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDdrLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIAD 351
Cdd:TIGR02720 236 KGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 352 CKRFLECLNDKnVETIEHSDWVKHCQNNKQ---KHPFKLGEEDQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQF 428
Cdd:TIGR02720 314 AKKALAAILAQ-VEPRESTPWWQANVANVKnwrAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 429 YPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQ 508
Cdd:TIGR02720 393 LKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQ 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 509 DKfFNQRFSHSVFNgQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQG--PVLIEVRIS-----PTE 571
Cdd:TIGR02720 473 ED-TNQPLIGVDFN-DADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIKQgkPVLIDAKITgdrplPVE 540
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
39-193 |
2.29e-75 |
|
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: 236.66 E-value: 2.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 39 EVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGITD 118
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445969956 119 AHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPK 193
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
34-565 |
7.07e-72 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 240.26 E-value: 7.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVM 113
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 114 TGITDAHCDSLPLVVFTG--QVATPGIGKDAFQE-ADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVID 190
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSvnRRASLGKGRGKLHElPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 191 FPKDMGVLATNVDLCDEINIPGYEvvtEPENKDIDTFISLLKEAKKPVVLAGAG-INQSKSnqlLTQFVNKHQIPTVTTL 269
Cdd:PRK07524 161 IPLDVLAAPADHLLPAPPTRPARP---GPAPAALAQAAERLAAARRPLILAGGGaLAAAAA---LRALAERLDAPVALTI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 270 LGLGAVPYEDTLFLGMGgmhGSYASNMAL-TECDLLINLGSR---------FDDRlaskpdaFAPNAKIVHVDIDPSEIN 339
Cdd:PRK07524 235 NAKGLLPAGHPLLLGAS---QSLPAVRALiAEADVVLAVGTElgetdydvyFDGG-------FPLPGELIRIDIDPDQLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 340 KVIHVDLGIIADCKRFLECLNDKNVETIEHSDW-------VKHCQNNKQKHPFklgeedqvfckpQQTIEYIGKITNG-- 410
Cdd:PRK07524 305 RNYPPALALVGDARAALEALLARLPGQAAAADWgaarvaaLRQALRAEWDPLT------------AAQVALLDTILAAlp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 411 EAIVTTDVGQHQMWAAQFYPFKNHGQWVTSG-GLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGL 489
Cdd:PRK07524 373 DAIFVGDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 490 DVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNgqPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:PRK07524 453 PLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYT--PDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
37-572 |
4.40e-69 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 233.07 E-value: 4.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKDMG 196
Cdd:PRK05858 87 AAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 197 vlatnVDLCDEINIPGYEVV----TEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGL 272
Cdd:PRK05858 167 -----FSMADDDGRPGALTElpagPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 273 GAVPYEDTLFLgmggmhgSYASNMALTECDLLINLGSRFDDRLASkpDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADC 352
Cdd:PRK05858 242 GVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRLGF--GVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 353 KRFLECLNDKNVETIEHSDWVKHCQNNKQKHPFKLGEE---DQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFY 429
Cdd:PRK05858 313 SAILSALAGAGGDRTDHQGWIEELRTAETAARARDAAEladDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 430 PFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQwqd 509
Cdd:PRK05858 393 DPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKH--- 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 510 kFFNQRFSHSVF-NGQPD--FMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTEA 572
Cdd:PRK05858 470 -PMEALYGYDVAaDLRPGtrYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSVA 534
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
26-569 |
1.50e-67 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 229.65 E-value: 1.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 26 LNEKTLNDMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDgkIKHILARHEQGAVHAAEGYARVSGKTGVVVVTS 105
Cdd:PRK06112 5 LSAPGFTLNGTVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIG--IRQIAYRTENAGGAMADGYARVSGKVAVVTAQN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 106 GPGATNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKqnyQVKRVEDIPKI---VHEAFHVANSG 182
Cdd:PRK06112 83 GPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTK---WVRRVTVAERIddyVDQAFTAATSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 183 RKGPVVIDFPKD-MGVLATNVDLCDEINIPGYEV-VTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNK 260
Cdd:PRK06112 160 RPGPVVLLLPADlLTAAAAAPAAPRSNSLGHFPLdRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 261 HQIPTVTTLLGLGAVPYEDTLFLGMGGM------HGSYASNMaLTECDLLINLGSRFDDRLASKPDAFAPNAKIVHVDID 334
Cdd:PRK06112 240 AGLPVATTNMGKGAVDETHPLSLGVVGSlmgprsPGRHLRDL-VREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 335 PSEINKVIHVdLGIIADCKRFLECLND---------------KNVETIEHSdWVKHcqnNKQKHPFKLGEEDQVfcKPQQ 399
Cdd:PRK06112 319 GEEVGRNYEA-LRLVGDARLTLAALTDalrgrdlaaragrraALEPAIAAG-REAH---REDSAPVALSDASPI--RPER 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 400 TIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQ-WVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTN 478
Cdd:PRK06112 392 IMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVW 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 479 QEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQrFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQ 558
Cdd:PRK06112 472 AELETARRMGVPVTIVVLNNGILGFQKHAETVKFGT-HTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAP 550
|
570
....*....|.
gi 445969956 559 GPVLIEVRISP 569
Cdd:PRK06112 551 GPTLIEVITDP 561
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
417-565 |
1.11e-66 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 213.60 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 417 DVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLI 496
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445969956 497 NNGTLGMVKQWQDKFFNQRFSHSVFNGQ--PDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
39-565 |
6.86e-65 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 221.79 E-value: 6.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 39 EVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGIT 117
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGALV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 118 DAHCDSLPLVVFTGQVATPGIGKDA--FQEA-DILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:PRK07064 87 EALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 195 mgVLATNVDLCDEINiPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNqlLTQFVnKHQIPTVTTLLGLGA 274
Cdd:PRK07064 167 --IQAAEIELPDDLA-PVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLV-DLGFGVVTSTQGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 275 VPYEDTLFLgmGGMHGSYASNMALTECDLLINLGSRFDDRLASKPDAFAPnAKIVHVDIDPSEINKVIHVDLGIIADCKR 354
Cdd:PRK07064 241 VPEDHPASL--GAFNNSAAVEALYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPNDLFVHGDAAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 355 FLECLNDKnVETIEHSD--WVKHCQNNKQKHPFKLGEEDQVFCKPQQTIEyigKITNGEAIVTTDVG-QHQMWAAQFYPF 431
Cdd:PRK07064 318 VLARLADR-LEGRLSVDpaFAADLRAAREAAVADLRKGLGPYAKLVDALR---AALPRDGNWVRDVTiSNSTWGNRLLPI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 432 --KNHGQWVTSGGLGTmgfGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQD 509
Cdd:PRK07064 394 fePRANVHALGGGIGQ---GLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQD 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 510 KFFNQRfSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:PRK07064 471 AQYGGR-RYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
35-565 |
1.71e-63 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 218.53 E-value: 1.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 35 RSGSEVLVEALLKENVDYLFGYPggaVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARV-SGKT-GVVVVTSGPGATNV 112
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARAtSGERvGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 113 MTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEAdiLSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFP 192
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTGYPRGSTDVAPNFES--LRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 193 KDMgvLATNVDLCDEINIPGYEVVTEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGL 272
Cdd:PRK06154 175 VDV--LAEELDELPLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 273 GAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRLASKPdafAPNAK-IVHVDIDPSEINKVIHVDLGIIAD 351
Cdd:PRK06154 253 SAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLP---MPEGKtIIHSTLDDADLNKDYPIDHGLVGD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 352 CKRFLECL--------------NDKNVETIE--HSDWVkhcqnnKQKHPfKLGEED------QVFCKPQQTIEyigkitN 409
Cdd:PRK06154 330 AALVLKQMieelrrrvgpdrgrAQQVAAEIEavRAAWL------AKWMP-KLTSDStpinpyRVVWELQHAVD------I 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 410 GEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGL 489
Cdd:PRK06154 397 KTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 490 DVKIVLINNGTLGMvkqwQDKFF---NQRFSHSVFNGqpDFMKMAEAYGVKGFLIDKPEQL----EEQLDAAFAYQgPVL 562
Cdd:PRK06154 477 PILTILLNNFSMGG----YDKVMpvsTTKYRATDISG--DYAAIARALGGYGERVEDPEMLvpalLRALRKVKEGT-PAL 549
|
...
gi 445969956 563 IEV 565
Cdd:PRK06154 550 LEV 552
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
34-569 |
1.42e-61 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 213.70 E-value: 1.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTF-YDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNV 112
Cdd:PRK06546 2 AKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 113 MTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEadilsmTSPitKQNYQ--------VKRVEDIPKIVHEAFHVAnSGRK 184
Cdd:PRK06546 82 INGLYDAHRSGAPVLAIASHIPSAQIGSGFFQE------THP--DRLFVecsgycemVSSAEQAPRVLHSAIQHA-VAGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 185 GPVVIDFPKDMGVLATNVDLCDEINIPGYEVVTePENKDIDTFISLLKEAKKPVVLAGAGINQSKSNqlLTQFVNKHQIP 264
Cdd:PRK06546 153 GVSVVTLPGDIADEPAPEGFAPSVISPRRPTVV-PDPAEVRALADAINEAKKVTLFAGAGVRGAHAE--VLALAEKIKAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 265 TVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFddrlaskP-DAFAPNAKIVHVDIDPSEINKVIH 343
Cdd:PRK06546 230 VGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF-------PyDQFLPDVRTAQVDIDPEHLGRRTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 344 VDLGIIADCK----------------RFLECLNDKNVETIEH--SDWVKHCQNNKQKHPfklgeedqvfckpqqtiEYIG 405
Cdd:PRK06546 303 VDLAVHGDVAetirallplvkektdrRFLDRMLKKHARKLEKvvGAYTRKVEKHTPIHP-----------------EYVA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 406 KITNGEA----IVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEM 481
Cdd:PRK06546 366 SILDELAaddaVFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGEL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 482 ALLPEYGLDVKIVLINNGTLGMVKqwQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPV 561
Cdd:PRK06546 446 LTVKLYDLPVKVVVFNNSTLGMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPA 523
|
....*...
gi 445969956 562 LIEVRISP 569
Cdd:PRK06546 524 LVDVVTDP 531
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
37-195 |
7.23e-61 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 199.38 E-value: 7.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 37 GSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTG 115
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 116 ITDAHCDSLPLVVFTGQVATPGIGKDAFQ-EADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDFPKD 194
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
.
gi 445969956 195 M 195
Cdd:pfam02776 161 V 161
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
401-567 |
1.75e-58 |
|
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: 192.86 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 401 IEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQE 480
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 481 MALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNGqPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGP 560
Cdd:cd00568 83 LATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN-PDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 445969956 561 VLIEVRI 567
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
34-575 |
1.67e-56 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 199.83 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFY-DGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNV 112
Cdd:PRK09124 2 KQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 113 MTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEadilsmTSPitkQNY---------QVKRVEDIPKIVHEAFHVAnSGR 183
Cdd:PRK09124 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQE------THP---QELfrecshyceLVSNPEQLPRVLAIAMRKA-ILN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 184 KGPVVIDFPKDMGVLATNVDLCDEINIPGYEVVTEPENkDIDTFISLLKEAKKPVVLAGAGInqSKSNQLLTQFVNKHQI 263
Cdd:PRK09124 152 RGVAVVVLPGDVALKPAPERATPHWYHAPQPVVTPAEE-ELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 264 PTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDDRlaskpdAFAP-NAKIVHVDIDPSEINKVI 342
Cdd:PRK09124 229 PIVHALRGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR------QFYPtDAKIIQIDINPGSLGRRS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 343 HVDLGIIADCKRFLECLNDKnvetIEHSDWVKHCQNNkQKHPFK---------LGEEDQVFCKPQQTIEYIGKITNGEAI 413
Cdd:PRK09124 303 PVDLGLVGDVKATLAALLPL----LEEKTDRKFLDKA-LEHYRKarkglddlaVPSDGGKPIHPQYLARQISEFAADDAI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 414 VTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKI 493
Cdd:PRK09124 378 FTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 494 VLINNGTLGMVKqwqdkfFNQRFSHSVFNG----QPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISP 569
Cdd:PRK09124 458 VVFNNSVLGFVA------MEMKAGGYLTDGtdlhNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAK 531
|
....*.
gi 445969956 570 TEAVTP 575
Cdd:PRK09124 532 QELAMP 537
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
33-570 |
4.31e-54 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 193.29 E-value: 4.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 33 DMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKH------ILARHEQGAVHAAEGYARVSGKTGVVVVTSG 106
Cdd:PRK08327 5 TMYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 107 PGATNVMTGITDAHCDSLPLVVFTGqvATPGIGKDAF----------QEA-DILSMTSPITKQNYQVKRVEDIPKIVHEA 175
Cdd:PRK08327 85 VGTANALGGVHNAARSRIPVLVFAG--RSPYTEEGELgsrntrihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 176 FHVANSGRKGPVVIDFPKDmgVLATNVD---LCDEINIPGYEVVTEPEnkDIDTFISLLKEAKKPVVLAGAGINQSKSNQ 252
Cdd:PRK08327 163 IQIAMSEPKGPVYLTLPRE--VLAEEVPevkADAGRQMAPAPPAPDPE--DIARAAEMLAAAERPVIITWRAGRTAEGFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 253 LLTQFVNKHQIPTVTTLLGLGAVPYEDTLFLGmggmhgsYASNMALTECDLLINLGSR---FDDRLASKPDAfapnaKIV 329
Cdd:PRK08327 239 SLRRLAEELAIPVVEYAGEVVNYPSDHPLHLG-------PDPRADLAEADLVLVVDSDvpwIPKKIRPDADA-----RVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 330 HVDIDPSEiNKV----IHVDLGIIADCKRFLECLND------KNVETIEHSDWVKHCQNNKQKHPFKLGEEDQVFCKPQQ 399
Cdd:PRK08327 307 QIDVDPLK-SRIplwgFPCDLCIQADTSTALDQLEErlkslaSAERRRARRRRAAVRELRIRQEAAKRAEIERLKDRGPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 400 TIEY----IGKITNGEAIVTTDVG--QHQMWAAQFypfknhGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGG 473
Cdd:PRK08327 386 TPAYlsycLGEVADEYDAIVTEYPfvPRQARLNKP------GSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 474 FQMTNQEMAL--LPEYGLDVKIVLINNGTLGMVKQWQDKFF-------NQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKP 544
Cdd:PRK08327 460 FIFGVPEAAHwvAERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaarKGTFPGTDFDPRPDFAKIAEAFGGYGERVEDP 539
|
570 580 590
....*....|....*....|....*....|
gi 445969956 545 EQLEEQLDAAFAY----QGPVLIEVRISPT 570
Cdd:PRK08327 540 EELKGALRRALAAvrkgRRSAVLDVIVDRV 569
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
224-359 |
5.31e-54 |
|
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: 180.07 E-value: 5.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 224 IDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDL 303
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 304 LINLGSRFDD-RLASKPDAFAPNAKIVHVDIDPSEINKVIHVDLGIIADCKRFLECL 359
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
34-578 |
1.18e-53 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 192.43 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTF--YDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATN 111
Cdd:PRK08273 2 SQTVADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 112 VMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRV-EDIPKIVHEAFHVAnSGRKGPVVID 190
Cdd:PRK08273 82 LLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGAFVQMVTVpEQLRHLVDRAVRTA-LAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 191 FPKDMGVLatnvdlcdEINIPGYE---VVTE---------PENKDIDTFISLLKEAKKPVVLAGAGINQSKSNqlLTQFV 258
Cdd:PRK08273 161 LPNDVQEL--------EYEPPPHAhgtVHSGvgytrprvvPYDEDLRRAAEVLNAGRKVAILVGAGALGATDE--VIAVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 259 NKHQIPTVTTLLGLGAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFddrlaskPDA-FAP---NAKIVHVDID 334
Cdd:PRK08273 231 ERLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF-------PYSeFLPkegQARGVQIDID 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 335 PSEINKVIHVDLGIIADCK----RFLECLNDKN----VETIEHS--DWVKHCQnnKQKHPfklgEEDQVfcKPQQTIEYI 404
Cdd:PRK08273 304 GRMLGLRYPMEVNLVGDAAetlrALLPLLERKKdrswRERIEKWvaRWWETLE--ARAMV----PADPV--NPQRVFWEL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 405 GKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQ-EMAL 483
Cdd:PRK08273 376 SPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMaELIT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 484 LPEYGLDVK----IVLI-NNGTLGMVkQWQdkffnQRfshsVFNGQP-----------DFMKMAEAYGVKGFLIDKPEQL 547
Cdd:PRK08273 456 VAKYWRQWSdprlIVLVlNNRDLNQV-TWE-----QR----VMEGDPkfeasqdlpdvPYARFAELLGLKGIRVDDPEQL 525
|
570 580 590
....*....|....*....|....*....|.
gi 445969956 548 EEQLDAAFAYQGPVLIEVRISPteAVTPMVP 578
Cdd:PRK08273 526 GAAWDEALAADRPVVLEVKTDP--NVPPLPP 554
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
396-572 |
3.50e-53 |
|
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: 179.26 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 396 KPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQ 475
Cdd:cd02014 3 HPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 476 MTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNgqPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAF 555
Cdd:cd02014 83 MLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPN--PDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|....*..
gi 445969956 556 AYQGPVLIEVRISPTEA 572
Cdd:cd02014 161 AADGPVVIDVVTDPNEP 177
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
41-572 |
1.30e-48 |
|
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: 177.66 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 41 LVEALLKENVDYLFGYPGGAVLPLYDTFYDGK-IKHILARHEQGAVHAAEGYARVSGkTGVVVVTSGPGATNVMTGITDA 119
Cdd:COG3961 11 LLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPgIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 120 HCDSLPLVVFTGqvaTPGigKDAFQEADILS-------------MTSPITK-------QNYqvkrVEDIPKIVHEAFHva 179
Cdd:COG3961 90 YAERVPVVHIVG---APG--TRAQRRGPLLHhtlgdgdfdhflrMFEEVTVaqavltpENA----AAEIDRVLAAALR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 180 nsgRKGPVVIDFPKDMGVLatnvdlcdEINIPGYEVVTEPENKD-------IDTFISLLKEAKKPVVLAGAGINQSKSNQ 252
Cdd:COG3961 159 ---EKRPVYIELPRDVADA--------PIEPPEAPLPLPPPASDpaalaaaVAAAAERLAKAKRPVILAGVEVHRFGLQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 253 LLTQFVNKHQIPTVTTLLGLGAVPYEDTLFLGM--GGMHGSYASNmALTECDLLINLGSRF-DDRLASKPDAFAPnAKIV 329
Cdd:COG3961 228 ELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyaGAASSPEVRE-YVENADCVLCLGVVFtDTNTGGFTAQLDP-ERTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 330 HVDIDPSEINKVI--HVDLgiiadcKRFLECLNDKnvetiehsdwvkhCQNNKQKHPFKLGEEDQVFCKPQQTIEY---- 403
Cdd:COG3961 306 DIQPDSVRVGGHIypGVSL------ADFLEALAEL-------------LKKRSAPLPAPAPPPPPPPAAPDAPLTQdrlw 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 404 --IGKITNGEAIVTTDVGQhQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEM 481
Cdd:COG3961 367 qrLQAFLDPGDIVVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQEL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 482 ALLPEYGLDVKIVLINNG--T-----LGM------VKQWqdkffnqrfshsvfngqpDFMKMAEAYG---VKGFLIDKPE 545
Cdd:COG3961 446 STMLRYGLKPIIFVLNNDgyTieraiHGPdgpyndIANW------------------DYAKLPEAFGggnALGFRVTTEG 507
|
570 580
....*....|....*....|....*...
gi 445969956 546 QLEEQLDAAFAYQ-GPVLIEVRISPTEA 572
Cdd:COG3961 508 ELEEALAAAEANTdRLTLIEVVLDKMDA 535
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
69-582 |
3.20e-46 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 172.23 E-value: 3.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 69 YDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTS--GPGATNVMTGITDAHCDSLPLVVFTGQV-AT---------- 135
Cdd:COG3962 54 DPDELPTYQGRNEQGMAHAAIAYAKQKNRRRIMACTSsiGPGATNMVTAAALATANRLPVLLLPGDTfATrqpdpvlqql 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 136 -----PGIG-KDAFQeadilsmtsPITKqnY--QVKRVEDIPKIVHEAFHV----ANSgrkGPVVIDFPKDmgVLATNVD 203
Cdd:COG3962 134 ehfhdPTISvNDAFR---------PVSR--YwdRITRPEQLMSALPRAMRVltdpAET---GAVTLALPQD--VQAEAYD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 204 lcdeinipgYEVV-----------TEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTVTTLLGL 272
Cdd:COG3962 198 ---------YPESffakrvhrirrPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 273 GAVPYEDTLFLGMGGMHGSYASNMALTECDLLINLGSRFDD-RLASKpDAFA-PNAKIVHVDIDPSEINKviHVDLGIIA 350
Cdd:COG3962 269 GALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLQDfTTGSK-TLFAnPDVRFVNINVARFDAYK--HDALPVVA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 351 DCKRFLECLNDKNVETIEHSDWVKHCQNNKQKHpfkLGEEDQVFckpqqTIEYIGKITNGEAIVT-------TDV----- 418
Cdd:COG3962 346 DAREGLEALTEALAGWRYPAAWTDEAAELKAEW---DAEVDRLY-----APTNGGLPTQAQVIGAvneaagpDDIvvcaa 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 419 ----GQ-HQMWAAqfypfKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKI 493
Cdd:COG3962 418 gslpGDlHKLWRT-----RDPGTYHVEYGYSCMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIV 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 494 VLINNGTLGMVKQWQDKFFNQRF---------SHSVFNGQP---DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPV 561
Cdd:COG3962 493 VLLDNHGFGCINRLQMSTGSQSFgtelrdrdtETGRLDGGLlpvDFAANAASLGAKAYRVTTIAELRAALERAKAADRTT 572
|
570 580
....*....|....*....|.
gi 445969956 562 LIEVRISPteavTPMVPSGKS 582
Cdd:COG3962 573 VIVIKTDP----KTMTPGGGS 589
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
34-570 |
2.36e-44 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 165.93 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 34 MRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVM 113
Cdd:PRK09259 9 LTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 114 TGITDAHCDSLPLVVFTG--QVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDF 191
Cdd:PRK09259 89 TALANATTNCFPMIMISGssEREIVDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 192 PKDmgVLATNVDlCDEINIPGYEVV-----TEPENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNKHQIPTV 266
Cdd:PRK09259 169 PAK--VLAQTMD-ADEALTSLVKVVdpapaQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 267 TTLLGLGAVPyeDTLFLGMGGmhgsyASNMALTECDLLINLGSRFDDRLA-SKPDAFAPNAKIVHVDIDPSEINKVIHVD 345
Cdd:PRK09259 246 PMSMAKGLLP--DTHPQSAAA-----ARSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIEPQEIDSNRPIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 346 LGIIADCKRFLECLND--KNVETIEHSDWV-----KHCQN--------NKQKHPFK----LGEEDQVFCKPQQTIeyigk 406
Cdd:PRK09259 319 APVVGDIGSVMQALLAglKQNTFKAPAEWLdalaeRKEKNaakmaeklSTDTQPMNfynaLGAIRDVLKENPDIY----- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 407 ITNgEAIVTTDVGqhQMWAAQFYPFKNhgqwVTSGGLGTMGFGIPSSIGAKLANpDKTVVCFVGDGGFQMTNQEMALLPE 486
Cdd:PRK09259 394 LVN-EGANTLDLA--RNIIDMYKPRHR----LDCGTWGVMGIGMGYAIAAAVET-GKPVVAIEGDSAFGFSGMEVETICR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 487 YGLDVKIVLINNGtlGMVK-QWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEV 565
Cdd:PRK09259 466 YNLPVTVVIFNNG--GIYRgDDVNLSGAGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINV 543
|
....*
gi 445969956 566 RISPT 570
Cdd:PRK09259 544 VIDPA 548
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
27-567 |
5.08e-42 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 158.97 E-value: 5.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 27 NEKTLNDMRSGSEVLVEALLKENVDYLFGYPGGAVLPLYDTFYDGkIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSG 106
Cdd:PRK07092 4 ATAPAAAMTTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 107 PGATNVMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEA-DILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKG 185
Cdd:PRK07092 83 AGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFLAAvQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 186 PVVIDFPKDmgvlatnvDL---CDeiNIPGYEVVTE--PENKDIDTFISLLKEAKKPVVLAGAGINQSKSNQLLTQFVNK 260
Cdd:PRK07092 163 PVFVSIPYD--------DWdqpAE--PLPARTVSSAvrPDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 261 HQIPT-VTTLLGLGAVPYEDTLFLGMggMHGSYAS-NMALTECDLLINLGS---RFDDRLASkpDAFAPNAKIVHVDIDP 335
Cdd:PRK07092 233 HRAPVwVAPMSGRCSFPEDHPLFAGF--LPASREKiSALLDGHDLVLVIGApvfTYHVEGPG--PHLPEGAELVQLTDDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 336 SEInKVIHVDLGIIADCKRFLECLNDKNVETIehsdwvkhCQNNKQKHPFKLGEEDQVFCKPQQTIEYIGKITNGEAIVT 415
Cdd:PRK07092 309 GEA-AWAPMGDAIVGDIRLALRDLLALLPPSA--------RPAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 416 TDVGQHQ--MWaaQFYPFKNHGQWVT--SGGLgtmGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDV 491
Cdd:PRK07092 380 EEAPSTRpaMQ--EHLPMRRQGSFYTmaSGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 492 KIVLINNGTLGMVkQWqdkffnqrFSHsVFNGQP---------DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVL 562
Cdd:PRK07092 455 TFVILNNGRYGAL-RW--------FAP-VFGVRDvpgldlpglDFVALARGYGCEAVRVSDAAELADALARALAADGPVL 524
|
....*
gi 445969956 563 IEVRI 567
Cdd:PRK07092 525 VEVEV 529
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
397-571 |
1.58e-41 |
|
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: 147.82 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 397 PQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQM 476
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 477 TNQEMALLPEYGLDVKIVLINNGTLGMVKqWQDKFFNQRFSHSVFnGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFA 556
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDF-GNPDFVKYAESFGAKGYRIESADDLLPVLERALA 158
|
170
....*....|....*
gi 445969956 557 YQGPVLIEVRISPTE 571
Cdd:cd02010 159 ADGVHVIDCPVDYSE 173
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
38-194 |
8.55e-39 |
|
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: 139.99 E-value: 8.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 38 SEVLVEALLKENVDYLFGYPGGAVLPLYDTFY-DGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGI 116
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445969956 117 TDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSgRKGPVVIDFPKD 194
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIA-KRGVAVLILPGD 159
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
40-193 |
1.99e-37 |
|
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: 135.94 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 40 VLVEALLKENVDYLFGYPGGAVLPLYDTFYDG-KIKHILARHEQGAVHAAEGYARVSGKtGVVVVTSGPGATNVMTGITD 118
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445969956 119 AHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRkGPVVIDFPK 193
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQ-GPVVVRLPR 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
427-567 |
4.28e-34 |
|
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: 127.71 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 427 QFYPFKNHGQWVTSGGlGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQ 506
Cdd:cd02002 33 DQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRS 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 507 WQDKFFNQRFSHSVFNGQ------PDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRI 567
Cdd:cd02002 112 FLKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPEELDEALREALAEGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
411-568 |
3.63e-30 |
|
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: 116.48 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 411 EAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLD 490
Cdd:cd02004 15 DAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGMELETAVRYNLP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445969956 491 VKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNGQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRIS 568
Cdd:cd02004 95 IVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
397-570 |
1.21e-28 |
|
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: 112.99 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 397 PQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQM 476
Cdd:cd02013 6 PRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 477 TNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKFFNQRFSHSVFNgQPDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFA 556
Cdd:cd02013 86 SMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELE-SESFAKIAEACGAKGITVDKPEDVGPALQKAIA 164
|
170
....*....|....*..
gi 445969956 557 YQG---PVLIEVRISPT 570
Cdd:cd02013 165 MMAegkTTVIEIVCDQE 181
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
391-565 |
5.63e-22 |
|
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: 94.27 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 391 DQVFCKPQQTIEYIGKITNGEAIVTTDVGQHQMWAAQFYPFKNHGQWVTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVG 470
Cdd:cd02006 4 DDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 471 DGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKF---------FNQRFSHSVFNGQPDFMKMAEAYGVKGFLI 541
Cdd:cd02006 84 DYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFdmdyqvnlaFENINSSELGGYGVDHVKVAEGLGCKAIRV 163
|
170 180
....*....|....*....|....*...
gi 445969956 542 DKPEQLEEQLDAAFA----YQGPVLIEV 565
Cdd:cd02006 164 TKPEELAAAFEQAKKlmaeHRVPVVVEA 191
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
36-567 |
6.11e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 96.48 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 36 SGSEVLVEALLKENVDYLFGYPGGA----VLPLyDTfyDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATN 111
Cdd:PRK12474 6 NGADSVVDTLLNCGVEVCFANPGTSemhfVAAL-DR--VPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 112 VMTGITDAHCDSLPLVVFTGQVATPGIGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKGPVVIDF 191
Cdd:PRK12474 83 GLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 192 PKDMgvlATNVDLCDEINIPGYEvvTEPENKDIDTFISLLKEAKKPVVL-------------AGAGINQSKSNQLLTQFV 258
Cdd:PRK12474 163 PADV---AWNEAAYAAQPLRGIG--PAPVAAETVERIAALLRNGKKSALllrgsalrgapleAAGRIQAKTGVRLYCDTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 259 NKHqiptvtTLLGLGAVPYED-TLFLGMGGMHgsyasnmaLTECDLLINLGSR-----FddRLASKPDAFAP-NAKIVHV 331
Cdd:PRK12474 238 APR------IERGAGRVPIERiPYFHEQITAF--------LKDVEQLVLVGAKppvsfF--AYPGKPSWGAPpGCEIVYL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 332 dIDPSEinkvihvdlgiiaDCKRFLECLNDKnvetiehsdwVKHCQNNKQKHPFKLGEEDQVFCKPQQTIEYIGKITNGE 411
Cdd:PRK12474 302 -AQPDE-------------DLAQALQDLADA----------VDAPAEPAARTPLALPALPKGALNSLGVAQLIAHRTPDQ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 412 AIV----TTDVGQHQMWAAQFYPfknHGQWVTSGGlgTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEY 487
Cdd:PRK12474 358 AIYadeaLTSGLFFDMSYDRARP---HTHLPLTGG--SIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 488 GLDVKIVLINNGTLGMVKQWQDKFFNQ---RFSHSVFN-GQP--DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPV 561
Cdd:PRK12474 433 NLDVTVVIFANRSYAILNGELQRVGAQgagRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPR 512
|
....*.
gi 445969956 562 LIEVRI 567
Cdd:PRK12474 513 LIEAMI 518
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
421-582 |
2.78e-20 |
|
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: 89.29 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 421 HQMWAAQfYPFKNHGQWvtsgGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGT 500
Cdd:cd02003 30 HKLWRAR-TPGGYHLEY----GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 501 LGMVKQWQDKFFNQRF---------SHSVFNGQP---DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRIS 568
Cdd:cd02003 105 FGCINNLQESTGSGSFgtefrdrdqESGQLDGALlpvDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
170
....*....|....
gi 445969956 569 PTEavtpMVPSGKS 582
Cdd:cd02003 185 PKS----MTPGYGS 194
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
444-569 |
2.51e-19 |
|
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: 86.05 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 444 GTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQDKffnqrfsHSVFNG 523
Cdd:cd02005 50 GSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGP-------EASYND 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 445969956 524 -QP-DFMKMAEAYG----VKGFLIDKPEQLEEQL-DAAFAYQGPVLIEVRISP 569
Cdd:cd02005 123 iANwNYTKLPEVFGggggGLSFRVKTEGELDEALkDALFNRDKLSLIEVILPK 175
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
437-567 |
2.64e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 78.73 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 437 WVTSGGlGTMGFGIPSSIGAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNGTLGMVKQWQdkffnQRF 516
Cdd:PRK07586 379 WLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGEL-----ARV 452
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969956 517 SHsvfnGQP---------------DFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRI 567
Cdd:PRK07586 453 GA----GNPgpraldmldlddpdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
39-137 |
8.43e-15 |
|
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: 72.14 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 39 EVLVEALLKENVDYLFGYPGGAVLPLYDTFYD-GKIKHILARHEQGAVHAAEGYARVSGkTGVVVVTSGPGATNVMTGIT 117
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90 100
....*....|....*....|
gi 445969956 118 DAHCDSLPLVVFTGqvaTPG 137
Cdd:cd07038 80 GAYAEHVPVVHIVG---APS 96
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
450-568 |
1.29e-09 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 57.61 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 450 IPSSIGAKLANpDKTVVCFVGD-------GGFqmtnqemALLPEYGLDVKIVLINNGTLG----MVKQWQDKFFNQRFS- 517
Cdd:cd02009 57 LSTALGIALAT-DKPTVLLTGDlsflhdlNGL-------LLGKQEPLNLTIVVINNNGGGifslLPQASFEDEFERLFGt 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 445969956 518 -HSVfngqpDFMKMAEAYGVKGFLIDKPEQLEEQLDAAFAYQGPVLIEVRIS 568
Cdd:cd02009 129 pQGL-----DFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
444-571 |
2.37e-09 |
|
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: 56.94 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 444 GTMGFGipSSI--GAKLANPDKTVVCFVGDGGFQMTNQEMALLPEYGLD-VKIVLINNGTlgmvkqwqdkffnqrfsHSV 520
Cdd:cd03371 48 GSMGHA--SQIalGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGA-----------------HDS 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 445969956 521 FNGQP------DFMKMAEAYGV-KGFLIDKPEQLEEQLDAAFAYQGPVLIEVRISPTE 571
Cdd:cd03371 109 VGGQPtvsfdvSLPAIAKACGYrAVYEVPSLEELVAALAKALAADGPAFIEVKVRPGS 166
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
400-589 |
8.45e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 55.99 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 400 TIEYIGKITNGEAIVTtDVG--QHQMWAA-----QFYPfknhgqwvtsggLGTMGFGIPSSIGAKLANPDKTVVCFVGDG 472
Cdd:PRK06163 19 TCRLVAKLKDEEAVIG-GIGntNFDLWAAgqrpqNFYM------------LGSMGLAFPIALGVALAQPKRRVIALEGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 473 gfqmtnqemALLPEYGLDVKIVLINNGTLGMVkQWQDKFFNqrfshsVFNGQP-------DFMKMAEAYGV-KGFLIDKP 544
Cdd:PRK06163 86 ---------SLLMQLGALGTIAALAPKNLTII-VMDNGVYQ------ITGGQPtltsqtvDVVAIARGAGLeNSHWAADE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445969956 545 EQLEEQLDAAFAYQGPVLIEVRI--SPTEAVTPMVPSGKSNHEMEGL 589
Cdd:PRK06163 150 AHFEALVDQALSGPGPSFIAVRIddKPGVGTTERDPAQIRERFMQGL 196
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
41-499 |
1.05e-08 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 58.17 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 41 LVEAllkeNVDYLFGYPGGAVLPLYDTF-YDGKIKHILARHEQGAVHAAEGYARVSGkTGVVVVTSGPGATNVMTGITDA 119
Cdd:PLN02573 26 LVEI----GVTDVFSVPGDFNLTLLDHLiAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 120 HCDSLPLVVFTG----------QVATPGIGKDAF-QEadiLSMTSPITKQNYQVKRVEDIPKIVHEAFHVANSGRKgPVV 188
Cdd:PLN02573 101 YSENLPVICIVGgpnsndygtnRILHHTIGLPDFsQE---LRCFQTVTCYQAVINNLEDAHELIDTAISTALKESK-PVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 189 IDFPkdmgvlatnvdlCDEINIPGYEVVTEP---------ENKD-----IDTFISLLKEAKKPVVLAGAGINQSKSNQLL 254
Cdd:PLN02573 177 ISVS------------CNLAAIPHPTFSREPvpffltprlSNKMsleaaVEAAAEFLNKAVKPVLVGGPKLRVAKACKAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 255 TQFVNKHQIPTVTTLLGLGAVPYEDTLFLGM--GGMHGSYASNMaLTECDLLINLGSRFDD------RLASKPDafapNA 326
Cdd:PLN02573 245 VELADASGYPVAVMPSAKGLVPEHHPHFIGTywGAVSTPFCAEI-VESADAYLFAGPIFNDyssvgySLLLKKE----KA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 327 KIVHVDidpseinKVIhVDLGIIADC---KRFLECLNDKnvetiehsdwVKHcqNNKQKHPFK---LGEEDQVFCKPQQT 400
Cdd:PLN02573 320 IIVQPD-------RVT-IGNGPAFGCvlmKDFLEALAKR----------VKK--NTTAYENYKrifVPEGEPLKSEPGEP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 401 I------EYIGKITNGEAIVTTDVGQHqmWaaqF------------YPFKnhgqwvtsgglgtMGFG-IPSSIGAKL--- 458
Cdd:PLN02573 380 LrvnvlfKHIQKMLSGDTAVIAETGDS--W---FncqklklpegcgYEFQ-------------MQYGsIGWSVGATLgya 441
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 445969956 459 -ANPDKTVVCFVGDGGFQMTNQEMALLPEYGLDVKIVLINNG 499
Cdd:PLN02573 442 qAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNG 483
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
455-569 |
6.53e-08 |
|
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: 53.99 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 455 GAKLANPDKTVVCFVGDG-----GFQMTNQEMallpEYGLDVKIVLINNGTLGMVK-------------------QWQDK 510
Cdd:COG1013 75 GIKLANPDLTVIVFGGDGdtydiGGNHLIHAA----RRNEDITYIVYDNEIYGNTGgqrspttplgakttttpygKPEPP 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445969956 511 FfnqrfshsvfngqpDFMKMAEAYGVkGFL----IDKPEQLEEQLDAAFAYQGPVLIEVrISP 569
Cdd:COG1013 151 K--------------DPAEIAAAHGA-TYVarasVGDPKDLKKKIKKAIEHKGFSFIEV-LSP 197
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
40-192 |
1.04e-07 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 51.73 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 40 VLVEALLKENVDYLFGYPGGAVLPL-YDTFYDGKIKHILARHEQGAVHAAEGYARVSGKTGVVVVTSGPGATNVMTGITD 118
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGSRSAPLaLAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 119 AHCDSLPLVVFTGQvaTPG--IGKDAFQEADILSMTSPITKQNYQVKRVEDIPKIVH------EAFHVANSGRKGPVVID 190
Cdd:cd07037 82 AYYSGVPLLVLTAD--RPPelRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYllrlanRAVLEALSAPPGPVHLN 159
|
..
gi 445969956 191 FP 192
Cdd:cd07037 160 LP 161
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
444-569 |
9.17e-07 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 49.45 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 444 GTMGFGIPSSIGAKLANPDKTVVCFVGDG-----GfqmTNQEMALLPEyGLDVKIVLINNGTLGMVKqwqdkffNQ---- 514
Cdd:cd03375 51 TLHGRALAVATGVKLANPDLTVIVVSGDGdlaaiG---GNHFIHAARR-NIDITVIVHNNQIYGLTK-------GQaspt 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 515 -----RFSHSVF-NGQPDF--MKMAEAYGV----KGFLIDkPEQLEEQLDAAFAYQGPVLIEVrISP 569
Cdd:cd03375 120 tpegfKTKTTPYgNIEEPFnpLALALAAGAtfvaRGFSGD-IKQLKEIIKKAIQHKGFSFVEV-LSP 184
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
406-563 |
1.02e-06 |
|
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: 49.20 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 406 KITNGEAIVTTDVGQHQMWAAQfyPFKnhgqwvTSGGLGTMGFGIPSSIGAKLANPDKTVVCFVGDGGF---QMTnqemA 482
Cdd:cd02008 21 KAFKKDSIVSGDIGCYTLGALP--PLN------AIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFfhsGIL----G 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 483 LLPEY--GLDVKIVLINNGTLGMVKQwQDKFFNQRFSHSVFNgQPDFMKMAEAYGVKGFLIDKPEQLE---EQLDAAFAY 557
Cdd:cd02008 89 LINAVynKANITVVILDNRTTAMTGG-QPHPGTGKTLTEPTT-VIDIEALVRAIGVKRVVVVDPYDLKairEELKEALAV 166
|
....*..
gi 445969956 558 QGP-VLI 563
Cdd:cd02008 167 PGVsVII 173
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
444-569 |
8.74e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 47.95 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 444 GTMGFGIPSSIGAKLANPDKTVVCFVGDG-----GFqmtNQEMALLpEYGLDVKIVLINNGTLGMVK-QwqdkF-----F 512
Cdd:PRK05778 70 TLHGRAIAFATGAKLANPDLEVIVVGGDGdlasiGG---GHFIHAG-RRNIDITVIVENNGIYGLTKgQ----AspttpE 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445969956 513 NQRFSHSVF-NGQPDFMKMAEA------YGVKGFLIDkPEQLEEQLDAAFAYQGPVLIEVrISP 569
Cdd:PRK05778 142 GSKTKTAPYgNIEPPIDPCALAlaagatFVARSFAGD-VKQLVELIKKAISHKGFAFIDV-LSP 203
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
441-564 |
2.06e-04 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 43.70 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 441 GGLGTMGFGIPSSIGA-----------KLANPDKTVVCFVGDGG------FQMTNqeMALLpeYGLDVKIVLINNgtlgm 503
Cdd:CHL00149 125 GGFAFIGEGIPIALGAafqsiyrqqvlKEVQPLRVTACFFGDGTtnngqfFECLN--MAVL--WKLPIIFVVENN----- 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969956 504 vkQWQDKFFNQRFShsvfnGQPDFMKMAEAYGVKGFLIDKPEQL------EEQLDAAFAYQGPVLIE 564
Cdd:CHL00149 196 --QWAIGMAHHRST-----SIPEIHKKAEAFGLPGIEVDGMDVLavrevaKEAVERARQGDGPTLIE 255
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
443-589 |
1.05e-03 |
|
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: 40.35 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969956 443 LGTMGFGIPSSIGAKLANPDKtVVCFVGDGGFQMtnqEMALLPEYGL----DVKIVLINNGTLGMVKqwqdkffNQRfSH 518
Cdd:cd03372 41 LGSMGLASSIGLGLALAQPRK-VIVIDGDGSLLM---NLGALATIAAekpkNLIIVVLDNGAYGSTG-------NQP-TH 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445969956 519 SVFNgqPDFMKMAEAYGVKGFL-IDKPEQLEEQLdaAFAYQGPVLIEVRISPTEA---VTPMVPSGKSNHEMEGL 589
Cdd:cd03372 109 AGKK--TDLEAVAKACGLDNVAtVASEEAFEKAV--EQALDGPSFIHVKIKPGNTdvpNIPRDPVEIKNRFMEAL 179
|
|
| |
