|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02470 |
PLN02470 |
acetolactate synthase |
86-671 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 1257.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 86 STFVPRFAADEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVC 165
Cdd:PLN02470 1 ETFQSRFAPDEPRKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 166 VATSGPGATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASS 245
Cdd:PLN02470 81 IATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 246 GRPGPVLIDIPKDIQQQLVVPNWNTQMKLPGYLSRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELT 325
Cdd:PLN02470 161 GRPGPVLVDIPKDIQQQLAVPNWNQPMKLPGYLSRLPKPPEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 326 GIPVASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKN 405
Cdd:PLN02470 241 GIPVASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 406 KQPHLSICTDVKLALEAINRLIEDKQPKlKFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTG 485
Cdd:PLN02470 321 KQPHVSVCADVKLALQGLNKLLEERKAK-RPDFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 486 VGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLN 565
Cdd:PLN02470 400 VGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 566 NQHLGMVVQWEDRFYKANRAHTYLGNPRNESEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQ 645
Cdd:PLN02470 480 NQHLGMVVQWEDRFYKANRAHTYLGDPDAEAEIFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQ 559
|
570 580
....*....|....*....|....*.
gi 720058595 646 EHVLPMIPSGGAFKDVITEGDGRSTY 671
Cdd:PLN02470 560 EHVLPMIPGGGTFKDIITEGDGRTKY 585
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
96-661 |
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: 740.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 96 EPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATN 175
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 176 LVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDI 255
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 256 PKDIQQQLVVPNwNTQMKLPGYLSRLPksPEEAHLEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTL 333
Cdd:COG0028 161 PKDVQAAEAEEE-PAPPELRGYRPRPA--PDPEAIEEAAELLAAAKRPVILAGGGARRAgaAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAINRLIEDKQPklkfDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWA 493
Cdd:COG0028 318 GDAKAVLAALLEALEPRAD----DRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 494 AQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVV 573
Cdd:COG0028 394 ARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 574 QWEDRFYKANRAHTYLGNPRneseiFPnmlKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHvlpmiP 653
Cdd:COG0028 474 QWQELFYGGRYSGTDLPNPD-----FA---KLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN-----P 540
|
....*...
gi 720058595 654 SGGAFKDV 661
Cdd:COG0028 541 PGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
99-664 |
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: 729.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 99 KGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKD 258
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 259 IQQQLVVPNWNTQMKLPGYlsrlpKSPEEAHLEQI---LRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTL 333
Cdd:TIGR00118 162 VTTAEIEYPYPEKVNLPGY-----RPTVKGHPLQIkkaAELINLAKKPVILVGGGVIiaGASEELKELAERIQIPVTTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:TIGR00118 237 MGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEA-INRLIEDKQPklkfDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMW 492
Cdd:TIGR00118 317 GDARNVLEElLKKLFELKER----KESAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 493 AAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV 572
Cdd:TIGR00118 393 AAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 573 VQWEDRFYKANRAHTYLGNprneseiFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMI 652
Cdd:TIGR00118 473 RQWQELFYEERYSHTHMGS-------LPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMV 545
|
570
....*....|..
gi 720058595 653 PSGGAFKDVITE 664
Cdd:TIGR00118 546 APGGGLDEMIGE 557
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
98-664 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 693.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 98 RKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLV 177
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGV-EHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 178 SGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPK 257
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 258 DIQQqlvvpnwnTQMKLPGYLSRLPKSPE--EAHLEQILRFISESKKPVLYVGGGC--LNSSEELRRFVELTGIPVASTL 333
Cdd:PRK08978 160 DIQL--------AEGELEPHLTTVENEPAfpAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALREFLAATGMPAVATL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK08978 232 KGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAInrliedKQPklkFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWA 493
Cdd:PRK08978 312 GDLNALLPAL------QQP---LNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 494 AQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVV 573
Cdd:PRK08978 383 AQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 574 QWEDRFYKANRAHTYLGNprNeseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMIP 653
Cdd:PRK08978 463 QWQQLFFDERYSETDLSD--N-----PDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVP 535
|
570
....*....|.
gi 720058595 654 SGGAFKDVITE 664
Cdd:PRK08978 536 PGASNSEMLEK 546
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
82-655 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 690.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 82 PSSPSTFVPRFAADEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGL 161
Cdd:PRK07789 15 PPAAPAARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 162 PGVCVATSGPGATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFY 241
Cdd:PRK07789 95 VGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 242 LASSGRPGPVLIDIPKDIQQQLVVPNWNTQMKLPGYlsrlpKSPEEAHLEQI---LRFISESKKPVLYVGGGCL--NSSE 316
Cdd:PRK07789 175 IASTGRPGPVLVDIPKDALQAQTTFSWPPRMDLPGY-----RPVTKPHGKQIreaAKLIAAARRPVLYVGGGVIraEASA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 317 ELRRFVELTGIPVASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHID 396
Cdd:PRK07789 250 ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHAD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 397 IDPAEIGKNKQPHLSICTDVKlalEAINRLIE----DKQPKLKFDFSAWRKELHEQKLKFPLSFKTFAE-AIPPQYAIQV 471
Cdd:PRK07789 330 IDPAEIGKNRHADVPIVGDVK---EVIAELIAalraEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIER 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 472 LDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELAT 551
Cdd:PRK07789 407 LGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELAT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 552 VRVENLPIKILLLNNQHLGMVVQWEDRFYKANRAHTYLGnprNESEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLE 631
Cdd:PRK07789 487 CAIEGIPIKVALINNGNLGMVRQWQTLFYEERYSNTDLH---THSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARA 563
|
570 580
....*....|....*....|....*
gi 720058595 632 TPG-PYLLDVIVPHQEHVLPMIPSG 655
Cdd:PRK07789 564 INDrPVVIDFVVGKDAMVWPMVAAG 588
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
100-655 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 666.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSS---IIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEaegWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQQQLV--VPNWNTQMKLPGYlsRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNSS--EELRRFVELTGIPVAST 332
Cdd:PRK07418 181 KDVGQEEFdyVPVEPGSVKPPGY--RPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGahAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 333 LMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSI 412
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 413 CTDVKLALEAINRLIedKQPKLKFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQyaiQVLDELTD--GNAIISTGVGQHQ 490
Cdd:PRK07418 339 VGDVRKVLVKLLERS--LEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQ---EVLLAVRDlaPDAYYTTDVGQHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAAQWYKyKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLG 570
Cdd:PRK07418 414 MWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 571 MVVQWEDRFYKANRAHTylgnprNESEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLP 650
Cdd:PRK07418 493 MVRQWQESFYGERYSAS------NMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYP 566
|
....*
gi 720058595 651 MIPSG 655
Cdd:PRK07418 567 MVPPG 571
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
96-664 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 657.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 96 EPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATN 175
Cdd:PRK06048 6 EKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDL-RHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 176 LVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDI 255
Cdd:PRK06048 85 LVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 256 PKDIQQQLVVPNWNTQMKLPGYlsrlpKSPEEAHLEQILR---FISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVA 330
Cdd:PRK06048 165 PKDVTTAEIDFDYPDKVELRGY-----KPTYKGNPQQIKRaaeLIMKAERPIIYAGGGVIssNASEELVELAETIPAPVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 331 STLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHL 410
Cdd:PRK06048 240 TTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 411 SICTDVKLALEAINRLIEDKqpklkfDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDgNAIISTGVGQHQ 490
Cdd:PRK06048 320 PIVGDAKQVLKSLIKYVQYC------DRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLG 570
Cdd:PRK06048 393 MWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 571 MVVQWEDRFYKANRAHTYLGNPrneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLP 650
Cdd:PRK06048 473 MVRQWQELFYDKRYSHTCIKGS-------VDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
570
....*....|....
gi 720058595 651 MIPSGGAFKDVITE 664
Cdd:PRK06048 546 MVPAGAAINEILDL 559
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
99-668 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 653.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 99 KGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:PRK08527 4 SGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKD 258
Cdd:PRK08527 84 GLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 259 IQQQLVVPNWNTQMKLPGYlsrlpKSPEEAHLEQILRF---ISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTL 333
Cdd:PRK08527 164 VTATLGEFEYPKEISLKTY-----KPTYKGNSRQIKKAaeaIKEAKKPLFYLGGGAILSnaSEEIRELVKKTGIPAVETL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK08527 239 MARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAINRLIEDKQPKlkfDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWA 493
Cdd:PRK08527 319 GDLKNVLKEMLEELKEENPT---TYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 494 AQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVV 573
Cdd:PRK08527 396 AQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 574 QWEDRFYKANRAHTYLgnprnesEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMIP 653
Cdd:PRK08527 476 QWQTFFYEERYSETDL-------STQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVP 548
|
570
....*....|....*
gi 720058595 654 SGGAFKDVITEGDGR 668
Cdd:PRK08527 549 AGGALYNMILPKKKD 563
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
100-655 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 652.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQAL---TRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:CHL00099 12 GAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:CHL00099 92 VTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KD-----IQQQLVVPNwNTQMKLPGYlsRLPKSPEEAHLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPV 329
Cdd:CHL00099 172 KDvglekFDYYPPEPG-NTIIKILGC--RPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIisDAHQEITELAELYKIPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 330 ASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPH 409
Cdd:CHL00099 249 TTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 410 LSICTDVKLALEAINRLIEDKQPKL-KFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQyaiQVLDELTD--GNAIISTGV 486
Cdd:CHL00099 329 VAIVGDVKKVLQELLELLKNSPNLLeSEQTQAWRERINRWRKEYPLLIPKPSTSLSPQ---EVINEISQlaPDAYFTTDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 487 GQHQMWAAQWYKYKrPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNN 566
Cdd:CHL00099 406 GQHQMWAAQFLKCK-PRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 567 QHLGMVVQWEDRFYKANRAHTYLgnprneSEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQE 646
Cdd:CHL00099 485 KWQGMVRQWQQAFYGERYSHSNM------EEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDE 558
|
....*....
gi 720058595 647 HVLPMIPSG 655
Cdd:CHL00099 559 NCYPMVAPG 567
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
100-662 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 640.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGL-KHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK06725 96 LADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQQLVVPNWNTQMKLPGYlsRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTLMGLG 337
Cdd:PRK06725 176 QNEKVTSFYNEVVEIPGY--KPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSggSEELIEFARENRIPVVSTLMGLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 338 AYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVK 417
Cdd:PRK06725 254 AYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 418 LALEAINRLIEDKQPKlkfdfsAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWY 497
Cdd:PRK06725 334 KALHMLLHMSIHTQTD------EWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 498 KYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVVQWED 577
Cdd:PRK06725 408 KAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 578 RFYKANRAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMIPSGGA 657
Cdd:PRK06725 488 MFYENRLSESKIGS--------PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKG 559
|
....*
gi 720058595 658 FKDVI 662
Cdd:PRK06725 560 NNEMI 564
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
100-657 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 639.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 Q---QQLVVPNWNTQMKlpGYLSRLPKSPEEahLEQILRFISESKKPVLYVGGGCLNS----SEELRRFVELTGIPVAST 332
Cdd:PRK09107 173 QfatGTYTPPQKAPVHV--SYQPKVKGDAEA--ITEAVELLANAKRPVIYSGGGVINSgpeaSRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 333 LMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSI 412
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 413 CTDVKLALEAINRLIEDKQPKL-KFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDG-NAIISTGVGQHQ 490
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKARGKKPdKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGrDTYITTEVGQHQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLG 570
Cdd:PRK09107 409 MWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 571 MVVQWEDRFYKANRAHTYlgnprneSEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLP 650
Cdd:PRK09107 489 MVRQWQQLLHGNRLSHSY-------TEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
....*..
gi 720058595 651 MIPSGGA 657
Cdd:PRK09107 562 MIPSGKA 568
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
100-664 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 630.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQQLV-VPNWntqmKLPGYLSRLPkSPEEAHLEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTLMGL 336
Cdd:PRK08155 175 QTAVIeLEAL----PAPAEKDAAP-AFDEESIRDAAAMINAAKRPVLYLGGGVINSgaPARARELAEKAQLPTTMTLMAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 337 GAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDV 416
Cdd:PRK08155 250 GMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 417 KLALEAINRLIEDKQPKlkfdfsAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQW 496
Cdd:PRK08155 330 DDVLAQLLPLVEAQPRA------EWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 497 YKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVVQWE 576
Cdd:PRK08155 404 YPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 577 DRFYKANR-AHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMIPSG 655
Cdd:PRK08155 484 SLFYGQRVfAATYPGK--------INFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPG 555
|
....*....
gi 720058595 656 GAFKDVITE 664
Cdd:PRK08155 556 AANTEMIGE 564
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
100-655 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 629.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIrNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK07710 18 GAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIP-HILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK07710 97 LADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQQLVVPNWNTQMKLPGYlsRLPKSPEEAHLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTLMGLG 337
Cdd:PRK07710 177 VVEEGEFCYDVQMDLPGY--QPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLhaKASKELTSYAEQQEIPVVHTLLGLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 338 AYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVK 417
Cdd:PRK07710 255 GFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 418 LALEAinrLIedKQPKLKFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWY 497
Cdd:PRK07710 335 QALQV---LL--QQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 498 KYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMVVQWED 577
Cdd:PRK07710 410 PFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 720058595 578 RFYKANRAHTYLGNPrneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVLPMIPSG 655
Cdd:PRK07710 490 EFYNQRYSHSLLSCQ-------PDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPG 560
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
99-664 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 619.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 99 KGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIrNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLI-HILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKD 258
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 259 IQ-QQLVVPNWN--TQMKLPGYlsrlpKSPEEAHLEQILR---FISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVA 330
Cdd:PRK06276 161 VQeGELDLEKYPipAKIDLPGY-----KPTTFGHPLQIKKaaeLIAEAERPVILAGGGVIisGASEELIELSELVKIPVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 331 STLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHL 410
Cdd:PRK06276 236 TTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 411 SICTDVKLALEAINRLIEDKQPKLKfdfSAWRKELHE-QKLKFPLSfkTFAEA-IPPQYAIQVLDELTDG-----NAIIS 483
Cdd:PRK06276 316 PIVGDAKNVLRDLLAELMKKEIKNK---SEWLERVKKlKKESIPRM--DFDDKpIKPQRVIKELMEVLREidpskNTIIT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILL 563
Cdd:PRK06276 391 TDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 564 LNNQHLGMVVQWEDRFYKANRAHTYLGNPrneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVP 643
Cdd:PRK06276 471 FDNRTLGMVYQWQNLYYGKRQSEVHLGET-------PDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIID 543
|
570 580
....*....|....*....|.
gi 720058595 644 HQEhVLPMIPSGGAFKDVITE 664
Cdd:PRK06276 544 PAE-ALPMVPPGGNLTNILGP 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
95-655 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 569.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 95 DEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGAT 174
Cdd:PRK07282 7 ESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 175 NLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLID 254
Cdd:PRK07282 87 NAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 255 IPKDIQQQLVVPNWNTQMKLPGYLSRLpkSPEEAHLEQILRFISESKKPVLYVGGGC--LNSSEELRRFVELTGIPVAST 332
Cdd:PRK07282 167 LPKDVSALETDFIYDPEVNLPSYQPTL--EPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 333 LMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSI 412
Cdd:PRK07282 245 LLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 413 CTDVKLALEainRLIEdkQPKLKFDFSAWRKELHEQKLKFPlSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMW 492
Cdd:PRK07282 325 VGDAKKALQ---MLLA--EPTVHNNTEKWIEKVTKDKNRVR-SYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 493 AAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV 572
Cdd:PRK07282 399 AAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 573 VQWEDRFYKANRAHTYLgnprnesEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPgPYLLDVIVPHQEHVLPMI 652
Cdd:PRK07282 479 RQWQESFYEGRTSESVF-------DTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-PMLIEVDISRKEHVLPMV 550
|
...
gi 720058595 653 PSG 655
Cdd:PRK07282 551 PAG 553
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
100-660 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 558.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQqlvvPNWNTQMKLPGYLSRLPKSPE-EAHLEQILRFISE---SKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTL 333
Cdd:PRK06466 166 TN----PAEKFEYEYPKKVKLRSYSPAvRGHSGQIRKAVEMllaAKRPVIYSGGGVVlgNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLAL-EAINRLIEDKQPKLKFDFSAWRKELHEQKLKFPLSF--KTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQ 490
Cdd:PRK06466 322 GPVESVLtEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLFPydKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLG 570
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 571 MVVQWEDRFYKANRAHTYLgnprnesEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLE-TPGPYLLDVIVPHQEHVL 649
Cdd:PRK06466 482 MVRQWQDMQYEGRHSHSYM-------ESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVY 554
|
570
....*....|.
gi 720058595 650 PMIPSGGAFKD 660
Cdd:PRK06466 555 PMQIADGSMRD 565
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
100-661 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 531.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQqlvvPNWNTQMKLPGYLSRLPKSPEEA-HLEQI---LRFISESKKPVLYVGGGCLNSS--EELRRFVELTGIPVASTL 333
Cdd:PRK08979 166 LN----PAILHPYEYPESIKMRSYNPTTSgHKGQIkrgLQALLAAKKPVLYVGGGAIISGadKQILQLAEKLNLPVVSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK08979 242 MGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEA-INRLIEDKQPKLKFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMW 492
Cdd:PRK08979 322 GSADKVLDSmLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 493 AAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV 572
Cdd:PRK08979 402 AALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 573 VQWEDRFYKANRAHTYLGNprneseiFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYL-LDVIVPHQEHVLPM 651
Cdd:PRK08979 482 KQWQDMIYQGRHSHSYMDS-------VPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINVDETEHVYPM 554
|
570
....*....|
gi 720058595 652 IPSGGAFKDV 661
Cdd:PRK08979 555 QIRGGAMNEM 564
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
93-655 |
2.27e-180 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 525.14 E-value: 2.27e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 93 AADEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPG 172
Cdd:PRK06965 16 PPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 173 ATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVL 252
Cdd:PRK06965 96 VTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 253 IDIPKDIQQQLVVPNWNTQMKLPGYlsrlpkSP-EEAHLEQI---LRFISESKKPVLYVGGGCL--NSSEELRRFVELTG 326
Cdd:PRK06965 176 VDIPKDVSKTPCEYEYPKSVEMRSY------NPvTKGHSGQIrkaVSLLLSAKRPYIYTGGGVIlaNASRELRQLADLLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 327 IPVASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRA-KIVHIDIDPAEIGKN 405
Cdd:PRK06965 250 YPVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 406 KQPHLSICTDVKLALEAINRLIEDKQPKLKFD-FSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIIST 484
Cdd:PRK06965 330 VKVDIPIVGDVKEVLKELIEQLQTAEHGPDADaLAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 485 GVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLL 564
Cdd:PRK06965 410 DVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 565 NNQHLGMVVQWEDRFYKANRAHTYLgnprnesEIFPNMLKFAEACDIPAARVTKKSE----LREAMKKMLETpgpYLLDV 640
Cdd:PRK06965 490 NNRYLGMVRQWQEIEYSKRYSHSYM-------DALPDFVKLAEAYGHVGMRIEKTSDvepaLREALRLKDRT---VFLDF 559
|
570
....*....|....*
gi 720058595 641 IVPHQEHVLPMIPSG 655
Cdd:PRK06965 560 QTDPTENVWPMVQAG 574
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
100-662 |
5.74e-178 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 518.70 E-value: 5.74e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 qqqlVVPNWNTQMKLPGYLSRLPKSPE-EAHLEQI---LRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTL 333
Cdd:PRK06882 166 ----VNPANKFTYEYPEEVSLRSYNPTvQGHKGQIkkaLKALLVAKKPVLFVGGGVItaECSEQLTQFAQKLNLPVTSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK06882 242 MGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAINRLIEDKQ-PKLKFDFSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMW 492
Cdd:PRK06882 322 GSAKNVLEEFLSLLEEENlAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 493 AAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV 572
Cdd:PRK06882 402 AALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 573 VQWEDRFYKANRAHTYLGNprneseiFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYL-LDVIVPHQEHVLPM 651
Cdd:PRK06882 482 KQWQDLIYSGRHSQVYMNS-------LPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPM 554
|
570
....*....|.
gi 720058595 652 IPSGGAFKDVI 662
Cdd:PRK06882 555 QIRGGAMNEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
100-657 |
9.92e-169 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 494.75 E-value: 9.92e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 qqqlVVPNWNTQMKLPGYLSRLPKSPE-EAHLEQI---LRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTL 333
Cdd:PRK07979 166 ----LNPANKLPYVWPESVSMRSYNPTtQGHKGQIkraLQTLVAAKKPVVYVGGGAINAacHQQLKELVEKLNLPVVSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK07979 242 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAINRLIEDKQPKLKFD-FSAWRKELHEQKLKFPLSFKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQMW 492
Cdd:PRK07979 322 GDARQVLEQMLELLSQESAHQPLDeIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 493 AAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV 572
Cdd:PRK07979 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 573 VQWEDRFYKANRAHTYLgnprnesEIFPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLL---DVIVPHQEHVL 649
Cdd:PRK07979 482 KQWQDMIYSGRHSQSYM-------QSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLvfvDVTVDGSEHVY 554
|
....*...
gi 720058595 650 PMIPSGGA 657
Cdd:PRK07979 555 PMQIRGGG 562
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
100-662 |
8.11e-135 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 407.69 E-value: 8.11e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALT---RSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQ-QQLVVPNWNTQMKLPGYlSRLPKSPEEAHLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTL 333
Cdd:PRK06456 164 RDIFyEKMEEIKWPEKPLVKGY-RDFPTRIDRLALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDR-VTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSI 412
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRtFTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 413 CTDVKLAL-EAINRLIEDKQpklKFDFSAWRKELHEQKlKFPLSFKTFAE--AIPPQYAIQVLDELTDGNAIISTGVGQH 489
Cdd:PRK06456 323 YGNAKIILrELIKAITELGQ---KRDRSAWLKRVKEYK-EYYSQFYYTEEngKLKPWKIMKTIRQALPRDAIVTTGVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 490 QMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHL 569
Cdd:PRK06456 399 QMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 570 GMVVQWEDRFYKANRAHTYLGNPrneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHVL 649
Cdd:PRK06456 479 GLVRQVQDLFFGKRIVGVDYGPS-------PDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAL 551
|
570
....*....|...
gi 720058595 650 PMIPSGGAFKDVI 662
Cdd:PRK06456 552 PTLPPGGRLKQVI 564
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
101-642 |
9.10e-118 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 364.30 E-value: 9.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARAS-GLPGVCVATSGPGATNLVSG 179
Cdd:PRK11269 7 VDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK11269 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQQLVVPNWNTQMKLPGYlsrlPKSPEEAHLEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTLMGLG 337
Cdd:PRK11269 167 QVAEIEFDPDTYEPLPVY----KPAATRAQIEKALEMLNAAERPLIVAGGGVINAdaSDLLVEFAELTGVPVIPTLMGWG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 338 AYPgsDDLSLhMLGMHG----TVYANYAVDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK11269 243 AIP--DDHPL-MAGMVGlqtsHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAINRLIEDKQP--KLKfDFSAWRKELheQKLKFPLSFKTFAEAIP--PQYAIQVLDELTDGNAIISTGVGQH 489
Cdd:PRK11269 320 SDAKAALELLVEVAREWKAagRLP-DRSAWVADC--QERKRTLLRKTHFDNVPikPQRVYEEMNKAFGRDTCYVSTIGLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 490 QMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHL 569
Cdd:PRK11269 397 QIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 570 GMVVQWEDRF---YKANRAHTYLGNPRNESEIFPNmLKFAEACDIPAARVTKKSELREAMKK----MLETPGPYLLDVIV 642
Cdd:PRK11269 477 GLIRQAQRAFdmdYCVQLAFENINSPELNGYGVDH-VKVAEGLGCKAIRVFKPEDIAPALEQakalMAEFRVPVVVEVIL 555
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
99-646 |
7.19e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 360.68 E-value: 7.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 99 KGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSI-KLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVP--RRMIGTdaFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK08322 81 GVAYAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQQQLV--VPnwntqmkLPGYLSRLPkSPEEAHLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVAST 332
Cdd:PRK08322 159 EDIAAEETdgKP-------LPRSYSRRP-YASPKAIERAAEAIQAAKNPLILIGAGANrkTASKALTEFVDKTGIPFFTT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 333 LMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGvrFDdrVTGKVEAFASRA---KIVHIDIDPAEIGKNKQPH 409
Cdd:PRK08322 231 QMGKGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD--VIEKPPFFMNPNgdkKVIHINFLPAEVDPVYFPQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 410 LSICTDVKLALEAINRLIEDkQPKLKFDFSAWRKELHEQKLK-------FPlsfktfaeaIPPQYAIQVLDELTDGNAII 482
Cdd:PRK08322 307 VEVVGDIANSLWQLKERLAD-QPHWDFPRFLKIREAIEAHLEegadddrFP---------MKPQRIVADLRKVMPDDDIV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 483 STGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELAT-VRvENLPIKI 561
Cdd:PRK08322 377 ILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETaVR-LGLPLVV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 562 LLLNNQHLGMvVQW-EDRFYKANRAHTYlGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDV 640
Cdd:PRK08322 456 LILNDNAYGM-IRWkQENMGFEDFGLDF-GN--------PDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDC 525
|
....*.
gi 720058595 641 IVPHQE 646
Cdd:PRK08322 526 PVDYSE 531
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
463-655 |
1.86e-115 |
|
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: 343.71 E-value: 1.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 463 IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSF 542
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 543 IMNVQELATVRVENLPIKILLLNNQHLGMVVQWEDRFYKANRAHTYLGnprneseIFPNMLKFAEACDIPAARVTKKSEL 622
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLD-------SNPDFVKLAEAYGIKGLRVEKPEEL 153
|
170 180 190
....*....|....*....|....*....|...
gi 720058595 623 REAMKKMLETPGPYLLDVIVPHQEHVLPMIPSG 655
Cdd:cd02015 154 EAALKEALASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
97-650 |
2.28e-97 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 310.27 E-value: 2.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 97 PRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:PRK08199 7 ARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK08199 87 SIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDI-QQQLVVPNwntqmkLPGYlSRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTL 333
Cdd:PRK08199 167 EDVlSETAEVPD------APPY-RRVAAAPGAADLARLAELLARAERPLVILGGSGWTEaaVADLRAFAERWGLPVACAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSD-----DLSlhmLGMHGTVYAnyAVDKSDLLLAFGVRFDDRVTGK---VEAFASRAKIVHIDIDPAEIGKN 405
Cdd:PRK08199 240 RRQDLFDNRHpnyagDLG---LGINPALAA--RIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 406 KQPHLSICTDVKLALEAINRLiedkQPKLKFDFSAWRKELHEQKLKFplsfkTFAEAIPPQY----AIQVLDELTDGNAI 481
Cdd:PRK08199 315 YRPDLAIVADPAAFAAALAAL----EPPASPAWAEWTAAAHADYLAW-----SAPLPGPGAVqlgeVMAWLRERLPADAI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 482 ISTGVGQHQMWAAQWYKYKRPRQWL--TSgglGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPI 559
Cdd:PRK08199 386 ITNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 560 KILLLNNQHLGMVVQWEDRFYKANRAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLD 639
Cdd:PRK08199 463 IVIVVNNGMYGTIRMHQEREYPGRVSGTDLTN--------PDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIE 534
|
570
....*....|.
gi 720058595 640 VIVPhQEHVLP 650
Cdd:PRK08199 535 IRID-PEAITP 544
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
100-650 |
8.19e-95 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 303.09 E-value: 8.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSI-IRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQ--ETP-IVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDI 255
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPdQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 256 PKDIQQQlvvpnwNTQMKLPGYLSRLPK-SPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLM 334
Cdd:PRK08266 166 PWDVFGQ------RAPVAAAPPLRPAPPpAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 335 GLGAYPGSDDLSLHMLgmhgtvyANYAV-DKSDLLLAFGVRFDDRVTgKVEAFASRAKIVHIDIDPAEIGKnKQPHLSIC 413
Cdd:PRK08266 240 GRGIVSDRHPLGLNFA-------AAYELwPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRR-LKPDVAIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEAInrliEDKQPKLKFDFSAWRKELHEqklkfpLSFKTFAE--AIPPQYA-IQVLDELTDGNAIISTGVGQHQ 490
Cdd:PRK08266 311 ADAKAGTAAL----LDALSKAGSKRPSRRAELRE------LKAAARQRiqAVQPQASyLRAIREALPDDGIFVDELSQVG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAaqWYKYK--RPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQH 568
Cdd:PRK08266 381 FAS--WFAFPvyAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 569 LGMVVQWEDRFYKANRAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHV 648
Cdd:PRK08266 459 YGNVRRDQKRRFGGRVVASDLVN--------PDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEA 530
|
..
gi 720058595 649 LP 650
Cdd:PRK08266 531 SP 532
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
98-650 |
1.50e-94 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 303.46 E-value: 1.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 98 RKGADVLVEALEREGVTTVFAYPGGASLEIHQAL-TRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:PRK08611 4 IKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIdIP 256
Cdd:PRK08611 84 LNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLT-IP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQQQLVvpNWNTQMKLPGYLSRLPkSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMGL 336
Cdd:PRK08611 163 DDLPAQKI--KDTTNKTVDTFRPTVP-SPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 337 GAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDdrvtgKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDV 416
Cdd:PRK08611 240 GIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYP-----YVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 417 KLALEAINRLIEdKQPKLKF------DFSAWRKELHEQKLK--FPLSfktfaeaipPQYAIQVLDELTDGNAIISTGVGQ 488
Cdd:PRK08611 315 KKALHQLTENIK-HVEDRRFleacqeNMAKWWKWMEEDENNasTPIK---------PERVMAAIQKIADDDAVLSVDVGT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 489 HQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQH 568
Cdd:PRK08611 385 VTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 569 LGMvVQWEDRF-----YKANrahtyLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVP 643
Cdd:PRK08611 465 LAF-IKYEQQAageleYAID-----LSD--------MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD 530
|
....*..
gi 720058595 644 HQEHVLP 650
Cdd:PRK08611 531 PNAAPLP 537
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
101-644 |
1.00e-88 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 286.87 E-value: 1.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGI-RHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGqVPRRM---IGTDAFQETPIVE-VTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK07524 84 GQAYADSIPMLVISS-VNRRAslgKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIqqqLVVPNWNTQMKLPGYLSRLPKSPEEahLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMGL 336
Cdd:PRK07524 163 LDV---LAAPADHLLPAPPTRPARPGPAPAA--LAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTINAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 337 GAYPGSDDLSlhmLGMHGTVYANYA-VDKSDLLLAFGVRF---DDRVTGKvEAFASRAKIVHIDIDPAEIGKNKQPHLSI 412
Cdd:PRK07524 238 GLLPAGHPLL---LGASQSLPAVRAlIAEADVVLAVGTELgetDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 413 CTDVKLALEAINRLIEDKQPKLkfDFSAWRKELHEQKLkfplsfktfAEAIPPQYAIQ------VLDELTDgnAII---S 483
Cdd:PRK07524 314 VGDARAALEALLARLPGQAAAA--DWGAARVAALRQAL---------RAEWDPLTAAQvalldtILAALPD--AIFvgdS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TGV---GQHqmwaaqWYKYKRPRQWLTSG-GLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPI 559
Cdd:PRK07524 381 TQPvyaGNL------YFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 560 KILLLNNQHLGmvvqwEDRFYKANRAHTYLG-NPRNeseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLL 638
Cdd:PRK07524 455 IVLLWNNDGYG-----EIRRYMVARDIEPVGvDPYT-----PDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLI 524
|
....*.
gi 720058595 639 DVIVPH 644
Cdd:PRK07524 525 EVDQAC 530
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
101-653 |
1.28e-86 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 281.72 E-value: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKV-KYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRpGPVLIDIPKDIQ 260
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 261 QqlvvpnwNTQMKLPGYLSRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMGLGAYP 340
Cdd:PRK06457 163 R-------KSSEYKGSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 341 GSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDdrvtgKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVKlal 420
Cdd:PRK06457 236 DLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVA--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 421 EAINRLIEDKQPK----LKFDFSAWRKELheQKLKFPLSfktfaEAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQW 496
Cdd:PRK06457 308 EFLNIDIEEKSDKfyeeLKGKKEDWLDSI--SKQENSLD-----KPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 497 YKYKRPRQWLTSGGLGAMGFGLPAAIGASVAR-PDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMvVQW 575
Cdd:PRK06457 381 FRASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGM-IKF 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720058595 576 EDRFykanrahtyLGNPRNESEIF-PNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEHvlPMIP 653
Cdd:PRK06457 460 EQEV---------MGYPEWGVDLYnPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNER--PMPP 527
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
95-642 |
6.41e-85 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 277.12 E-value: 6.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 95 DEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGAT 174
Cdd:PRK08617 2 DKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGP-ELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 175 NLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLID 254
Cdd:PRK08617 81 NLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 255 IPKDIQQQLVvpnwNTQMKLPGYLSRLPKSPEEAhLEQILRFISESKKPVLYVG--GGCLNSSEELRRFVELTGIPVAST 332
Cdd:PRK08617 161 LPQDVVDAPV----TSKAIAPLSKPKLGPASPED-INYLAELIKNAKLPVLLLGmrASSPEVTAAIRRLLERTNLPVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 333 LMGLGAYpgSDDLSLHMLGMHGtVYANYAVD----KSDLLLAFG---VRFDDRVTGKveafASRAKIVHIDIDPAEIGKN 405
Cdd:PRK08617 236 FQAAGVI--SRELEDHFFGRVG-LFRNQPGDellkKADLVITIGydpIEYEPRNWNS----EGDATIIHIDVLPAEIDNY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 406 KQPHLSICTDVKLALEAINRLIEDKQ--PKLKFDFSAWRKELHEQKlKFPLSFKTFaeAIPPQYAIQVLDELTDGNAIIS 483
Cdd:PRK08617 309 YQPERELIGDIAATLDLLAEKLDGLSlsPQSLEILEELRAQLEELA-ERPARLEEG--AVHPLRIIRALQDIVTDDTTVT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELAT-VRVeNLPIKIL 562
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETaVRL-KLNIVHI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 563 LLNNQHLGMVVQWEDRFYKANrAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIV 642
Cdd:PRK08617 465 IWNDGHYNMVEFQEEMKYGRS-SGVDFGP--------VDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
100-651 |
3.36e-84 |
|
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: 275.09 E-value: 3.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGI-ELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QQQLVvpnwnTQMKLPgyLSRLPK--SPEEAHLEQILRFISESKKPVLYVG--GGCLNSSEELRRFVELTGIPVASTLMG 335
Cdd:TIGR02418 160 VDSPV-----SVKAIP--ASYAPKlgAAPDDAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 336 LGAYpgSDDLSLHMLGMHGtVYANYAVD----KSDLLLAFG---VRFDDRVTGKveafASRAKIVHIDIDPAEIGKNKQP 408
Cdd:TIGR02418 233 AGAV--SRELEDHFFGRVG-LFRNQPGDrllkQADLVITIGydpIEYEPRNWNS----ENDATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 409 HLSICTDVKLALEAINR------LIEDKQPKLKfdfsAWRKELHEQKlKFPLSFKTFaeAIPPQYAIQVLDELTDGNAII 482
Cdd:TIGR02418 306 DLELVGDIASTLDLLAEripgyeLPPDALAILE----DLKQQREALD-RVPATLKQA--HLHPLEIIKAMQAIVTDDVTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 483 STGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELAT-VRVeNLPIKI 561
Cdd:TIGR02418 379 TVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETaVRL-KLNIVH 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 562 LLLNNQHLGMVVQWEDRFYKanrahtylgnpRNESEIFPNM--LKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLD 639
Cdd:TIGR02418 458 IIWNDNGYNMVEFQEEMKYQ-----------RSSGVDFGPIdfVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVD 526
|
570
....*....|..
gi 720058595 640 VIVPHQEHVLPM 651
Cdd:TIGR02418 527 IPVDYSDNPKLM 538
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
100-641 |
9.32e-82 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 269.71 E-value: 9.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFaypgGASLEIHQALTRSSI-IRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF----GQSLPSALFLAAEAIgIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKD 258
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 259 IqqqLVVPNWNTQMKLPGYLSRLP---KSPEEAHLEQILRFISESKKPVLYVGGG--CLNSSEELRRFVELTGIPVASTL 333
Cdd:PRK06112 172 L---LTAAAAAPAAPRSNSLGHFPldrTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLG--MHGTVYANYA---VDKSDLLLAFGVRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQP 408
Cdd:PRK06112 249 MGKGAVDETHPLSLGVVGslMGPRSPGRHLrdlVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYEA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 409 hLSICTDVKLALEAI-NRLIEDKQPKLKFDFSAWRKELHEQKLKFPLSFKTFA--EAIP--PQYAIQVLDELTDGNAIIS 483
Cdd:PRK06112 329 -LRLVGDARLTLAALtDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVAlsDASPirPERIMAELQAVLTGDTIVV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TGVGQHQMWAAQWYKYKRPRQ-WLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKIL 562
Cdd:PRK06112 408 ADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIV 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 563 LLNNQHLGmvvqwedrfYKANRAHTYLGNPRNESEIFP-NMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVI 641
Cdd:PRK06112 488 VLNNGILG---------FQKHAETVKFGTHTDACHFAAvDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVI 558
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
101-631 |
5.00e-74 |
|
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: 249.39 E-value: 5.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGI-RFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRpGPVLIDIPKDIQ 260
Cdd:TIGR03457 84 AAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 261 QQLVvpnwNTQMKLPGYLSRLPKSPEEahLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVASTLMGLGA 338
Cdd:TIGR03457 163 YGEI----DVEIPRPVRLDRGAGGATS--LAQAARLLAEAKFPVIISGGGVVmgDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 339 YPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVR---FDDRVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTD 415
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 416 VKLALEAINRLI---------EDKQPKLKFDFSAWRKELHE---QKLKFPLSFKTFAEAIPPQY--AIQVLDELTDG--- 478
Cdd:TIGR03457 317 AKAAAAEILQRLagkagdanrAERKAKIQAERSAWEQELSEmthERDPFSLDMIVEQRQEEGNWlhPRQVLRELEKAmpe 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 479 NAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLP 558
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720058595 559 IKILLLNNQHLGMVVQWEDRFYKANRAHTYLGNPrneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLE 631
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESE-------LSFAGIADAMGAKGVVVDKPEDVGPALKKAIA 542
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
100-640 |
3.80e-73 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 246.06 E-value: 3.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDA--FQETP-IVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIP 256
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPYLDQDLgyIHEAPdQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQQQLVVpnwntqmkLPGYLSRLPKS---PEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELtGIPVASTL 333
Cdd:PRK07064 165 IDIQAAEIE--------LPDDLAPVHVAvpePDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDL-GFGVVTST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 334 MGLGAYPGSDDLSLHMLGMHGTVYANYAvdKSDLLLAFGVRFDDRVTGKVEaFASRAKIVHIDIDPAEIGKNKQPHLSIC 413
Cdd:PRK07064 236 QGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLRGNETLKYS-LALPRPLIRVDADAAADGRGYPNDLFVH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 414 TDVKLALEainRLIEDKQPKLKFDfSAWRKELHEQKlkfPLSFKTFAEAIPPqYA--IQVLDELTDGNAII--------S 483
Cdd:PRK07064 313 GDAARVLA---RLADRLEGRLSVD-PAFAADLRAAR---EAAVADLRKGLGP-YAklVDALRAALPRDGNWvrdvtisnS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TgvgqhqmWAAQWYKYKRPRQWLTSGGlGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILL 563
Cdd:PRK07064 385 T-------WGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVL 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 720058595 564 LNNQHLGMVVQWEDRFYKANRAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDV 640
Cdd:PRK07064 457 MNDGGYGVIRNIQDAQYGGRRYYVELHT--------PDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
104-631 |
1.24e-71 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 242.98 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 104 LVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGLADA 183
Cdd:PRK07525 12 FVETLQAHGITHAFGIIGSAFMDASDLFPPAGI-RFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 184 MLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRpGPVLIDIPKDIQQQL 263
Cdd:PRK07525 91 YWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFYGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 264 VvpnwntQMKLPGyLSRLPKSP-EEAHLEQILRFISESKKPVLYVGGGCLNSS--EELRRFVELTGIPVASTLMGLGAYP 340
Cdd:PRK07525 170 I------DVEIPQ-PVRLERGAgGEQSLAEAAELLSEAKFPVILSGAGVVLSDaiEECKALAERLDAPVACGYLHNDAFP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 341 GSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVT----GkVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDV 416
Cdd:PRK07525 243 GSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGTlpqyG-IDYWPKDAKIIQVDINPDRIGLTKKVSVGICGDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 417 KLALEAINRLIEDKQP----------KLKFDFSAWRKEL----HEQKlKFPLSFKTFAEAIPPQY--AIQVLDELTDG-- 478
Cdd:PRK07525 322 KAVARELLARLAERLAgdagreerkaLIAAEKSAWEQELsswdHEDD-DPGTDWNEEARARKPDYmhPRQALREIQKAlp 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 479 -NAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENL 557
Cdd:PRK07525 401 eDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNW 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 558 PIKILLLNNQhlgmvvQW--EDR----FYKANRAHTYLGNPRNESEIfpnmlkfAEACDIPAARVTKKSELREAMKKMLE 631
Cdd:PRK07525 481 PVTAVVFRNY------QWgaEKKnqvdFYNNRFVGTELDNNVSYAGI-------AEAMGAEGVVVDTQEELGPALKRAID 547
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
101-650 |
1.16e-70 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 239.89 E-value: 1.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRpGPVLIDIPKDIQ 260
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVAVVVLPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 261 QQLV----VPNWntqmklpgYLSRLPK-SPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMG 335
Cdd:PRK09124 165 LKPAperaTPHW--------YHAPQPVvTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 336 LGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRvtgkvEAFASRAKIVHIDIDPAEIGKNKQPHLSICTD 415
Cdd:PRK09124 237 KEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 416 VKLALEAINRLIEDKQPKLKFD-----FSAWRKELHEqkLKFPlsfKTFAEAIPPQYAIQVLDELTDGNAIISTGVGQHQ 490
Cdd:PRK09124 312 VKATLAALLPLLEEKTDRKFLDkalehYRKARKGLDD--LAVP---SDGGKPIHPQYLARQISEFAADDAIFTCDVGTPT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 491 MWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLG 570
Cdd:PRK09124 387 VWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 571 MvVQWEdrfYKAN---RAHTYLGNPRneseiFPNMlkfAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIVPHQEH 647
Cdd:PRK09124 467 F-VAME---MKAGgylTDGTDLHNPD-----FAAI---AEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQEL 534
|
...
gi 720058595 648 VLP 650
Cdd:PRK09124 535 AMP 537
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
102-257 |
1.19e-69 |
|
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: 223.56 E-value: 1.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 102 DVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIiRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGLA 181
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGI-RYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720058595 182 DAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPK 257
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
101-641 |
1.24e-66 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 229.10 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASsGRPGPVLIDIPKDIQ 260
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 261 QQLVVPNWNTQMKLPGylsRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMGLGAYP 340
Cdd:PRK06546 165 DEPAPEGFAPSVISPR---RPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 341 GSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFddrvtgKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVKLAL 420
Cdd:PRK06546 242 YDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 421 EAINRLIEDKQPKlKFDFSAWRKelHEQKLKFPL-SFKTFAE---AIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAqw 496
Cdd:PRK06546 316 RALLPLVKEKTDR-RFLDRMLKK--HARKLEKVVgAYTRKVEkhtPIHPEYVASILDELAADDAVFTVDTGMCNVWAA-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 497 yKYKRP---RQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGMV- 572
Cdd:PRK06546 391 -RYITPngrRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVk 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720058595 573 ----VQwedrfykanrahtylGNPRNESEIFP-NMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVI 641
Cdd:PRK06546 470 lemlVD---------------GLPDFGTDHPPvDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVV 528
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
100-644 |
6.28e-65 |
|
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: 224.71 E-value: 6.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALT-RSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSaERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSgRPGPVLIDIPKD 258
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 259 IQQQLVVPNWNTQMKLPGYLSRLPkSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLMGLGA 338
Cdd:TIGR02720 160 FGWQEIPDNDYYASSVSYQTPLLP-APDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 339 YPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDdrVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVKL 418
Cdd:TIGR02720 239 IEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 419 ALEAINRLIEDKQPK-----LKFDFSAWRKELHEqklkfpLSFKTFAEAIPPQyAIQVLDELTDGNAIISTGVGQHQMWA 493
Cdd:TIGR02720 317 ALAAILAQVEPRESTpwwqaNVANVKNWRAYLAS------LEDKTEGPLQAYQ-VYRAINKIAEDDAIYSIDVGDININS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 494 AQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQHLGmvv 573
Cdd:TIGR02720 390 NRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYG--- 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720058595 574 qwedrFYKANRAHTylgnPRNESEI-FPNM--LKFAEACDIPAARVTKKSELREAMK--KMLETPGPYLLDVIVPH 644
Cdd:TIGR02720 467 -----FIKDEQEDT----NQPLIGVdFNDAdfAKIAEGVGAVGFRVNKIEQLPAVFEqaKAIKQGKPVLIDAKITG 533
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
485-640 |
3.69e-63 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 206.28 E-value: 3.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 485 GVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLL 564
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720058595 565 NNQHLGMVVQWEDRFYKANRAHTYLGNPRNeseifPNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDV 640
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILPP-----VDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
85-641 |
1.88e-61 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 215.06 E-value: 1.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 85 PSTFVPrfAADEPRKGADVLVEALEREGVTTVFAYPGGASLEIHQALTrssiIRNVLPRHEQGGIFAAEGYARASG--LP 162
Cdd:PRK06154 9 PNAHLP--AEAKTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAAG----IRPVIARTERVAVHMADGYARATSgeRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 163 GVCVATSGPGATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETpiVEVTRSITKHNYLVLDVEDIPRIVHEAFYL 242
Cdd:PRK06154 83 GVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPNFES--LRNYRHITKWCEQVTLPDEVPELMRRAFTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 243 ASSGRPGPVLIDIPKDIQQQLVVpnwntqmKLPGYLSRLPKS---PEEAHLEQILRFISESKKPVLYVGGGCLNSS--EE 317
Cdd:PRK06154 161 LRNGRPGPVVLELPVDVLAEELD-------ELPLDHRPSRRSrpgADPVEVVEAAALLLAAERPVIYAGQGVLYAQatPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 318 LRRFVELTGIPVASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDLLLAFGVRFDDRVTGKveAFASRAKIVHIDI 397
Cdd:PRK06154 234 LKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 398 DPAEIGKNKQPHLSICTDVKLALEAINRLIE---DKQPKLKFDFSAWRKELHEQKLKFPLSFKTFAEA-IPPQYAIQVLD 473
Cdd:PRK06154 312 DDADLNKDYPIDHGLVGDAALVLKQMIEELRrrvGPDRGRAQQVAAEIEAVRAAWLAKWMPKLTSDSTpINPYRVVWELQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 474 E-LTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATV 552
Cdd:PRK06154 392 HaVDIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 553 RVENLPIKILLLNNQHLG-----MVVQWEDrfYKANRahtylgnprneseIFPNMLKFAEACDIPAARVTKKSELREAMK 627
Cdd:PRK06154 472 VRERIPILTILLNNFSMGgydkvMPVSTTK--YRATD-------------ISGDYAAIARALGGYGERVEDPEMLVPALL 536
|
570
....*....|....*..
gi 720058595 628 KML---ETPGPYLLDVI 641
Cdd:PRK06154 537 RALrkvKEGTPALLEVI 553
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
100-264 |
2.54e-61 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 202.08 E-value: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETP-IVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKD 258
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQELdQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*.
gi 720058595 259 IQQQLV 264
Cdd:pfam02776 161 VLLEEV 166
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
100-566 |
1.33e-58 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 206.50 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQAlTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDG-AREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDi 259
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 qqqlVVPNWNTQMKLPGYLSRLPK--SPEEAHLEQILRFISESKKPVLYVGGGC-LNSSEE-LRRFVELTGIPVASTLMG 335
Cdd:PRK05858 165 ----HAFSMADDDGRPGALTELPAgpTPDPDALARAAGLLAEAQRPVIMAGTDVwWGHAEAaLLRLAEELGIPVLMNGMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 336 LGAYPGSDDLSLhmlgmhgTVYANYAVDKSDLLLAFGVRFDDRVTGKVeaFASRAKIVHIDIDPAEIGKNKQPHLSICTD 415
Cdd:PRK05858 241 RGVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRLGFGV--FGGTAQLVHVDDAPPQRAHHRPVAAGLYGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 416 VKLALEAINrliedKQPKLKFDFSAWRKELHE------QKLKFPLSfktfAEAIP--PQYAIQVLDELTDGNAIISTGVG 487
Cdd:PRK05858 312 LSAILSALA-----GAGGDRTDHQGWIEELRTaetaarARDAAELA----DDRDPihPMRVYGELAPLLDRDAIVIGDGG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720058595 488 QHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNN 566
Cdd:PRK05858 383 DFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNN 461
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
290-423 |
1.59e-56 |
|
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: 188.16 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 290 LEQILRFISESKKPVLYVGGGCLNS--SEELRRFVELTGIPVASTLMGLGAYPGSDDLSLHMLGMHGTVYANYAVDKSDL 367
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSgaSEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 720058595 368 LLAFGVRFDD-RVTGKVEAFASRAKIVHIDIDPAEIGKNKQPHLSICTDVKLALEAI 423
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
101-642 |
6.38e-56 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 200.52 E-value: 6.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRS-SIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITkHNYLVLDV--EDIPRIVHEAFYLASSGRpGPVLIDIPK 257
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTvpEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 258 DIQQQLVVP---NWNTQMKLPGYlSRLPKSPEEAHLEQILRFISESKKPVLYVGGGCLNSSEELRRFVELTGIPVASTLM 334
Cdd:PRK08273 164 DVQELEYEPpphAHGTVHSGVGY-TRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKALL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 335 GLGAYPgsDDLSL--HMLGMHGTVYANYAVDKSDLLLAFGVRFddrvtgKVEAF---ASRAKIVHIDIDPAEIGkNKQP- 408
Cdd:PRK08273 243 GKAALP--DDLPWvtGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFlpkEGQARGVQIDIDGRMLG-LRYPm 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 409 HLSICTDVKLALEAINRLIEDKQP-----KLKFDFSAWRKELHEQKLkfplsfkTFAEAIPPQYAIQVLDELTDGNAIIS 483
Cdd:PRK08273 314 EVNLVGDAAETLRALLPLLERKKDrswreRIEKWVARWWETLEARAM-------VPADPVNPQRVFWELSPRLPDNAILT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 484 TGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMN-VQELATV-----RVENL 557
Cdd:PRK08273 387 ADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVakywrQWSDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 558 PIKILLLNNQHLGMVVqWEDRfykanrahTYLGNPRNE-SEIFPNM--LKFAEACDIPAARVTKKSELREAMKKMLETPG 634
Cdd:PRK08273 467 RLIVLVLNNRDLNQVT-WEQR--------VMEGDPKFEaSQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEALAADR 537
|
....*...
gi 720058595 635 PYLLDVIV 642
Cdd:PRK08273 538 PVVLEVKT 545
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
469-642 |
2.16e-50 |
|
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: 172.83 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 469 IQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQE 548
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 549 LATVRVENLPIKILLLNNQHLGMVVQWEDRFYKANRAHTYLGNprneseifPNMLKFAEACDIPAARVTKKSELREAMKK 628
Cdd:cd00568 83 LATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN--------PDFAALAEAYGAKGVRVEDPEDLEAALAE 154
|
170
....*....|....
gi 720058595 629 MLETPGPYLLDVIV 642
Cdd:cd00568 155 ALAAGGPALIEVKT 168
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
99-262 |
1.42e-48 |
|
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: 167.73 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 99 KGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVS 178
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 179 GLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRpGPVLIDIPKD 258
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....
gi 720058595 259 IQQQ 262
Cdd:cd07039 160 VQDA 163
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
98-644 |
1.69e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 167.87 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 98 RKGADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPR-----HEQGGIFAAEGYARASGLPGVCVATSGPG 172
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRPLPEfvicpHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 173 ATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPI---------VEVTRSITKHNYLVLDVEDIPRIVHEAFYLA 243
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAGRSPYTEEGELGSRNTRIhwtqemrdqGGLVREYVKWDYEIRRGDQIGEVVARAIQIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 244 SSGRPGPVLIDIPKDIqqqLVVPNWNTQMKLPGYLSRLPKSPEEAHLEQILRFISESKKPVLYV--GGGCLNSSEELRRF 321
Cdd:PRK08327 167 MSEPKGPVYLTLPREV---LAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITwrAGRTAEGFASLRRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 322 VELTGIPVASTLMGLGAYPGSddlslHmlGMHGTVYANYAVDKSDLLLAFgvrfDDRV--TGKVEAFASRAKIVHIDIDP 399
Cdd:PRK08327 244 AEELAIPVVEYAGEVVNYPSD-----H--PLHLGPDPRADLAEADLVLVV----DSDVpwIPKKIRPDADARVIQIDVDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 400 AeigKNKQP------HLSICTDVKLALEAIN-----RLIEDKQPKLKFDFSAWRKELHEQKLKFP-LSFKTFAEAIPPQY 467
Cdd:PRK08327 313 L---KSRIPlwgfpcDLCIQADTSTALDQLEerlksLASAERRRARRRRAAVRELRIRQEAAKRAeIERLKDRGPITPAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 468 AIQVLDELTDGNAIIST--GVGQHQMwaaqwyKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMN 545
Cdd:PRK08327 390 LSYCLGEVADEYDAIVTeyPFVPRQA------RLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 546 VQE--LATVRVENLPIKILLLNNQHLGMVVQWEDRFYK---ANRAHTYLG---NPRneseifPNMLKFAEACDIPAARVT 617
Cdd:PRK08327 464 VPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyAARKGTFPGtdfDPR------PDFAKIAEAFGGYGERVE 537
|
570 580 590
....*....|....*....|....*....|.
gi 720058595 618 KKSELREAMKKMLETP----GPYLLDVIVPH 644
Cdd:PRK08327 538 DPEELKGALRRALAAVrkgrRSAVLDVIVDR 568
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
101-567 |
3.42e-44 |
|
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: 166.49 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVaTSGPGATNLVSGL 180
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVT-TYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGqvprrMIGTDAFQETPIV-------------EVTRSITKHnYLVLDVED----IPRIVHEAFYla 243
Cdd:COG3961 87 AGAYAERVPVVHIVG-----APGTRAQRRGPLLhhtlgdgdfdhflRMFEEVTVA-QAVLTPENaaaeIDRVLAAALR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 244 sSGRpgPVLIDIPKDIQQQLVVPnwntqMKLPGYLSRLPKSPE--EAHLEQILRFISESKKPVLYVG-----GGClnsSE 316
Cdd:COG3961 159 -EKR--PVYIELPRDVADAPIEP-----PEAPLPLPPPASDPAalAAAVAAAAERLAKAKRPVILAGvevhrFGL---QE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 317 ELRRFVELTGIPVASTLMG-----------LGAYPGSddlslhmlGMHGTVYAnyAVDKSDLLLAFGVRFDDRVTGKVEA 385
Cdd:COG3961 228 ELLALAEKTGIPVATTLLGksvldeshpqfIGTYAGA--------ASSPEVRE--YVENADCVLCLGVVFTDTNTGGFTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 386 FASRAKIVHIDIDPAEIGKNKQPhlsictDVKLAlEAINRLIEdkqpKLKFDFSAWRKELHEQKLKF-----PLSFKTFA 460
Cdd:COG3961 298 QLDPERTIDIQPDSVRVGGHIYP------GVSLA-DFLEALAE----LLKKRSAPLPAPAPPPPPPPaapdaPLTQDRLW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 461 EaippqyaiQVLDELTDGNAIIS-TG-----------------VGQhqmwaAQWykykrprqwltsgglGAMGFGLPAAI 522
Cdd:COG3961 367 Q--------RLQAFLDPGDIVVAdTGtslfgaadlrlpegatfIAQ-----PLW---------------GSIGYTLPAAL 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 720058595 523 GASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQ 567
Cdd:COG3961 419 GAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNND 463
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
463-646 |
3.77e-44 |
|
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: 156.15 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 463 IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSF 542
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 543 IMNVQELATVRVENLPIKILLLNNQHLGMvVQWEDRFykanrahtyLGNPRNESE-IFPNMLKFAEACDIPAARVTKKSE 621
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGF-IKWEQEV---------MGQPEFGVDlPNPDFAKIAEAMGIKGIRVEDPDE 151
|
170 180
....*....|....*....|....*
gi 720058595 622 LREAMKKMLETPGPYLLDVIVPHQE 646
Cdd:cd02014 152 LEAALDEALAADGPVVIDVVTDPNE 176
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
100-643 |
7.46e-40 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 154.37 E-value: 7.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQaLTRSSIIRNVLPRHEQ--GGIFAAEGYAraSGLPGVCVATSGPGATNLV 177
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVGIPITDLAR-LAQAEGIRYIGFRHEQsaGNAAAAAGFL--TQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 178 SGLADAMLDSVPLVAITGQVPRRMIGTDA--FQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDI 255
Cdd:PRK09259 89 TALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 256 PKDI----------QQQLVVPNWNTQMKLPGylsrlPKSPEEAhleqiLRFISESKKPVLYVGGGCL--NSSEELRRFVE 323
Cdd:PRK09259 169 PAKVlaqtmdadeaLTSLVKVVDPAPAQLPA-----PEAVDRA-----LDLLKKAKRPLIILGKGAAyaQADEQIREFVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 324 LTGIPVASTLMGLGAYPGSDDLSlhmlgmhGTVYANYAVDKSDLLLAFGVRFDDRVT-GKVEAFASRAKIVHIDIDPAEI 402
Cdd:PRK09259 239 KTGIPFLPMSMAKGLLPDTHPQS-------AAAARSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIEPQEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 403 GKNKQPHLSICTDVKLALEAINRLIEDKQPKLKfdfSAWRKELHEQK----LKF---------PLSFKTFAEAIPPQYA- 468
Cdd:PRK09259 312 DSNRPIAAPVVGDIGSVMQALLAGLKQNTFKAP---AEWLDALAERKeknaAKMaeklstdtqPMNFYNALGAIRDVLKe 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 469 ---IQVLDE----LTDGNAIIstgvGQHQmwaaqwykykrPRQWLTSGGLGAMGFGLPAAIGASVA--RPdtlVVDIDGD 539
Cdd:PRK09259 389 npdIYLVNEgantLDLARNII----DMYK-----------PRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 540 GSFIMNVQELATVRVENLPIKILLLNNqhlgmvvqweDRFYKANRAhtylgNPRNESEIFPNML-------KFAEACDIP 612
Cdd:PRK09259 451 SAFGFSGMEVETICRYNLPVTVVIFNN----------GGIYRGDDV-----NLSGAGDPSPTVLvhharydKMMEAFGGV 515
|
570 580 590
....*....|....*....|....*....|.
gi 720058595 613 AARVTKKSELREAMKKMLETPGPYLLDVIVP 643
Cdd:PRK09259 516 GYNVTTPDELRHALTEAIASGKPTLINVVID 546
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
102-642 |
1.49e-33 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 135.47 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 102 DVLVEALEREGVTTVFAYPGGASLEIHQALtrSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGLA 181
Cdd:PRK07092 16 DATIDLLRRFGITTVFGNPGSTELPFLRDF--PDDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 182 DAMLDSVPLVAITGQVPRRMIGTDAF-QETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDiq 260
Cdd:PRK07092 94 TAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYD-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 261 qqlvvpNWN--TQMKLPGYLSRlPKSPEEAHLEQILRFISESKKPVLYVGGGC--LNSSEELRRFVELTGIPV-ASTLMG 335
Cdd:PRK07092 172 ------DWDqpAEPLPARTVSS-AVRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRLAERHRAPVwVAPMSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 336 LGAYPGSDDLSLHML-GMHGTVYAnyAVDKSDLLLAFGVR-FDDRVTGKVEAFASRAKIVHIDIDPAE-----IGKnkqp 408
Cdd:PRK07092 245 RCSFPEDHPLFAGFLpASREKISA--LLDGHDLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPGEaawapMGD---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 409 hlSICTDVKLALEAINRLIEDKQpklkfdfsawRKELHEQKLkfPLSFKTFAEAIPPQYAIQVLDELTDGNAII------ 482
Cdd:PRK07092 319 --AIVGDIRLALRDLLALLPPSA----------RPAPPARPM--PPPAPAPGEPLSVAFVLQTLAALRPADAIVveeaps 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 483 STGVGQHQMwaaqwyKYKRPRQWLT--SGGLgamGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIK 560
Cdd:PRK07092 385 TRPAMQEHL------PMRRQGSFYTmaSGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 561 ILLLNNQHLGmVVQWEDRFYKANRAH-TYLgnprneseifPNM--LKFAEACDIPAARVTKKSELREAMKKMLETPGPYL 637
Cdd:PRK07092 456 FVILNNGRYG-ALRWFAPVFGVRDVPgLDL----------PGLdfVALARGYGCEAVRVSDAAELADALARALAADGPVL 524
|
....*
gi 720058595 638 LDVIV 642
Cdd:PRK07092 525 VEVEV 529
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
102-257 |
2.14e-33 |
|
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: 125.15 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 102 DVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGlPGVCVATSGPGATNLVSGLA 181
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720058595 182 DAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGrPGPVLIDIPK 257
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
465-646 |
1.17e-32 |
|
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: 123.94 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 465 PQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIM 544
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 545 NVQELATVRVENLPIKILLLNNQHLGMVVQWEDRFYKANRAHTYlGNprneseifPNMLKFAEACDIPAARVTKKSELRE 624
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDF-GN--------PDFVKYAESFGAKGYRIESADDLLP 151
|
170 180
....*....|....*....|..
gi 720058595 625 AMKKMLETPGPYLLDVIVPHQE 646
Cdd:cd02010 152 VLERALAADGVHVIDCPVDYSE 173
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
463-642 |
3.23e-31 |
|
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: 120.01 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 463 IPPQYAIQVLDELTDGNAIIST-GVGQHQMWAAQWyKYKRPRQWLTSGGlGAMGFGLPAAIGASVARPDTLVVDIDGDGS 541
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDeAVTNGLPLRDQL-PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 542 FIMNVQELATVRVENLPIKILLLNNQ-----HLGMVVQWEDRFYKANRAHTYLGNPRneseifPNMLKFAEACDIPAARV 616
Cdd:cd02002 79 FMYTIQALWTAARYGLPVTVVILNNRgygalRSFLKRVGPEGPGENAPDGLDLLDPG------IDFAAIAKAFGVEAERV 152
|
170 180
....*....|....*....|....*.
gi 720058595 617 TKKSELREAMKKMLETPGPYLLDVIV 642
Cdd:cd02002 153 ETPEELDEALREALAEGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
465-642 |
2.08e-25 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 103.38 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 465 PQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIM 544
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 545 NVQELAT-VRvENLPIKILLLNNQHLGMVVQWEDRFYKANRAH-TYLGNPRNEseifpnmlKFAEACDIPAARVTKKSEL 622
Cdd:cd02004 81 SGMELETaVR-YNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVtTLLPDTRYD--------LVAEAFGGKGELVTTPEEL 151
|
170 180
....*....|....*....|
gi 720058595 623 REAMKKMLETPGPYLLDVIV 642
Cdd:cd02004 152 KPALKRALASGKPALINVII 171
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
100-642 |
3.06e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 103.80 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSG 179
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 180 LADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYLASSGRPGPVLIDIPKDI 259
Cdd:PRK12474 87 LHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPADV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 260 QqqlvvpnWNTQMKLPGYLSRLPKSPEEAH-LEQILRFISESKKPVLYVGGGCLNSSEelrrfVELTGIPVAST---LMG 335
Cdd:PRK12474 167 A-------WNEAAYAAQPLRGIGPAPVAAEtVERIAALLRNGKKSALLLRGSALRGAP-----LEAAGRIQAKTgvrLYC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 336 LGAYP----GSDDLSLHMLGMHGTVYANYAVDKSDLLLafgvrfddrVTGK--VEAFASRAKIVHIDIDPAEIGKNKQPH 409
Cdd:PRK12474 235 DTFAPrierGAGRVPIERIPYFHEQITAFLKDVEQLVL---------VGAKppVSFFAYPGKPSWGAPPGCEIVYLAQPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 410 lsicTDVKLALEAI-NRLIEDKQPKLKFDFSAwrKELHEQKLKFPLSFKTFAEAIPPQyAIqVLDEltdgnAIISTGVGQ 488
Cdd:PRK12474 306 ----EDLAQALQDLaDAVDAPAEPAARTPLAL--PALPKGALNSLGVAQLIAHRTPDQ-AI-YADE-----ALTSGLFFD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 489 HQmwaaqwYKYKRPRQWLTSGGlGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQH 568
Cdd:PRK12474 373 MS------YDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 569 LGMV------VQWEDRFYKANRAhTYLGNPrnesEIfpNMLKFAEACDIPAARVTKKSELREAMKKMLETPGPYLLDVIV 642
Cdd:PRK12474 446 YAILngelqrVGAQGAGRNALSM-LDLHNP----EL--NWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
100-642 |
8.09e-21 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 96.45 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 100 GADVLVEALEREGVTTVFAYPGGAslEIH--QALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLV 177
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTS--EMHfvAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 178 SGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRIVHEAFYlASSGRPGPVLIDI-P 256
Cdd:PRK07586 81 ANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVA-AARGAPGQVATLIlP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 257 KDIQqqlvvpnWN--TQMKLPGYLSRLPKSPEEAhLEQILRFISESKKPVLYVGGGCL--NSSEELRRFVELTGIPVAS- 331
Cdd:PRK07586 160 ADVA-------WSegGPPAPPPPAPAPAAVDPAA-VEAAAAALRSGEPTVLLLGGRALreRGLAAAARIAAATGARLLAe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 332 ---TLMGLGA---------YPGsdDLSLHMLgmhgtvyanyavDKSDLLLAFGVRfdDRVT-----GKVEAFASRAKIVH 394
Cdd:PRK07586 232 tfpARMERGAgrpaverlpYFA--EQALAQL------------AGVRHLVLVGAK--APVAffaypGKPSRLVPEGCEVH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 395 IDIDPAEigknkqphlsictDVKLALEAINRLI--EDKQPKLkfdfsawrkelhEQKLKFPLSfktfAEAIPPQYAIQVL 472
Cdd:PRK07586 296 TLAGPGE-------------DAAAALEALADALgaKPAAPPL------------AAPARPPLP----TGALTPEAIAQVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 473 DELTDGNAIIS-----TGVGQHQMWAAqwykyKRPRQWLTSGGlGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQ 547
Cdd:PRK07586 347 AALLPENAIVVdesitSGRGFFPATAG-----AAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQ 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 548 ELATVRVENLPIKILLLNN----------QHLGMVVQWEdrfyKANRAhTYLGNPRneseifPNMLKFAEACDIPAARVT 617
Cdd:PRK07586 421 ALWTQARENLDVTTVIFANrayailrgelARVGAGNPGP----RALDM-LDLDDPD------LDWVALAEGMGVPARRVT 489
|
570 580
....*....|....*....|....*
gi 720058595 618 KKSELREAMKKMLETPGPYLLDVIV 642
Cdd:PRK07586 490 TAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
470-631 |
1.40e-20 |
|
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: 90.26 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 470 QVLDELTDG---NAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNV 546
Cdd:cd02013 8 QVLRELEKAmpeDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 547 QELATVRVENLPIKILLLNNQHLGMVVQWEDRFYKANRAHTYLGNPRneseifpnMLKFAEACDIPAARVTKKSELREAM 626
Cdd:cd02013 88 MEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESES--------FAKIAEACGAKGITVDKPEDVGPAL 159
|
....*
gi 720058595 627 KKMLE 631
Cdd:cd02013 160 QKAIA 164
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
463-642 |
3.49e-19 |
|
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: 86.18 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 463 IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSF 542
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 543 IMNVQELATVRVENLPIKILLLNNQHLGMVVQWEDRF---YKANRAHTYLGNPrNESEIFPNMLKFAEACDIPAARVTKK 619
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFdmdYQVNLAFENINSS-ELGGYGVDHVKVAEGLGCKAIRVTKP 166
|
170 180
....*....|....*....|....*..
gi 720058595 620 SEL----REAMKKMLETPGPYLLDVIV 642
Cdd:cd02006 167 EELaaafEQAKKLMAEHRVPVVVEAIL 193
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
468-661 |
5.94e-17 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 80.04 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 468 AIQVLDELTDGNAIISTGVGQ-----HQMWAAqwykyKRPRQWLTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSF 542
Cdd:cd02003 4 VLGALNEAIGDDDVVINAAGSlpgdlHKLWRA-----RTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 543 IMNVQELATVRVENLPIKILLLNNQ------HLGMVVQwEDRFYKANRAHTYLGNPRNESEIFPNMLKFAEACDIPAARV 616
Cdd:cd02003 79 LMLHSEIVTAVQEGLKIIIVLFDNHgfgcinNLQESTG-SGSFGTEFRDRDQESGQLDGALLPVDFAANARSLGARVEKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 720058595 617 TKKSELREAMKKMLETPGPYLLDVivphqeHVLP--MIPSGGAFKDV 661
Cdd:cd02003 158 KTIEELKAALAKAKASDRTTVIVI------KTDPksMTPGYGSWWDV 198
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
103-256 |
6.23e-17 |
|
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: 78.69 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 103 VLVEALEREGVTTVFAYPGGAS------LEIHQALTRSSIIrnvlprHEQGGIFAAEGYARASGLPGVCVATSGPGATNL 176
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGSRSaplalaAAEHPEFRLHVRV------DERSAAFFALGLAKASGRPVAVVCTSGTAVANL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 177 VSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLV------LDVEDIPRIVHEAFYLASSGRPGP 250
Cdd:cd07037 76 LPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLpppeddDDLWYLLRLANRAVLEALSAPPGP 155
|
....*.
gi 720058595 251 VLIDIP 256
Cdd:cd07037 156 VHLNLP 161
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
512-643 |
1.53e-16 |
|
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: 77.96 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 512 GAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATVRVENLPIKILLLNNQhlGmvvqwedrfYKANRA-Htylg 590
Cdd:cd02005 50 GSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINND--G---------YTIERAiH---- 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 720058595 591 nPRNES--EIFP-NMLKFAEA----CDIPAARVTKKSELREAMKKMLETP-GPYLLDVIVP 643
Cdd:cd02005 115 -GPEASynDIANwNYTKLPEVfgggGGGLSFRVKTEGELDEALKDALFNRdKLSLIEVILP 174
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
102-206 |
2.70e-14 |
|
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: 70.99 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 102 DVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLpGVCVATSGPGATNLVSGLA 181
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGL-GALVTTYGVGELSALNGIA 79
|
90 100
....*....|....*....|....*
gi 720058595 182 DAMLDSVPLVAITGQVPRRMIGTDA 206
Cdd:cd07038 80 GAYAEHVPVVHIVGAPSTKAQASGL 104
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
81-566 |
1.53e-10 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 64.34 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 81 SPSSPSTFVPRFAADEPRKGADVLVEAlereGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASG 160
Cdd:PLN02573 3 SAPKPATPVSSSDATLGRHLARRLVEI----GVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 161 LpGVCVATSGPGATNLVSGLADAMLDSVPLVAITG----------QVPRRMIGTDAF-QEtpiVEVTRSITKHNYLVLDV 229
Cdd:PLN02573 79 V-GACVVTFTVGGLSVLNAIAGAYSENLPVICIVGgpnsndygtnRILHHTIGLPDFsQE---LRCFQTVTCYQAVINNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 230 EDipriVHEAFYLASS---GRPGPVLI-------DIPKDIQQQLVVPNWNTQmKLPGYLSRlpkspeEAHLEQILRFISE 299
Cdd:PLN02573 155 ED----AHELIDTAIStalKESKPVYIsvscnlaAIPHPTFSREPVPFFLTP-RLSNKMSL------EAAVEAAAEFLNK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 300 SKKPVLyVGGGCLNSSEELRRFVEL---TGIPVASTLMGLGAYPGSDDlslHMLGMH----GTVYANYAVDKSDLLLAFG 372
Cdd:PLN02573 224 AVKPVL-VGGPKLRVAKACKAFVELadaSGYPVAVMPSAKGLVPEHHP---HFIGTYwgavSTPFCAEIVESADAYLFAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 373 VRFDDRVTGKVEAFASRAKIVHIDIDPAEIGKNkqPHLSiCTDVKLALEAINRliedkqpKLKFDFSAWRK--------- 443
Cdd:PLN02573 300 PIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNG--PAFG-CVLMKDFLEALAK-------RVKKNTTAYENykrifvpeg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 444 ELHEQKLKFPLS----FKtfaeaippqyAIQvlDELTDGNAIIS-TGvgqhqmwaAQWY---KYKRPR--------QWlt 507
Cdd:PLN02573 370 EPLKSEPGEPLRvnvlFK----------HIQ--KMLSGDTAVIAeTG--------DSWFncqKLKLPEgcgyefqmQY-- 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 508 sgglGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELAT-VRVENLPIkILLLNN 566
Cdd:PLN02573 428 ----GSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTmIRCGQKSI-IFLINN 482
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
468-642 |
7.04e-10 |
|
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: 58.86 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 468 AIQ-VLDELTDGNAIIST-GVGQHQMWAAQ-WYKYKRPRQWLTSGGlgaMGFGLPAAIGASVARPDTLVVDIDGDGSFIM 544
Cdd:cd03371 4 AIEiVLSRAPATAAVVSTtGMTSRELFELRdRPGGGHAQDFLTVGS---MGHASQIALGIALARPDRKVVCIDGDGAALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 545 NVQELATV---RVENLpiKILLLNNqhlgmvvqwedrfykanRAHTYLGNPRNESEIFpNMLKFAEACDIPAAR-VTKKS 620
Cdd:cd03371 81 HMGGLATIgglAPANL--IHIVLNN-----------------GAHDSVGGQPTVSFDV-SLPAIAKACGYRAVYeVPSLE 140
|
170 180
....*....|....*....|..
gi 720058595 621 ELREAMKKMLETPGPYLLDVIV 642
Cdd:cd03371 141 ELVAALAKALAADGPAFIEVKV 162
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
475-559 |
1.72e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 55.22 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 475 LTDGNAIIStGVG--QHQMWAAQwykyKRPRQWLTsggLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMNVQELATV 552
Cdd:PRK06163 26 LKDEEAVIG-GIGntNFDLWAAG----QRPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTI 97
|
90
....*....|
gi 720058595 553 ---RVENLPI 559
Cdd:PRK06163 98 aalAPKNLTI 107
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
468-638 |
1.89e-07 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 50.95 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 468 AIQVLDELTDGNAIIST-GVGQHQMWAAQwykyKRPRQWLTsggLGAMGFGLPAAIGASVARPDTLVVdIDGDGSFIMNV 546
Cdd:cd02001 4 AIAEIIEASGDTPIVSTtGYASRELYDVQ----DRDGHFYM---LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 547 QELATVRVEN-LPIKILLLNNQhlgmvvqwedrfykanrAHTYLGNPRNESeIFPNMLKFAEACDIPAARVTKKSELREA 625
Cdd:cd02001 76 GVLLTAGEFTpLNLILVVLDNR-----------------AYGSTGGQPTPS-SNVNLEAWAAACGYLVLSAPLLGGLGSE 137
|
170
....*....|...
gi 720058595 626 MKKMLETPGPYLL 638
Cdd:cd02001 138 FAGLLATTGPTLL 150
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
468-658 |
3.53e-07 |
|
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: 50.75 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 468 AIQVL-DELTDGNAIISTGVGQHQMWAAQwykyKRPRQWLTsggLGAMGFGLPAAIGASVARPDTLVVdIDGDGSFIMNV 546
Cdd:cd03372 4 AIKTLiADLKDELVVSNIGFPSKELYAAG----DRPLNFYM---LGSMGLASSIGLGLALAQPRKVIV-IDGDGSLLMNL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 547 QELATVRVENLP-IKILLLNNQHLGMVvqwedrfykanrahtylGNPRNESEIFPNMLKFAEACDIPAAR-VTKKSELRE 624
Cdd:cd03372 76 GALATIAAEKPKnLIIVVLDNGAYGST-----------------GNQPTHAGKKTDLEAVAKACGLDNVAtVASEEAFEK 138
|
170 180 190
....*....|....*....|....*....|....*
gi 720058595 625 AMKKMLEtpGPYLLDVIV-PHQEHVlPMIPSGGAF 658
Cdd:cd03372 139 AVEQALD--GPSFIHVKIkPGNTDV-PNIPRDPVE 170
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
101-256 |
4.19e-05 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 47.16 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 101 ADVLVEALEREGVTTVFAYPGGASLEIHQALTRSSIIRNVLPRHEQGGIFAAEGYARASGLPGVCVATSGPGATNLVSGL 180
Cdd:PLN02980 304 ASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAV 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 181 ADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNY-LVLDVEDIP-RIV----HEAFYLASSGRPGPVLID 254
Cdd:PLN02980 384 VEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFnLPPPTDLIPaRMVlttlDSAVHWATSSPCGPVHIN 463
|
..
gi 720058595 255 IP 256
Cdd:PLN02980 464 CP 465
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
469-643 |
6.66e-05 |
|
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: 44.44 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 469 IQVLDEL--TDGNAIISTGVGQhqmwAAQWYKYkrprqwLTSGGL-GAMGFGLPAAIGASVARPDTLVVDI--DGDGSFI 543
Cdd:cd03375 15 AKALAELgiDPEKVVVVSGIGC----SSRLPYY------FNTYGFhTLHGRALAVATGVKLANPDLTVIVVsgDGDLAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 544 MNVQELATVRvENLPIKILLLNNQHLGM----VVQWEDRFYKAnrAHTYLGNPrnESEIFPnmLKFAEACDIP-AARVT- 617
Cdd:cd03375 85 GGNHFIHAAR-RNIDITVIVHNNQIYGLtkgqASPTTPEGFKT--KTTPYGNI--EEPFNP--LALALAAGATfVARGFs 157
|
170 180
....*....|....*....|....*..
gi 720058595 618 -KKSELREAMKKMLETPGPYLLDVIVP 643
Cdd:cd03375 158 gDIKQLKEIIKKAIQHKGFSFVEVLSP 184
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
471-646 |
2.22e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 42.65 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 471 VLDELTDGNAIISTGVGQHQMWAAQwykykrPRQwlTSGGLGAMGFGLPAAIGASVARPDTLVVDIDGDGSFIMN-VQEL 549
Cdd:cd02008 18 ALRKAFKKDSIVSGDIGCYTLGALP------PLN--AIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSgILGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 550 ATVRVENLPIKILLLNNQHLGMVVQwedrfykanRAHTYLGNPRNESEIFPNMLKFAEACDIPAARVTK---KSELREAM 626
Cdd:cd02008 90 INAVYNKANITVVILDNRTTAMTGG---------QPHPGTGKTLTEPTTVIDIEALVRAIGVKRVVVVDpydLKAIREEL 160
|
170 180
....*....|....*....|
gi 720058595 627 KKMLETPGPyllDVIVPHQE 646
Cdd:cd02008 161 KEALAVPGV---SVIIAKRP 177
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
521-643 |
2.46e-04 |
|
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: 42.20 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 521 AIGASVARPDTLVVdIDGDGSFI--MNVqeLATVRVENLPIKILLLNNQ-----HLGMVVQWEDRFYKanrahtYLGNPR 593
Cdd:cd02009 60 ALGIALATDKPTVL-LTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNgggifSLLPQASFEDEFER------LFGTPQ 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 720058595 594 NeseifpnmLKFAEAC---DIPAARVTKKSELREAMKKMLETPGPYLLDVIVP 643
Cdd:cd02009 131 G--------LDFEHLAkayGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
515-571 |
7.15e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 39.05 E-value: 7.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 720058595 515 GFGLPAAIGASVARPDTLVVDI--DGDGSFI-MNvQELATVRvENLPIKILLLNNQHLGM 571
Cdd:PRK11867 72 GRALAIATGLKLANPDLTVIVVtgDGDALAIgGN-HFIHALR-RNIDITYILFNNQIYGL 129
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