|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-588 |
0e+00 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 1044.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDV-SAYVETVVSPAQLLHVLDRALRVAVGERQVATVI 159
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQQMAAPKrQPHEHGHVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVAK 239
Cdd:PRK08273 161 LPNDVQELEYEP-PPHAHGTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 240 ALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKAGQARAVQIDLYPRNIGIRYPIDQALLG 319
Cdd:PRK08273 240 ALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKEGQARGVQIDIDGRMLGLRYPMEVNLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 320 DAGETLERLLPLLEQKKHGAWRRRVERAVTASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARD 399
Cdd:PRK08273 320 DAAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 400 IRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNAELVTVQQYWQRWDSPTFIVLVLNNGDLN 479
Cdd:PRK08273 400 LRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMAELITVAKYWRQWSDPRLIVLVLNNRDLN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 480 QVTWEQRALAGDPEFSPAQEVIDFPYARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNVPPLPPHISFE 559
Cdd:PRK08273 480 QVTWEQRVMEGDPKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITLE 559
|
570 580
....*....|....*....|....*....
gi 15597304 560 QAKHLLGAMLQDDPKRWGVIRQSARQVLA 588
Cdd:PRK08273 560 QAKAFASALLKGDPDAGGVIVQTAKQVLQ 588
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-557 |
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: 532.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEaFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSG-IRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQQMAAPKRQPHehghvmSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGV 237
Cdd:COG0028 160 IPKDVQAAEAEEEPAP------PELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARraGAAEELRALAERLGAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 238 AKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPKagqARAVQIDLYPRNIGIRY 311
Cdd:COG0028 234 VTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDdrvtgnWDEFAPD---AKIIHIDIDPAEIGKNY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 312 PIDQALLGDAGETLERLLPLLEQKK--HGAWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDS 389
Cdd:COG0028 311 PVDLPIVGDAKAVLAALLEALEPRAddRAAWLARIAAW----RAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGnAELVTVQQYwqrwDSPtFI 469
Cdd:COG0028 387 GQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNL-QELATAVRY----GLP-VK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 470 VLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNV 549
Cdd:COG0028 461 VVVLNNGGLGMVRQWQELFYGGRYSGTDLPNPDF--AKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEE 538
|
....*...
gi 15597304 550 PPLPPHIS 557
Cdd:COG0028 539 NPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-587 |
1.07e-166 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 486.82 E-value: 1.07e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIV 160
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDV--QQMaapKRQPHEhghvmSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVA 238
Cdd:PRK08611 162 PDDLpaQKI---KDTTNK-----TVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKagQARAVQIDLYPRNIGIRYPIDQALL 318
Cdd:PRK08611 234 HTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPK--KAKAIQIDTDPANIGKRYPVNVGLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 319 GDAGETLERLLPLLEQKKHgawrRRVERAVTASREEARRQAEE----PADPINPQRVFRSLSEQLPDDAILCGDSGSHTN 394
Cdd:PRK08611 312 GDAKKALHQLTENIKHVED----RRFLEACQENMAKWWKWMEEdennASTPIKPERVMAAIQKIADDDAVLSVDVGTVTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 395 WYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPtFIVLVLN 474
Cdd:PRK08611 388 WSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQ-DFVTAVKY----KLP-IVVVVLN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 475 NGDLNQVTWEQRAlAGDPEFspaqeVIDFP---YARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNVPP 551
Cdd:PRK08611 462 NQQLAFIKYEQQA-AGELEY-----AIDLSdmdYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAP 535
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 15597304 552 LPPHISFEQA----KHLLGAMLQDdpKRWGVI---RQSARQVL 587
Cdd:PRK08611 536 LPGKIVNDEAlgysKWAIKSLFED--KKLDQMpplKKALKRFL 576
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-562 |
4.68e-143 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 426.33 E-value: 4.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSL-RRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIV 160
Cdd:PRK09124 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVQQMAAPKRQPhehghvmsAVGFVQPRPYAR--DADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVA 238
Cdd:PRK09124 160 PGDVALKPAPERAT--------PHWYHAPQPVVTpaEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKagQARAVQIDLYPRNIGIRYPIDQALL 318
Cdd:PRK09124 232 HALRGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPT--DAKIIQIDINPGSLGRRSPVDLGLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 319 GDAGETLERLLPLLEQKKHgawRRRVERAVTASReEARR------QAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSH 392
Cdd:PRK09124 310 GDVKATLAALLPLLEEKTD---RKFLDKALEHYR-KARKglddlaVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 393 TNWYARDIRM--RPGMLGSLSGklATMGSGVPYAIAAKLAYPQRPVVAMVGDG--AMQMngnAELVTVQQYwqrwDSPTF 468
Cdd:PRK09124 386 TVWAARYLKMngKRRLLGSFNH--GSMANAMPQALGAQAAHPGRQVVALSGDGgfSMLM---GDFLSLVQL----KLPVK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 469 IVlVLNNGDLNQVTWEQRAlAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPN 548
Cdd:PRK09124 457 IV-VFNNSVLGFVAMEMKA-GGYLTDGTDLHNPDF--AAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQ 532
|
570
....*....|....
gi 15597304 549 VPPLPPHISFEQAK 562
Cdd:PRK09124 533 ELAMPPQIKLEQAK 546
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-568 |
8.40e-125 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 379.33 E-value: 8.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAV-RRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIV 160
Cdd:PRK06546 80 HLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVQQMAAPKrqphehGHVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVAKA 240
Cdd:PRK06546 160 PGDIADEPAPE------GFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 241 LLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPkagQARAVQIDLYPRNIGIRYPIDQALLGD 320
Cdd:PRK06546 234 LRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP---DVRTAQVDIDPEHLGRRTRVDLAVHGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 321 AGETLERLLPLLEQK-----------KHgawRRRVERAVTASREEARRQAeepadPINPQRVFRSLSEQLPDDAILCGDS 389
Cdd:PRK06546 311 VAETIRALLPLVKEKtdrrfldrmlkKH---ARKLEKVVGAYTRKVEKHT-----PIHPEYVASILDELAADDAVFTVDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTNWYARDI----RMRpgMLGSLSGklATMGSGVPYAIAAKLAYPQRPVVAMVGDG--AMQMngnAELVTVQQYwqrw 463
Cdd:PRK06546 383 GMCNVWAARYItpngRRR--VIGSFRH--GSMANALPHAIGAQLADPGRQVISMSGDGglSMLL---GELLTVKLY---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 464 DSPTFIVlVLNNGDLNQVTWEQrALAGDPEFSPAQEVIDfpYARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEV 543
Cdd:PRK06546 452 DLPVKVV-VFNNSTLGMVKLEM-LVDGLPDFGTDHPPVD--YAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDV 527
|
570 580
....*....|....*....|....*
gi 15597304 544 VTDPNVPPLPPHISFEQAKHLLGAM 568
Cdd:PRK06546 528 VTDPNALSIPPTITGEQVKGFALAA 552
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-571 |
1.20e-124 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 378.02 E-value: 1.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI--RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIVPND 163
Cdd:PRK06457 81 NGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 164 VQQMAAPKRqPHEHGHVMSavgfvqprpYARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVAKALLG 243
Cdd:PRK06457 161 ILRKSSEYK-GSKNTEVGK---------VKYSIDFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 244 KAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKagQARAVQIDLYPRNIGIRYPIDQALLGDAGE 323
Cdd:PRK06457 231 KGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNK--SAKVIQVDIDNSNIGKRLDVDLSYPIPVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 324 tlerLLPLLEQKKHGAWRRRVERAVTASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMR 403
Cdd:PRK06457 309 ----FLNIDIEEKSDKFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRAS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 404 PGMLGSLSGKLATMGSGVPYAIAAKLAY-PQRPVVAMVGDGAMQMNgNAELVTVQQYwqrwDSPTFIVlVLNNGDLNQVT 482
Cdd:PRK06457 385 GEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMT-MMELITAKKY----DLPVKII-IYNNSKLGMIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 483 WEQRALaGDPEFspAQEVIDFPYARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNVPPLPPHISFEQAK 562
Cdd:PRK06457 459 FEQEVM-GYPEW--GVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAG 535
|
....*....
gi 15597304 563 HLLGAMLQD 571
Cdd:PRK06457 536 EYVLSIFRE 544
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-563 |
3.92e-107 |
|
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: 333.73 E-value: 3.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:TIGR02720 2 SAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIVPNDVQ 165
Cdd:TIGR02720 82 LYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 166 QMAAPKRqpHEHGHVMSAVGFVQPRPyaRDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVAKALLGKA 245
Cdd:TIGR02720 162 WQEIPDN--DYYASSVSYQTPLLPAP--DVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 246 AVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKAGQAR-AVQIDLYPRNIGIRYPIDQALLGDAGET 324
Cdd:TIGR02720 238 IIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAFKNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 325 LERLLPLLEQKKHGAWRRRVERAVTASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMRP 404
Cdd:TIGR02720 318 LAAILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 405 GMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNgNAELVTVQQYwqrwDSPTfIVLVLNNGDLNQVTWE 484
Cdd:TIGR02720 398 KNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMT-MQDLLTQVQY----HLPV-INIVFSNCTYGFIKDE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 485 QRalaGDPEFSPAQEVIDFPYARYADMLGFKGIRVDRPEDIDAA--WAEAFAADRPVLLEVVTDPNVPPLPPHISFEQAK 562
Cdd:TIGR02720 472 QE---DTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVfeQAKAIKQGKPVLIDAKITGDRPLPVEKLRLDPAL 548
|
.
gi 15597304 563 H 563
Cdd:TIGR02720 549 S 549
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-167 |
1.88e-95 |
|
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: 288.68 E-value: 1.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDAL-RREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIVPND 163
Cdd:cd07039 80 NGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGD 159
|
....
gi 15597304 164 VQQM 167
Cdd:cd07039 160 VQDA 163
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
6-553 |
5.37e-94 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 298.95 E-value: 5.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEaFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:TIGR00118 4 AEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSG-IEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 QQMAAPKRQPHEhghvMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKALL 242
Cdd:TIGR00118 163 TTAEIEYPYPEK----VNLPGY-RPTVKGHPLQIKKAAELINLAKKPVILVGGGVIiaGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 243 GKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPKagqARAVQIDLYPRNIGIRYPIDQA 316
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDdrvtgnLAKFAPN---AKIIHIDIDPAEIGKNVRVDIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLEQKKH---GAWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHT 393
Cdd:TIGR00118 315 IVGDARNVLEELLKKLFELKErkeSAWLEQINKW----KKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 394 NWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPTfIVLVL 473
Cdd:TIGR00118 391 MWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQ-ELSTAVQY----DIPV-KILIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 474 NNGDLNQVT-WEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNVPPL 552
Cdd:TIGR00118 465 NNRYLGMVRqWQELFYEERYSHTHMGSLPDF--VKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVL 542
|
.
gi 15597304 553 P 553
Cdd:TIGR00118 543 P 543
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
6-554 |
5.56e-80 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 263.15 E-value: 5.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDAL--YDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK06276 82 IATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 QQMAAPKrqphEHGHVMSAVGFVQPRPYARDADLE--AAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKA 240
Cdd:PRK06276 162 QEGELDL----EKYPIPAKIDLPGYKPTTFGHPLQikKAAELIAEAERPVILAGGGVIisGASEELIELSELVKIPVCTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 241 LLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPkagQARAVQIDLYPRNIGIRYPID 314
Cdd:PRK06276 238 LMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSdrttgdISSFAP---NAKIIHIDIDPAEIGKNVRVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 315 QALLGDAGETLERLLPLLEQKKHGAWRRRVERaVTASREEARRQAEEPADPINPQRVFRSLSEQLPD-----DAILCGDS 389
Cdd:PRK06276 315 VPIVGDAKNVLRDLLAELMKKEIKNKSEWLER-VKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTNWYAR--DIRMRPGMLGslSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPT 467
Cdd:PRK06276 394 GQNQMWMAHffKTSAPRSFIS--SGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQ-ELATIAEY----DIPV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 468 FIVlVLNNGDLNQVTWEQRaLAGDPEFSPAQ--EVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVT 545
Cdd:PRK06276 467 VIC-IFDNRTLGMVYQWQN-LYYGKRQSEVHlgETPDF--VKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIII 542
|
570
....*....|.
gi 15597304 546 DPN--VPPLPP 554
Cdd:PRK06276 543 DPAeaLPMVPP 553
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
365-551 |
3.15e-79 |
|
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: 247.44 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 365 PINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGA 444
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 445 MQMNgNAELVTVQQYwqrwdSPTFIVLVLNNGDLNQVTWEQRAlAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPED 524
Cdd:cd02014 81 FAML-MGDLITAVKY-----NLPVIVVVFNNSDLGFIKWEQEV-MGQPEFGVDLPNPDF--AKIAEAMGIKGIRVEDPDE 151
|
170 180
....*....|....*....|....*..
gi 15597304 525 IDAAWAEAFAADRPVLLEVVTDPNVPP 551
Cdd:cd02014 152 LEAALDEALAADGPVVIDVVTDPNEPP 178
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-561 |
6.18e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 253.05 E-value: 6.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEA---FDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGP 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDEL-YKAEAegwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 78 GAIHLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVAT 157
Cdd:PRK07418 96 GATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 158 VI-VPNDVQQMAApKRQPHEHGHVMSAvGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLA 234
Cdd:PRK07418 176 LIdIPKDVGQEEF-DYVPVEPGSVKPP-GY-RPTVKGNPRQINAALKLIEEAERPLLYVGGGAIsaGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 235 AGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPKagqARAVQIDLYPRNIG 308
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFddrvtgKLDEFASR---AKVIHIDIDPAEVG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 309 IRYPIDQALLGDAGETLERLLPLLEQKKH----GAWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPdDAI 384
Cdd:PRK07418 330 KNRRPDVPIVGDVRKVLVKLLERSLEPTTpprtQAWLERINRW----KQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 385 LCGDSGSHTNWYARDIRMRPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwD 464
Cdd:PRK07418 405 YTTDVGQHQMWAAQFLRNGPRRWIS-SAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQ-ELGTLAQY----G 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 465 SPTFIVLVlNNGDLNQV-TWEQ----------RALAGDPEFSpaqevidfpyaRYADMLGFKGIRVDRPEDIDAAWAEAF 533
Cdd:PRK07418 479 INVKTVII-NNGWQGMVrQWQEsfygerysasNMEPGMPDFV-----------KLAEAFGVKGMVISERDQLKDAIAEAL 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 15597304 534 AADRPVLLEV-VTD-----PNVPP---------LPPHISFEQA 561
Cdd:PRK07418 547 AHDGPVLIDVhVRRdencyPMVPPgksnaqmvgLPEHPELALA 589
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
4-525 |
2.39e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 249.74 E-value: 2.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEAL--RDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQaatALGSDYQ---QEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQK---PIKRSKQgsfQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQQMAAPKrQPHEHGHVmsavgfvqPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGV 237
Cdd:PRK08322 157 LPEDIAAEETDG-KPLPRSYS--------RRPYASPKAIERAAEAIQAAKNPLILIGAGANrkTASKALTEFVDKTGIPF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 238 AKALLGKAAVSDDLPYVTGSIGL----LGTRAssmlMEHCDTLLIVGstfpYS--EFLPK----AGQARAVQIDLYPRNI 307
Cdd:PRK08322 228 FTTQMGKGVIPETHPLSLGTAGLsqgdYVHCA----IEHADLIINVG----HDviEKPPFfmnpNGDKKVIHINFLPAEV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 308 GIRYPIDQALLGDAGETLERLLPLLEqKKHGAWRRRVERAVTASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCG 387
Cdd:PRK08322 300 DPVYFPQVEVVGDIANSLWQLKERLA-DQPHWDFPRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVIL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 388 DSGSHTNWYARDIRM-RPGMLgSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNgNAELVTVqqywQRWDSP 466
Cdd:PRK08322 379 DNGAYKIWFARNYRAyEPNTC-LLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMN-SQELETA----VRLGLP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597304 467 tFIVLVLNNGDLNQVTWEQRALAGDPEFspaqevIDF--P-YARYADMLGFKGIRVDRPEDI 525
Cdd:PRK08322 453 -LVVLILNDNAYGMIRWKQENMGFEDFG------LDFgnPdFVKYAESYGAKGYRVESADDL 507
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
4-554 |
5.56e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 249.31 E-value: 5.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrraeaFD----YIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGA 79
Cdd:PRK06048 9 TGARAIIKCLEKEGVEVIFGYPGGAIIPVYDEL------YDsdlrHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 80 IHLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI 159
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 -VPNDVQQ----------MAAPKRQPHEHGHvmsavgfvqPRPYARdadleaAAAILNRGRRVAILAGAGALG--AHRQL 226
Cdd:PRK06048 163 dLPKDVTTaeidfdypdkVELRGYKPTYKGN---------PQQIKR------AAELIMKAERPIIYAGGGVISsnASEEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 227 EAVAERLAAGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPKagqARAVQI 300
Cdd:PRK06048 228 VELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFddrvtgKLASFAPN---AKIIHI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 301 DLYPRNIGIRYPIDQALLGDAGETLERLLPLLEQKKHGAWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLP 380
Cdd:PRK06048 305 DIDPAEISKNVKVDVPIVGDAKQVLKSLIKYVQYCDRKEWLDKINQW----KKEYPLKYKEREDVIKPQYVIEQIYELCP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 381 dDAILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYw 460
Cdd:PRK06048 381 -DAIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQ-ELATAVQN- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 461 qrwDSPTfIVLVLNNGDLNQV-TWEQraLAGDPEFSPA--QEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADR 537
Cdd:PRK06048 458 ---DIPV-IVAILNNGYLGMVrQWQE--LFYDKRYSHTciKGSVDF--VKLAEAYGALGLRVEKPSEVRPAIEEAVASDR 529
|
570
....*....|....*....
gi 15597304 538 PVLLEVVTD--PNVPPLPP 554
Cdd:PRK06048 530 PVVIDFIVEceENVSPMVP 548
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-554 |
5.82e-68 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 230.15 E-value: 5.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrraeaFD----YIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIH 81
Cdd:PRK08978 4 AQWVVHALRAQGVDTVFGYPGGAIMPVYDAL------YDggveHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 82 LLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-V 160
Cdd:PRK08978 78 LITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVdI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVqQMAAPKRQPhehgHVMSavgfVQPRPYARDADLEAAAAILNRGRRvAILAGAGALGAHRQLEAVAERLAA----G 236
Cdd:PRK08978 158 PKDI-QLAEGELEP----HLTT----VENEPAFPAAELEQARALLAQAKK-PVLYVGGGVGMAGAVPALREFLAAtgmpA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 237 VAkALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPKagqARAVQIDLYPRNIGIR 310
Cdd:PRK08978 228 VA-TLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFddrvtgKLNTFAPH---AKVIHLDIDPAEINKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 311 YPIDQALLGDagetLERLLPLLEQKKH-GAWRRRVEravtASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDS 389
Cdd:PRK08978 304 RQAHVALQGD----LNALLPALQQPLNiDAWRQHCA----QLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTNWYARDIRM-RPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVqqywQRWDSPTF 468
Cdd:PRK08978 376 GQHQMWVAQHMRFtRPENFIT-SSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQ-ELGTI----KRKQLPVK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 469 IVLvLNNGDLNQV-TWEQraLAGDPEFSpaqEVI--DFP-YARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVV 544
Cdd:PRK08978 450 IVL-LDNQRLGMVrQWQQ--LFFDERYS---ETDlsDNPdFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVS 523
|
570
....*....|...
gi 15597304 545 TDP--NVPPL-PP 554
Cdd:PRK08978 524 IDEleNVWPLvPP 536
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-552 |
3.02e-66 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 226.50 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEA--FDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPG 78
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKKglIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 79 AIHLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATV 158
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 159 I-VPNDVqQMAAPKRQPHEHGHVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAA 235
Cdd:CHL00099 168 IdIPKDV-GLEKFDYYPPEPGNTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIisDAHQEITELAELYKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 236 GVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFlpkAGQARAVQIDLYPRNIGI 309
Cdd:CHL00099 247 PVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFddrvtgKLDEF---ACNAQVIHIDIDPAEIGK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 310 RYPIDQALLGDAGETLERLLPLLEQKKHG-------AWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPdD 382
Cdd:CHL00099 324 NRIPQVAIVGDVKKVLQELLELLKNSPNLleseqtqAWRERINRW----RKEYPLLIPKPSTSLSPQEVINEISQLAP-D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 383 AILCGDSGSHTNWYARDIRMRPGMLGSLSGkLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqr 462
Cdd:CHL00099 399 AYFTTDVGQHQMWAAQFLKCKPRKWLSSAG-LGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQ-ELGTIAQY--- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 463 wDSPTFIVLvLNN---GDLNQvtWEQ----------RALAGDPEFspaqevidfpyARYADMLGFKGIRVDRPEDIDAAW 529
Cdd:CHL00099 474 -NLPIKIII-INNkwqGMVRQ--WQQafygeryshsNMEEGAPDF-----------VKLAEAYGIKGLRIKSRKDLKSSL 538
|
570 580
....*....|....*....|....*
gi 15597304 530 AEAFAADRPVLLE--VVTDPNVPPL 552
Cdd:CHL00099 539 KEALDYDGPVLIDcqVIEDENCYPM 563
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-551 |
3.79e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 223.05 E-value: 3.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRrAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQ-STQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:PRK08155 90 NLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWId 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQ-QMAAPKRQPhehghvmsAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAG 236
Cdd:PRK08155 170 IPKDVQtAVIELEALP--------APAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVInsGAPARARELAEKAQLP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 237 VAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPkagQARAVQIDLYPRNIG-I 309
Cdd:PRK08155 242 TTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFddraigKTEQFCP---NAKIIHVDIDRAELGkI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 310 RYPiDQALLGDAGETLERLLPLLEQKKHGAWRRRVeravtasreeARRQAEEP------ADPINPQRVFRSLSEQLPDDA 383
Cdd:PRK08155 319 KQP-HVAIQADVDDVLAQLLPLVEAQPRAEWHQLV----------ADLQREFPcpipkaDDPLSHYGLINAVAACVDDNA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 384 ILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQywQRW 463
Cdd:PRK08155 388 IITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQ-EMATAAE--NQL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 464 DSPtfIVLvLNNGDLNQVT------WEQRALAGDPEFSPaqeviDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADR 537
Cdd:PRK08155 465 DVK--IIL-MNNEALGLVHqqqslfYGQRVFAATYPGKI-----NF--MQIAAGFGLETCDLNNEADPQAALQEAINRPG 534
|
570 580
....*....|....*....|
gi 15597304 538 PVLLEVVTD------PNVPP 551
Cdd:PRK08155 535 PALIHVRIDaeekvyPMVPP 554
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-548 |
1.07e-64 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 221.67 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDAL-HDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDV--QQMAAPKRQPHEhghvmsavgfvQPRPYARDADLEAAAAILNRGRR-VAILAGAG-ALGAHRQLEAVAERLAA 235
Cdd:PRK08199 165 LPEDVlsETAEVPDAPPYR-----------RVAAAPGAADLARLAELLARAERpLVILGGSGwTEAAVADLRAFAERWGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 236 GVAKALLGKAAVSDDLP-YVtgsiGLLGTRASSMLMEH---CDTLLIVGS------TFPYSEFLPKAGQARAVQIDLYPR 305
Cdd:PRK08199 234 PVACAFRRQDLFDNRHPnYA----GDLGLGINPALAARireADLVLAVGTrlgevtTQGYTLLDIPVPRQTLVHVHPDAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 306 NIGIRYPIDQALLGDAGETLERLLPlLEQKKHGAWRRRVERAVTASREEARRQAEEPadPINPQRVFRSLSEQLPDDAIL 385
Cdd:PRK08199 310 ELGRVYRPDLAIVADPAAFAAALAA-LEPPASPAWAEWTAAAHADYLAWSAPLPGPG--AVQLGEVMAWLRERLPADAII 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 386 CGDSGSHTNWYARDIRMR--PGMLGSLSGklaTMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrw 463
Cdd:PRK08199 387 TNGAGNYATWLHRFFRFRryRTQLAPTSG---SMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQ-ELATAVQY---- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 464 DSPtFIVLVLNNGDLNQVTWEQ------RALAGD---PEFspaqevidfpyARYADMLGFKGIRVDRPEDIDAAWAEAFA 534
Cdd:PRK08199 459 GLP-IIVIVVNNGMYGTIRMHQereypgRVSGTDltnPDF-----------AALARAYGGHGETVERTEDFAPAFERALA 526
|
570
....*....|....
gi 15597304 535 ADRPVLLEVVTDPN 548
Cdd:PRK08199 527 SGKPALIEIRIDPE 540
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-554 |
5.64e-62 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 214.58 E-value: 5.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAI 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQ-NYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 81 HLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:PRK08527 80 NAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHId 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDV----------QQMAAPKRQPHEHGHvmsavgfvqPRpyardaDLEAAAAILNRGRRVAILAGAGAL--GAHRQLE 227
Cdd:PRK08527 160 IPKDVtatlgefeypKEISLKTYKPTYKGN---------SR------QIKKAAEAIKEAKKPLFYLGGGAIlsNASEEIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 228 AVAERLAAGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFlpkAGQARAVQID 301
Cdd:PRK08527 225 ELVKKTGIPAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFddrvtgKLSEF---AKHAKIIHVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 302 LYPRNIGIRYPIDQALLGDAGETLERLLPLLEQ---KKHGAWRRRVERavtaSREEARRQAEEPADPINPQRVFRSLSEQ 378
Cdd:PRK08527 302 IDPSSISKIVNADYPIVGDLKNVLKEMLEELKEenpTTYKEWREILKR----YNELHPLSYEDSDEVLKPQWVIERVGEL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 379 LPDDAILCGDSGSHTNWYARDIRM-RPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQ 457
Cdd:PRK08527 378 LGDDAIISTDVGQHQMWVAQFYPFnYPRQLAT-SGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQ-ELMTAV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 458 QYwqrwDSPtFIVLVLNNGDLNQV-TW-----EQRALAGDPEFSPaqeviDFpyARYADMLGFKGIRVDRPEDIDAAWAE 531
Cdd:PRK08527 456 EY----KIP-VINIILNNNFLGMVrQWqtffyEERYSETDLSTQP-----DF--VKLAESFGGIGFRVTTKEEFDKALKE 523
|
570 580
....*....|....*....|....*
gi 15597304 532 AFAADRPVLLEVVTD--PNVPPLPP 554
Cdd:PRK08527 524 ALESDKVALIDVKIDrfENVLPMVP 548
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-552 |
2.17e-61 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 213.51 E-value: 2.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQ-DKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVdIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 QQMAAPKRQPHEhghvmsavgfVQPRPY-----ARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGV 237
Cdd:PRK06965 183 SKTPCEYEYPKS----------VEMRSYnpvtkGHSGQIRKAVSLLLSAKRPYIYTGGGVIlaNASRELRQLADLLGYPV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 238 AKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEF-LPK--AGQARA-VQIDLYPRNIGIRYPI 313
Cdd:PRK06965 253 TNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIgNPAhfASRPRKiIHIDIDPSSISKRVKV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 314 DQALLGDAGETLERLLPLLEQKKH-------GAWRRRVEravtASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILC 386
Cdd:PRK06965 333 DIPIVGDVKEVLKELIEQLQTAEHgpdadalAQWWKQIE----GWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVC 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 387 GDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSP 466
Cdd:PRK06965 409 SDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQ-ELSTCLQY----DTP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 467 TFIVlVLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDID-AAWAEAFAADRPVLLEVV 544
Cdd:PRK06965 484 VKII-SLNNRYLGMVrQWQEIEYSKRYSHSYMDALPDF--VKLAEAYGHVGMRIEKTSDVEpALREALRLKDRTVFLDFQ 560
|
570
....*....|
gi 15597304 545 TDP--NVPPL 552
Cdd:PRK06965 561 TDPteNVWPM 570
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-544 |
1.06e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 208.52 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 2 SSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIH 81
Cdd:PRK07282 9 PKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAI-YNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 82 LLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-V 160
Cdd:PRK07282 88 AITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVQQmaapKRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGA--LGAHRQLEAVAERLAAGVA 238
Cdd:PRK07282 168 PKDVSA----LETDFIYDPEVNLPSY-QPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFpySEFL---PK--AGQARAVQIDLYPRNIGIRYPI 313
Cdd:PRK07282 243 TTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRF--DDRLtgnPKtfAKNAKVAHIDIDPAEIGKIIKT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 314 DQALLGDAGETLERLLPllEQKKHGAWRRRVERaVTASREEArRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHT 393
Cdd:PRK07282 321 DIPVVGDAKKALQMLLA--EPTVHNNTEKWIEK-VTKDKNRV-RSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 394 NWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNgNAELVTVQQYwqrwDSPTFIVLvL 473
Cdd:PRK07282 397 MWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMT-NQELAILNIY----KVPIKVVM-L 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597304 474 NNGDLNQVTWEQRALAgdpEFSPAQEVID-FP-YARYADMLGFKGIRVDRPEDIDaAWAEAFAADRPVLLEVV 544
Cdd:PRK07282 471 NNHSLGMVRQWQESFY---EGRTSESVFDtLPdFQLMAQAYGIKHYKFDNPETLA-QDLEVITEDVPMLIEVD 539
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-551 |
1.15e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 208.28 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDAL--YESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPN 162
Cdd:PRK06725 94 TGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIdIPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 163 DVQQmaapKRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKA 240
Cdd:PRK06725 174 DVQN----EKVTSFYNEVVEIPGY-KPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIhsGGSEELIEFARENRIPVVST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 241 LLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPkagQARAVQIDLYPRNIGIRYPID 314
Cdd:PRK06725 249 LMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFddrvtgKLELFSP---HSKKVHIDIDPSEFHKNVAVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 315 QALLGDAGETLERLLPLLEQKKHGAWRRRVEravtASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTN 394
Cdd:PRK06725 326 YPVVGDVKKALHMLLHMSIHTQTDEWLQKVK----TWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 395 WYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPTfIVLVLN 474
Cdd:PRK06725 402 WAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQ-ELQTIAEN----NIPV-KVFIIN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 475 NGDLNQV-TWEQ----RALA----GDPEFspaqevidfpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVT 545
Cdd:PRK06725 476 NKFLGMVrQWQEmfyeNRLSeskiGSPDF-----------VKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCV 544
|
570
....*....|..
gi 15597304 546 D------PNVPP 551
Cdd:PRK06725 545 EegenvfPMVPP 556
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-525 |
1.85e-59 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 208.31 E-value: 1.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGdgiNGIMGAMGRRAEA-FDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGA 79
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIG---SAFMDASDLFPPAgIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 80 IHLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI 159
Cdd:PRK07525 81 TNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPND--VQQMAAPKRQPHEHghvmsavgfvqPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAA 235
Cdd:PRK07525 161 IPRDyfYGVIDVEIPQPVRL-----------ERGAGGEQSLAEAAELLSEAKFPVILSGAGVVlsDAIEECKALAERLDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 236 GVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEFLPKAG------QARAVQIDLYPRNIGI 309
Cdd:PRK07525 230 PVACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGTLPQYGidywpkDAKIIQVDINPDRIGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 310 RYPIDQALLGDAGETLERLLPLLEQKKHGAwRRRVERAVTASREEAR---------------------RQAEEPADPINP 368
Cdd:PRK07525 310 TKKVSVGICGDAKAVARELLARLAERLAGD-AGREERKALIAAEKSAweqelsswdhedddpgtdwneEARARKPDYMHP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 369 QRVFRSLSEQLPDDAILCGDSG---SHTNWYARDIRMR----PGMLGSlsgklatMGSGVPYAIAAKLAYPQRPVVAMVG 441
Cdd:PRK07525 389 RQALREIQKALPEDAIVSTDIGnncSIANSYLRFEKGRkylaPGSFGN-------CGYAFPAIIGAKIACPDRPVVGFAG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 442 DGA--MQMNgnaELVTVQQYwqrwDSPTfIVLVLNNGDL-----NQVTWEQRALAG---DPEFSpaqevidfpYARYADM 511
Cdd:PRK07525 462 DGAwgISMN---EVMTAVRH----NWPV-TAVVFRNYQWgaekkNQVDFYNNRFVGtelDNNVS---------YAGIAEA 524
|
570
....*....|....
gi 15597304 512 LGFKGIRVDRPEDI 525
Cdd:PRK07525 525 MGAEGVVVDTQEEL 538
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-544 |
1.09e-58 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 206.76 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGI----NGIMGAMGRRaeafdYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGA 79
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAIlpvyDPLFDSTKVR-----HVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 80 IHLLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI 159
Cdd:PRK07789 107 TNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 -VPNDVQQMAAPKRQPHEhghvMSAVGFvQP--RPYARdaDLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLA 234
Cdd:PRK07789 187 dIPKDALQAQTTFSWPPR----MDLPGY-RPvtKPHGK--QIREAAKLIAAARRPVLYVGGGVIraEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 235 AGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFLPKagqARAVQIDLYPRNIG 308
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFddrvtgKLDSFAPD---AKVIHADIDPAEIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 309 -IRYPiDQALLGDAGETLERLLPLL--EQKKHG-----AWRRRVERAvtasREEARRQAEEPAD-PINPQRVFRSLSEQL 379
Cdd:PRK07789 337 kNRHA-DVPIVGDVKEVIAELIAALraEHAAGGkpdltAWWAYLDGW----RETYPLGYDEPSDgSLAPQYVIERLGEIA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 380 PDDAILCGDSGSHTNWYARDIRM-RPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNgNAELVTvqq 458
Cdd:PRK07789 412 GPDAIYVAGVGQHQMWAAQFIDYeKPRTWLN-SGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMT-NQELAT--- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 459 ywqrwdspTFI------VLVLNNGDLNQV-TW-----EQRALAGDPEFSPaQEVIDFpyARYADMLGFKGIRVDRPEDID 526
Cdd:PRK07789 487 --------CAIegipikVALINNGNLGMVrQWqtlfyEERYSNTDLHTHS-HRIPDF--VKLAEAYGCVGLRCEREEDVD 555
|
570
....*....|....*....
gi 15597304 527 AA-WAEAFAADRPVLLEVV 544
Cdd:PRK07789 556 AViEKARAINDRPVVIDFV 574
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-548 |
1.09e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 203.05 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQ-DKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDv 164
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 qqMAAP-KRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKAL 241
Cdd:PRK06466 165 --MTNPaEKFEYEYPKKVKLRSY-SPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVlgNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 242 LGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPkagQARAVQIDLYPRNIGIRYPIDQ 315
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDdrvtngPAKFCP---NAKIIHIDIDPASISKTIKADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 316 ALLGDAGETLERLLPLLEQKKH-------GAWRRRVE--RAvtasREEARRQAEEPADPINPQRVFRSLSEQLPDDAILC 386
Cdd:PRK06466 319 PIVGPVESVLTEMLAILKEIGEkpdkealAAWWKQIDewRG----RHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 387 GDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSP 466
Cdd:PRK06466 395 SDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQ-ELSTCLQY----GLP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 467 TFIVLvLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEA-FAADRPVLLEVV 544
Cdd:PRK06466 470 VKIIN-LNNGALGMVrQWQDMQYEGRHSHSYMESLPDF--VKLAEAYGHVGIRITDLKDLKPKLEEAfAMKDRLVFIDIY 546
|
....
gi 15597304 545 TDPN 548
Cdd:PRK06466 547 VDRS 550
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-552 |
3.12e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 201.91 E-value: 3.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFdYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDAL-YDCGIP-HILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK07710 97 LADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 ----------QQMAAPKRQPHEHGHVMSAVGFVQPrpyardadleaaaaiLNRGRRVAILAGAGAL--GAHRQLEAVAER 232
Cdd:PRK07710 177 vveegefcydVQMDLPGYQPNYEPNLLQIRKLVQA---------------VSVAKKPVILAGAGVLhaKASKELTSYAEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 233 LAAGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPKAGQAravQIDLYPRN 306
Cdd:PRK07710 242 QEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDdrvtgnLAYFAKEATVA---HIDIDPAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 307 IGIRYPIDQALLGDAGETLERLL-PLLEQKKHGAWRRRVEravtASREEARRQAEEPADPINPQRVFRSLSEQLPDDAIL 385
Cdd:PRK07710 319 IGKNVPTEIPIVADAKQALQVLLqQEGKKENHHEWLSLLK----NWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 386 CGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwdS 465
Cdd:PRK07710 395 TTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQ-ELSVIKEL-----S 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 466 PTFIVLVLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLE-- 542
Cdd:PRK07710 469 LPVKVVILNNEALGMVrQWQEEFYNQRYSHSLLSCQPDF--VKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDcr 546
|
570
....*....|
gi 15597304 543 VVTDPNVPPL 552
Cdd:PRK07710 547 VLQSEKVMPM 556
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
4-543 |
1.04e-55 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 197.16 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK08266 5 TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSDYQQ--EVDLQ-SLFKDVSAYVETVVSPAQLLHVLDRALR-VAVGERQVATVI 159
Cdd:PRK08266 85 AALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQqMLSGRPRPVALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQQMAAPkrqphehghVMSAVGFVQPRPYARDAD-LEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVA 238
Cdd:PRK08266 165 MPWDVFGQRAP---------VAAAPPLRPAPPPAPDPDaIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYvtgSIGLLGTRAssmLMEHCDTLLIVGSTF--PYSEFLPKAGQARAVQIDLYPRNIGiRYPIDQA 316
Cdd:PRK08266 236 AFRSGRGIVSDRHPL---GLNFAAAYE---LWPQTDVVIGIGSRLelPTFRWPWRPDGLKVIRIDIDPTEMR-RLKPDVA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLEqkKHGAWRRRVERAVTASREEARRQAEEpadpINPQRVF-RSLSEQLPDDAILCGDSGS--HT 393
Cdd:PRK08266 309 IVADAKAGTAALLDALS--KAGSKRPSRRAELRELKAAARQRIQA----VQPQASYlRAIREALPDDGIFVDELSQvgFA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 394 NWYARDIrMRPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMqMNGNAELVTVQQYwqrwdSPTFIVLVL 473
Cdd:PRK08266 383 SWFAFPV-YAPRTFVT-CGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGF-MFGVQELATAVQH-----NIGVVTVVF 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597304 474 NNGDLNQVTWEQ------RALAGD---PEFspaqevidfpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEV 543
Cdd:PRK08266 455 NNNAYGNVRRDQkrrfggRVVASDlvnPDF-----------VKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEV 522
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-546 |
3.32e-55 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 196.20 E-value: 3.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEaFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSG-IEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIdLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 qqMAAPKRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKALL 242
Cdd:PRK08979 166 --LNPAILHPYEYPESIKMRSY-NPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIisGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 243 GKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPkagQARAVQIDLYPRNIGIRYPIDQA 316
Cdd:PRK08979 243 GLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDdrttnnLEKYCP---NATILHIDIDPSSISKTVRVDIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLEQKKH-------GAWRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDS 389
Cdd:PRK08979 320 IVGSADKVLDSMLALLDESGEtndeaaiASWWNEIEVW----RSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTnwyardirmrpgMLGSL------------SGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQ 457
Cdd:PRK08979 396 GQHQ------------MFAALyypfdkprrwinSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQ-ELSTAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 458 QYwqrwDSPTFIVlVLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEA-FAA 535
Cdd:PRK08979 463 QY----DIPVKII-NLNNRFLGMVkQWQDMIYQGRHSHSYMDSVPDF--AKIAEAYGHVGIRISDPDELESGLEKAlAMK 535
|
570
....*....|.
gi 15597304 536 DRPVLLEVVTD 546
Cdd:PRK08979 536 DRLVFVDINVD 546
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
6-546 |
6.97e-55 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 195.07 E-value: 6.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFdyIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK08617 8 ADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPEL--IVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVAT-VIVPNDV 164
Cdd:PRK08617 86 LVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAfVSLPQDV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 qqMAAPKRQPhehghVMSAVGFVQPRPyARDADLEAAAAILNRGRRVAILAGAGALGahrqlEAVAERLAAGVAKALL-- 242
Cdd:PRK08617 166 --VDAPVTSK-----AIAPLSKPKLGP-ASPEDINYLAELIKNAKLPVLLLGMRASS-----PEVTAAIRRLLERTNLpv 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 243 -----GKAAVSDDL-PYVTGSIGLLGTRASSMLMEHCDTLLIVGstfpYS--EFLPKA----GQARAVQIDLYPRNIGIR 310
Cdd:PRK08617 233 vetfqAAGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIG----YDpiEYEPRNwnseGDATIIHIDVLPAEIDNY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 311 YPIDQALLGDAGETLERLLPLLeqkkHGAWRRRVERAVTASREEARRQAEEPA-----DPINPQRVFRSLSEQLPDDAIL 385
Cdd:PRK08617 309 YQPERELIGDIAATLDLLAEKL----DGLSLSPQSLEILEELRAQLEELAERParleeGAVHPLRIIRALQDIVTDDTTV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 386 CGDSGSHTNWYARDIR-MRP-GMLgsLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGnAELVT-VqqywqR 462
Cdd:PRK08617 385 TVDVGSHYIWMARYFRsYEPrHLL--FSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSA-MELETaV-----R 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 463 WDSPtfIV-LVLNNGDLNQVTWEQRALAGDP---EFSPaqevIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRP 538
Cdd:PRK08617 457 LKLN--IVhIIWNDGHYNMVEFQEEMKYGRSsgvDFGP----VDF--VKYAESFGAKGLRVTSPDELEPVLREALATDGP 528
|
....*...
gi 15597304 539 VLLEVVTD 546
Cdd:PRK08617 529 VVIDIPVD 536
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
5-546 |
1.04e-54 |
|
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: 194.20 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 5 VADQLLERlsqwGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLN 84
Cdd:TIGR02418 5 VVDQLENQ----GVRYVFGIPGAKIDRVFDAL--EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 85 GLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPND 163
Cdd:TIGR02418 79 GLATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVsLPQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 164 VqqMAAPKRqphehGHVMSAVGFVQPRPyARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKAL 241
Cdd:TIGR02418 159 V--VDSPVS-----VKAIPASYAPKLGA-APDDAIDEVAEAIQNAKLPVLLLGLRASspETTEAVRRLLKKTQLPVVETF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 242 LGKAAVSDDL-PYVTGSIGLLGTRASSMLMEHCDTLLIVG-STFPY-SEFLPKAGQARAVQIDLYPRNIGIRYPIDQALL 318
Cdd:TIGR02418 231 QGAGAVSRELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYePRNWNSENDATIVHIDVEPAQIDNNYQPDLELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 319 GDAGETLERLLPLLEQKKHGAWRRRVERAVTASREEA-RRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTNWYA 397
Cdd:TIGR02418 311 GDIASTLDLLAERIPGYELPPDALAILEDLKQQREALdRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 398 RDIR-MRPGMLgSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMqMNGNAELVTVqqywQRWDSPTfIVLVLNNG 476
Cdd:TIGR02418 391 RYFRsYRARHL-LISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGF-LFSSMELETA----VRLKLNI-VHIIWNDN 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597304 477 DLNQVTWEQ----RALAGdPEFSPaqevIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTD 546
Cdd:TIGR02418 464 GYNMVEFQEemkyQRSSG-VDFGP----IDF--VKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
6-552 |
8.31e-54 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 192.44 E-value: 8.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK06882 7 AEMVVQSLRDEGVEYVFGYPGGSVLDIYDAI-HTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 QQMAapKRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAH--RQLEAVAERLAAGVAKALL 242
Cdd:PRK06882 166 VNPA--NKFTYEYPEEVSLRSY-NPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAEcsEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 243 GKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPkagQARAVQIDLYPRNIGIRYPIDQA 316
Cdd:PRK06882 243 GLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDdrttnnLAKYCP---NAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLE-------QKKHGAWRRRVERAvtasreEARR--QAEEPADPINPQRVFRSLSEQLPDDAILCG 387
Cdd:PRK06882 320 IVGSAKNVLEEFLSLLEeenlaksQTDLTAWWQQINEW------KAKKclEFDRTSDVIKPQQVVEAIYRLTNGDAYVAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 388 DSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPT 467
Cdd:PRK06882 394 DVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQ-ELSTAKQY----DIPV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 468 FIVlVLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEA-FAADRPVLLEVVT 545
Cdd:PRK06882 469 VIV-SLNNRFLGMVkQWQDLIYSGRHSQVYMNSLPDF--AKLAEAYGHVGIQIDTPDELEEKLTQAfSIKDKLVFVDVNV 545
|
....*....
gi 15597304 546 DP--NVPPL 552
Cdd:PRK06882 546 DEteHVYPM 554
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-556 |
1.50e-53 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 191.99 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNG 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDAL-HTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDV 164
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVdLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 165 QQMAapKRQPHEHGHVMSAVGFvQPRPYARDADLEAAAAILNRGRRVAILAGAGALGA--HRQLEAVAERLAAGVAKALL 242
Cdd:PRK07979 166 LNPA--NKLPYVWPESVSMRSY-NPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAacHQQLKELVEKLNLPVVSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 243 GKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPkagQARAVQIDLYPRNIGIRYPIDQA 316
Cdd:PRK07979 243 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDdrttnnLAKYCP---NATVLHIDIDPTSISKTVTADIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLEQKKHGA-------WRRRVERAvtasREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDS 389
Cdd:PRK07979 320 IVGDARQVLEQMLELLSQESAHQpldeirdWWQQIEQW----RARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 GSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqrwDSPTfI 469
Cdd:PRK07979 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQ-ELSTALQY----ELPV-L 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 470 VLVLNNGDLNQV-TWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDID---AAWAEAFAADRPVLLEVVT 545
Cdd:PRK07979 470 VLNLNNRYLGMVkQWQDMIYSGRHSQSYMQSLPDF--VRLAEAYGHVGIQISHPDELEsklSEALEQVRNNRLVFVDVTV 547
|
570
....*....|.
gi 15597304 546 DPNVPPLPPHI 556
Cdd:PRK07979 548 DGSEHVYPMQI 558
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-542 |
6.68e-52 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 187.61 E-value: 6.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQ-DDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPN 162
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 163 DVQQMAAPKRQPHEHGHVMSavgfVQPRPYARDADLEAAAAILNRGRRVAILAGAGAL----GAHRQLEAVAERLAAGVA 238
Cdd:PRK09107 171 DVQFATGTYTPPQKAPVHVS----YQPKVKGDAEAITEAVELLANAKRPVIYSGGGVInsgpEASRLLRELVELTGFPIT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFP------YSEFLPKagqARAVQIDLYPRNIGIRYP 312
Cdd:PRK09107 247 STLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDdritgrLDAFSPN---SKKIHIDIDPSSINKNVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 313 IDQALLGDAGETLERLLPLLEQKKH--------------GAWRRRVERAVTASReearrqaeepaDPINPQRVFRSLSEQ 378
Cdd:PRK09107 324 VDVPIIGDVGHVLEDMLRLWKARGKkpdkealadwwgqiARWRARNSLAYTPSD-----------DVIMPQYAIQRLYEL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 379 LPD-DAILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQ 457
Cdd:PRK09107 393 TKGrDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQ-EMSTAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 458 QYwqrwDSPTFIvLVLNNGDLNQVTWEQRALAGDP-EFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAAD 536
Cdd:PRK09107 472 QY----NLPVKI-FILNNQYMGMVRQWQQLLHGNRlSHSYTEAMPDF--VKLAEAYGAVGIRCEKPGDLDDAIQEMIDVD 544
|
....*.
gi 15597304 537 RPVLLE 542
Cdd:PRK09107 545 KPVIFD 550
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-544 |
5.06e-51 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 184.94 E-value: 5.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 6 ADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaeafDYIR---VRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHL 82
Cdd:PLN02470 16 ADILVEALEREGVDTVFAYPGGASMEIHQALTRS----NCIRnvlCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 83 LNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VP 161
Cdd:PLN02470 92 VTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 162 NDVQ-QMAAPKRQPHehghvMSAVGFVQ--PRPyARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVA 238
Cdd:PLN02470 172 KDIQqQLAVPNWNQP-----MKLPGYLSrlPKP-PEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 239 KALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFlpkAGQARAVQIDLYPRNIGIRYP 312
Cdd:PLN02470 246 STLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFddrvtgKLEAF---ASRASIVHIDIDPAEIGKNKQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 313 IDQALLGDAGETLERLLPLLEQKK-----HGAWRRRVEravtASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCG 387
Cdd:PLN02470 323 PHVSVCADVKLALQGLNKLLEERKakrpdFSAWRAELD----EQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIIST 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 388 DSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVqqywqRWDSPT 467
Cdd:PLN02470 399 GVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQ-ELATI-----HVENLP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 468 FIVLVLNNGDLNQVT-WEQRALAGDPEF----SPAQEVIDFP-YARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLL 541
Cdd:PLN02470 473 VKIMVLNNQHLGMVVqWEDRFYKANRAHtylgDPDAEAEIFPdFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLL 552
|
...
gi 15597304 542 EVV 544
Cdd:PLN02470 553 DVI 555
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-565 |
1.68e-49 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 180.73 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGypgdgiNGIMGAMGRRAEAFDY--IRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIH 81
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFG------QSLPSALFLAAEAIGIrqIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 82 LLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQ-VATVIV 160
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPgPVVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVQQMAAPK---RQPHEHGHvmsavgFVQPRPYARDADLEAAAAILNRGRRVAILAGAG--ALGAHRQLEAVAERLAA 235
Cdd:PRK06112 169 PADLLTAAAAApaaPRSNSLGH------FPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 236 GVAKALLGKAAVSDDLPYVTGSIG-LLGTRASSM----LMEHCDTLLIVGS------TFPYSEFLPkagQARAVQIDLYP 304
Cdd:PRK06112 243 PVATTNMGKGAVDETHPLSLGVVGsLMGPRSPGRhlrdLVREADVVLLVGTrtnqngTDSWSLYPE---QAQYIHIDVDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 305 RNIGIRYPIDQaLLGDAGETLERLLPLLEQKK-HGAWRRR------VERAVTASREEARRQAEEPADPINPQRVFRSLSE 377
Cdd:PRK06112 320 EEVGRNYEALR-LVGDARLTLAALTDALRGRDlAARAGRRaalepaIAAGREAHREDSAPVALSDASPIRPERIMAELQA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 378 QLPDDAILCGDSGSHTNWYARDIRMR-PGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQmNGNAELVTV 456
Cdd:PRK06112 399 VLTGDTIVVADASYSSIWVANFLTARrAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFA-HVWAELETA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 457 qqywQRWDSPTFIVlVLNNGDLNQvtweQRAlAGDPEFSPAQEVIDFP---YARYADMLGFKGIRVDRPEDIDAAWAEAF 533
Cdd:PRK06112 478 ----RRMGVPVTIV-VLNNGILGF----QKH-AETVKFGTHTDACHFAavdHAAIARACGCDGVRVEDPAELAQALAAAM 547
|
570 580 590
....*....|....*....|....*....|..
gi 15597304 534 AADRPVLLEVVTDPNVppLPPHISFEQAKHLL 565
Cdd:PRK06112 548 AAPGPTLIEVITDPSA--FPPISFFEPMDRAA 577
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
4-543 |
7.97e-49 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 178.26 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRaEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRR-GKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSD--YQQEVDLQ-SLFKDVSAYVETVVSPAQLLHVLDRALRVAvgerQVA---- 156
Cdd:PRK07064 83 GALVEALTAGTPLLHITGQIETPYLDQDlgYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVA----LTAptgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 157 -TVIVPNDVQQMaapkrqPHEHGHVMSAVGFVQPRPYArdADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAErLAA 235
Cdd:PRK07064 159 vSVEIPIDIQAA------EIELPDDLAPVHVAVPEPDA--AAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 236 GVAKALLGKAAVSDDLPYVTGSIGllGTRASSMLMEHCDTLLIVGS------TFPYSEFLPKAgqarAVQIDLYPRNIGI 309
Cdd:PRK07064 230 GVVTSTQGRGVVPEDHPASLGAFN--NSAAVEALYKTCDLLLVVGSrlrgneTLKYSLALPRP----LIRVDADAAADGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 310 RYPIDQALLGDAGETLERLLPLLEQKKHG--AWRRRVERAVTASREEARRQaeepadpINPQRVF-RSLSEQLPDDAILC 386
Cdd:PRK07064 304 GYPNDLFVHGDAARVLARLADRLEGRLSVdpAFAADLRAAREAAVADLRKG-------LGPYAKLvDALRAALPRDGNWV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 387 GD---SGShtNWYARDIRMRPGMLG--SLSGKLatmGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNgNAELVTVQQywq 461
Cdd:PRK07064 377 RDvtiSNS--TWGNRLLPIFEPRANvhALGGGI---GQGLAMAIGAALAGPGRKTVGLVGDGGLMLN-LGELATAVQ--- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 462 rwDSPTFIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLL 541
Cdd:PRK07064 448 --ENANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVELHTPDF--ALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLV 523
|
..
gi 15597304 542 EV 543
Cdd:PRK07064 524 EV 525
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
9-575 |
1.25e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 175.41 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 9 LLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAFD--YIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNGL 86
Cdd:PRK06456 8 LVDSLKREGVKVIFGIPGLSNMQIYDAFVEDLANGElrHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 87 YDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VPNDVQ 165
Cdd:PRK06456 88 ITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIdIPRDIF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 166 -----QMAAPKRqPHEHGHvmsavgfvQPRPYARD-ADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGV 237
Cdd:PRK06456 168 yekmeEIKWPEK-PLVKGY--------RDFPTRIDrLALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 238 AKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTF------PYSEFlpKAGQARAVQIDLYPRNIGIRY 311
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFsdrtftSYDEM--VETRKKFIMVNIDPTDGEKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 312 PIDQALLGDAG----ETLERLLPLLEQKKHGAWRRRVERAvtasRE--EARRQAEEPaDPINPQRVFRSLSEQLPDDAIL 385
Cdd:PRK06456 317 KVDVGIYGNAKiilrELIKAITELGQKRDRSAWLKRVKEY----KEyySQFYYTEEN-GKLKPWKIMKTIRQALPRDAIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 386 CGDSGSHTNWYARDIR-MRPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNAELVTVQQYWqrwd 464
Cdd:PRK06456 392 TTGVGQHQMWAEVFWEvLEPRTFLT-SSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHI---- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 465 spTFIVLVLNNGDLNQVTWEQRALAGDP----EFSPAQEvidfpYARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVL 540
Cdd:PRK06456 467 --PVISVIFDNRTLGLVRQVQDLFFGKRivgvDYGPSPD-----FVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAV 539
|
570 580 590
....*....|....*....|....*....|....*...
gi 15597304 541 LEVVTDPN---VPPLPPHISFEQakhllgaMLQDDPKR 575
Cdd:PRK06456 540 IRVPVDKEelaLPTLPPGGRLKQ-------VILRDPRK 570
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-543 |
2.72e-46 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 170.93 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGdgINGIMGAMGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLL 83
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPG--VHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 84 NGLYDARMDHQPVLAIVGQQAATALGSD--YQQEV-DLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI- 159
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSVNRRASLGKGrgKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVqqMAAPKrqphehGHVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAHRQLEAVAERLAAGVAK 239
Cdd:PRK07524 161 IPLDV--LAAPA------DHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 240 ALLGKAAVSDDLPYVTGSI-GLLGTRAssmLMEHCDTLLIVGSTFPYSEF-------LPKAGqaRAVQIDLYPRNIGIRY 311
Cdd:PRK07524 233 TINAKGLLPAGHPLLLGASqSLPAVRA---LIAEADVVLAVGTELGETDYdvyfdggFPLPG--ELIRIDIDPDQLARNY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 312 PIDQALLGDAGETLERLLPLLEQkkHGAWRRRVERAVTASREEARrqaEEPADPINPQ-RVFRSLSEQLPdDAILCGDS- 389
Cdd:PRK07524 308 PPALALVGDARAALEALLARLPG--QAAAADWGAARVAALRQALR---AEWDPLTAAQvALLDTILAALP-DAIFVGDSt 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 390 -----GSHTnwYARDirmRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGnAELVTVQQYwqrwD 464
Cdd:PRK07524 382 qpvyaGNLY--FDAD---APRRWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTL-PELASAVEA----D 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 465 SPtFIVLVLNNGDLNQVTWEQRALAGDPE----FSPaqeviDFpyARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVL 540
Cdd:PRK07524 452 LP-LIVLLWNNDGYGEIRRYMVARDIEPVgvdpYTP-----DF--IALARAFGCAAERVADLEQLQAALRAAFARPGPTL 523
|
...
gi 15597304 541 LEV 543
Cdd:PRK07524 524 IEV 526
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-545 |
1.43e-45 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 169.61 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 5 VADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAeafdyIRVRHEEMAAFMAGAHAKFTG--EVGVCLATSGPGAIHL 82
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFPVNELFDAAAAAGIRP-----VIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 83 LNGLYDARMDHQPVLAIVG--QQAATALGSDYQQEVDlqslFKDVSAYVETVVSPAQLLHVLDRAL-RVAVGERQVATVI 159
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTgyPRGSTDVAPNFESLRN----YRHITKWCEQVTLPDEVPELMRRAFtRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 160 VPNDVQQMAAPkRQPHEHGHVMSAvgfvqpRPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGV 237
Cdd:PRK06154 173 LPVDVLAEELD-ELPLDHRPSRRS------RPGADPVEVVEAAALLLAAERPVIYAGQGVLyaQATPELKELAELLEIPV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 238 AKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDTLLIVGSTFPYSEF-LPKAGQARAVQIDLYPRNIGIRYPIDQA 316
Cdd:PRK06154 246 MTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYgLPMPEGKTIIHSTLDDADLNKDYPIDHG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 317 LLGDAGETLERLLPLLEqKKHGAWRRRVERAVT---ASREEARRQAEEP----ADPINPQRVFRSLSEQL-PDDAILCGD 388
Cdd:PRK06154 326 LVGDAALVLKQMIEELR-RRVGPDRGRAQQVAAeieAVRAAWLAKWMPKltsdSTPINPYRVVWELQHAVdIKTVIITHD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 389 SGSHTN-----WYARdirmRPG-MLGSlsGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGnAELVTVqqywQR 462
Cdd:PRK06154 405 AGSPRDqlspfYVAS----RPGsYLGW--GKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTG-MDFETA----VR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 463 WDSPTFIVLvLNNGDL---------NQVTWEQRALAGDpefspaqevidfpYARYADMLGFKGIRVDRPEDIDAA---WA 530
Cdd:PRK06154 474 ERIPILTIL-LNNFSMggydkvmpvSTTKYRATDISGD-------------YAAIARALGGYGERVEDPEMLVPAllrAL 539
|
570
....*....|....*
gi 15597304 531 EAFAADRPVLLEVVT 545
Cdd:PRK06154 540 RKVKEGTPALLEVIT 554
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-171 |
1.01e-44 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 156.24 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 5 VADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEaFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLN 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPG-IRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 85 GLYDARMDHQPVLAIVGQQAATALGSDY-QQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAV-GERQVATVIVPN 162
Cdd:pfam02776 80 GLANAYVDSVPLLVISGQRPRSLVGRGAlQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALsGRPGPVYLEIPL 159
|
....*....
gi 15597304 163 DVQQMAAPK 171
Cdd:pfam02776 160 DVLLEEVDE 168
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
4-546 |
6.79e-44 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 165.15 E-value: 6.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFT-GEVGVCLATSGPGAIHL 82
Cdd:PRK11269 5 RAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAM-RKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 83 LNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVI-VP 161
Cdd:PRK11269 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIdLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 162 NDVQqmaapkrqphehghvMSAVGF----VQP----RPYARDADLEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAE 231
Cdd:PRK11269 164 FDVQ---------------VAEIEFdpdtYEPlpvyKPAATRAQIEKALEMLNAAERPLIVAGGGVInaDASDLLVEFAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 232 RLAAGVAKALLGKAAVSDDLPYVTGSIGL-LGTRASSMLMEHCDTLLIVGSTFP---------YSeflpkaGQARAVQID 301
Cdd:PRK11269 229 LTGVPVIPTLMGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWAnrhtgsvevYT------KGRKFVHVD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 302 LYPRNIGIRYPIDQALLGDAGETLERLLPLL-EQKKHGAWRRRveRAVTASREEARRQAEEPAD----PINPQRVFRSLS 376
Cdd:PRK11269 303 IEPTQIGRVFGPDLGIVSDAKAALELLVEVArEWKAAGRLPDR--SAWVADCQERKRTLLRKTHfdnvPIKPQRVYEEMN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 377 EQLPDDAILCGDSGSHTNWYARDIRM-RP------GMLGSLsgklatmGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNG 449
Cdd:PRK11269 381 KAFGRDTCYVSTIGLSQIAAAQFLHVyKPrhwincGQAGPL-------GWTIPAALGVRAADPDRNVVALSGDYDFQFLI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 450 NaELVTVQQYwqrwDSPtFIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFP--------YARYADMLGFKGIRVDR 521
Cdd:PRK11269 454 E-ELAVGAQF----NLP-YIHVLVNNAYLGLIRQAQRAFDMDYCVQLAFENINSPelngygvdHVKVAEGLGCKAIRVFK 527
|
570 580
....*....|....*....|....*....
gi 15597304 522 PEDI----DAAWAEAFAADRPVLLEVVTD 546
Cdd:PRK11269 528 PEDIapalEQAKALMAEFRVPVVVEVILE 556
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
7-161 |
3.06e-43 |
|
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: 151.92 E-value: 3.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 7 DQLLERLSQWGVKRVFGYPGDGINGIMGAMgrRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNGL 86
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDAL--ARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597304 87 YDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQ-VATVIVP 161
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPgPVALDLP 154
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
10-549 |
5.07e-43 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 161.81 E-value: 5.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 10 LERLSQWGVKRVFGYPGDGINGIMGamGRRAEAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNGLYDA 89
Cdd:PRK05858 12 ARRLKAHGVDTMFTLSGGHLFPLYD--GAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 90 RMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVG-ERQVATVIVPND-VQQM 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDhAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 168 AAPKRQPhehghvmsAVGFVQPRPYARDAD-LEAAAAILNRGRRVAILAGAG--ALGAHRQLEAVAERLAAGVAKALLGK 244
Cdd:PRK05858 170 ADDDGRP--------GALTELPAGPTPDPDaLARAAGLLAEAQRPVIMAGTDvwWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 245 AAVSDDLPyvtgsigLLGTRASSMLMEHCDTLLIVGSTFP----YSEFlpkAGQARAVQIDLYPRNIGIRYPIDQALLGD 320
Cdd:PRK05858 242 GVVPADHP-------LAFSRARGKALGEADVVLVVGVPMDfrlgFGVF---GGTAQLVHVDDAPPQRAHHRPVAAGLYGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 321 AGETLERLLPLLEQK-KHGAWRRRVERAVTASREEARRQAEEPADPINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARD 399
Cdd:PRK05858 312 LSAILSALAGAGGDRtDHQGWIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 400 IR-MRPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGnAELVTVqqywQRWDSPTFIVlVLNNGDL 478
Cdd:PRK05858 392 IDpYRPGCWLD-PGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSL-MDVDTL----VRHNLPVVSV-IGNNGIW 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597304 479 NQVTWEQRALAGdpeFSPAQEVIdfPYARY---ADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNV 549
Cdd:PRK05858 465 GLEKHPMEALYG---YDVAADLR--PGTRYdevVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSV 533
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-552 |
6.01e-37 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 144.53 E-value: 6.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 1 MSSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMgrraEAFDYIRV---RHEEMAAFMAGAHAKFTGeVGVCLATSGP 77
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAI----EAHPGIRWvgcCNELNAGYAADGYARVNG-LGALVTTYGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 78 GAIHLLNGLYDARMDHQPVLAIVGQQAATALGS-------------DYQQEVdlqslFKDVSAYvETVVSPAQLLHVLDR 144
Cdd:COG3961 78 GELSAINGIAGAYAERVPVVHIVGAPGTRAQRRgpllhhtlgdgdfDHFLRM-----FEEVTVA-QAVLTPENAAAEIDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 145 ALRVAVGERQVATVIVPNDVQQM-AAPKRQPHEHGHVMSAvgfvqprPYARDADLEAAAAILNRGRRVAILAG--AGALG 221
Cdd:COG3961 152 VLAAALREKRPVYIELPRDVADApIEPPEAPLPLPPPASD-------PAALAAAVAAAAERLAKAKRPVILAGveVHRFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 222 AHRQLEAVAERLAAGVAKALLGKAAVSDDLP-YV---TGSIGLLGTRAssmLMEHCDTLLIVGSTFpySEFLPKAGQAR- 296
Cdd:COG3961 225 LQEELLALAEKTGIPVATTLLGKSVLDESHPqFIgtyAGAASSPEVRE---YVENADCVLCLGVVF--TDTNTGGFTAQl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 297 --AVQIDLYPRNIGIRYPI-DQALLGDAgetLERLLPLLeqkkhgaWRRRVERAVTASREEarRQAEEPADPINPQRVFR 373
Cdd:COG3961 300 dpERTIDIQPDSVRVGGHIyPGVSLADF---LEALAELL-------KKRSAPLPAPAPPPP--PPPAAPDAPLTQDRLWQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 374 SLSEQLPDDAILCGDSGshTNWY-ARDIRMRPG------ML-GSlsgklatMGSGVPYAIAAKLAYPQRPVVAMVGDGAM 445
Cdd:COG3961 368 RLQAFLDPGDIVVADTG--TSLFgAADLRLPEGatfiaqPLwGS-------IGYTLPAALGAALAAPDRRVILLVGDGAF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 446 QMNGNaELVTVQQYWQRwdsPtfIVLVLNNGDLnqvTWEqRALAGDPEfsPAQEVIDFPYARYADMLG---FKGIRVDRP 522
Cdd:COG3961 439 QLTAQ-ELSTMLRYGLK---P--IIFVLNNDGY---TIE-RAIHGPDG--PYNDIANWDYAKLPEAFGggnALGFRVTTE 506
|
570 580 590
....*....|....*....|....*....|..
gi 15597304 523 EDIDAA-WAEAFAADRPVLLEVVTDPN-VPPL 552
Cdd:COG3961 507 GELEEAlAAAEANTDRLTLIEVVLDKMdAPPL 538
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
366-554 |
2.71e-35 |
|
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: 131.08 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 366 INPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRM-RPGMLGSlSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGA 444
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFkKPRSWLT-SGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 445 MQMNGNaELVTVQQYwqrwDSPtFIVLVLNNGDLNQVT-WEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPE 523
Cdd:cd02015 80 FQMNIQ-ELATAAQY----NLP-VKIVILNNGSLGMVRqWQELFYEGRYSHTTLDSNPDF--VKLAEAYGIKGLRVEKPE 151
|
170 180 190
....*....|....*....|....*....|...
gi 15597304 524 DIDAAWAEAFAADRPVLLEVVTDP--NVPPLPP 554
Cdd:cd02015 152 ELEAALKEALASDGPVLLDVLVDPeeNVLPMVP 184
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
198-328 |
2.36e-33 |
|
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: 124.21 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 198 LEAAAAILNRGRRVAILAGAGAL--GAHRQLEAVAERLAAGVAKALLGKAAVSDDLPYVTGSIGLLGTRASSMLMEHCDT 275
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 276 LLIVGSTF-------PYSEFLPkagQARAVQIDLYPRNIGIRYPIDQALLGDAGETLERL 328
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP---DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
4-526 |
3.14e-32 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 131.28 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 4 TVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAEAF----DYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGA 79
Cdd:PRK08327 8 TAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 80 IHLLNGLYDARMDHQPVLAIVGQQAAT---ALGS-----DYQQEV-DLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAV 150
Cdd:PRK08327 88 ANALGGVHNAARSRIPVLVFAGRSPYTeegELGSrntriHWTQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 151 GE-RQVATVIVPNDVQQMAAPKRQphehghvMSAVGFVQPRPYA-RDADLEAAAAILNRGRRVAILA--GAGALGAHRQL 226
Cdd:PRK08327 168 SEpKGPVYLTLPREVLAEEVPEVK-------ADAGRQMAPAPPApDPEDIARAAEMLAAAERPVIITwrAGRTAEGFASL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 227 EAVAERLAAGVAKALLGKAAVSDDLP-YVTGSIGLLGTRAssmlmehcDTLLIVGSTFPYSE-FLPKAGQARAVQID--- 301
Cdd:PRK08327 241 RRLAEELAIPVVEYAGEVVNYPSDHPlHLGPDPRADLAEA--------DLVLVVDSDVPWIPkKIRPDADARVIQIDvdp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 302 LYPRnIGIR-YPIDQALLGDAGETLERLLPLLEQKKHGAWRRRVERAVTAS-----REEARRQAEEPA---DPINPQRVF 372
Cdd:PRK08327 313 LKSR-IPLWgFPCDLCIQADTSTALDQLEERLKSLASAERRRARRRRAAVRelrirQEAAKRAEIERLkdrGPITPAYLS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 373 RSLSEQLPDDAILCGDSGShTNWYARdiRMRPG-MLGSLSGklATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMqMNGNA 451
Cdd:PRK08327 392 YCLGEVADEYDAIVTEYPF-VPRQAR--LNKPGsYFGDGSA--GGLGWALGAALGAKLATPDRLVIATVGDGSF-IFGVP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 452 ELVtvqqYW--QRWDSPTFIVlVLNNGDLNQVtwEQRALAGDPEfSPAQEVIDFP---------YARYADMLGFKGIRVD 520
Cdd:PRK08327 466 EAA----HWvaERYGLPVLVV-VFNNGGWLAV--KEAVLEVYPE-GYAARKGTFPgtdfdprpdFAKIAEAFGGYGERVE 537
|
....*.
gi 15597304 521 RPEDID 526
Cdd:PRK08327 538 DPEELK 543
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
370-545 |
2.26e-31 |
|
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: 119.67 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 370 RVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNG 449
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 450 NaELVTVQQYwqrwDSPTfIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFpyARYADMLGFKGIRVDRPEDIDAAW 529
Cdd:cd00568 81 Q-ELATAVRY----GLPV-IVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDF--AALAEAYGAKGVRVEDPEDLEAAL 152
|
170
....*....|....*.
gi 15597304 530 AEAFAADRPVLLEVVT 545
Cdd:cd00568 153 AEALAAGGPALIEVKT 168
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
388-543 |
3.79e-29 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 112.68 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 388 DSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNaELVTVQQYwqRWDspt 467
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRY--NLP--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597304 468 FIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFP-YARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEV 543
Cdd:pfam02775 75 ITVVVLNNGGYGMTRGQQTPFGGGRYSGPSGKILPPVdFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-161 |
3.87e-27 |
|
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: 107.43 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 9 LLERLSQWGVKRVFGYPGDGINGIMGAMgRRAEAFDYIRVRHEEMAAFMAGAHAKFTGeVGVCLATSGPGAIHLLNGLYD 88
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDAL-REGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597304 89 ARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVGERQVATVIVP 161
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLP 153
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
368-546 |
4.98e-27 |
|
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: 107.62 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 368 PQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMRP--GMLGSlsGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAM 445
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKprHRLDA--GTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 446 QMNGnAELVTVQQYwqrwDSPtFIVLVLNNGDLNQVTWEQRALAGDPEFsPAQEVIDFPYARYADMLGFKGIRVDRPEDI 525
Cdd:cd02004 79 GFSG-MELETAVRY----NLP-IVVVVGNNGGWYQGLDGQQLSYGLGLP-VTTLLPDTRYDLVAEAFGGKGELVTTPEEL 151
|
170 180
....*....|....*....|.
gi 15597304 526 DAAWAEAFAADRPVLLEVVTD 546
Cdd:cd02004 152 KPALKRALASGKPALINVIID 172
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
368-546 |
1.19e-25 |
|
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: 103.91 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 368 PQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRM-RPGMLgSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQ 446
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTyAPNTC-LISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 447 MNgNAELVTVqqywQRWDSPtFIVLVLNNGDLNQVTWEQRALAG---DPEFSPaqevIDFpyARYADMLGFKGIRVDRPE 523
Cdd:cd02010 80 MN-SQELETA----VRLKIP-LVVLIWNDNGYGLIKWKQEKEYGrdsGVDFGN----PDF--VKYAESFGAKGYRIESAD 147
|
170 180
....*....|....*....|...
gi 15597304 524 DIDAAWAEAFAADRPVLLEVVTD 546
Cdd:cd02010 148 DLLPVLERALAADGVHVIDCPVD 170
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
9-547 |
3.01e-22 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 100.83 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 9 LLERLSQWGVKRVFGYPGDGINGimgaMGRRAEA--FDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIHLLNGL 86
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITD----LARLAQAegIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 87 YDARMDHQPVLAIVGqqaatalgSDYQQEVDLQ-----SLfkDVSAYVETVVSPA-QLLHVLD------RALRVAVGERQ 154
Cdd:PRK09259 92 ANATTNCFPMIMISG--------SSEREIVDLQqgdyeEL--DQLNAAKPFCKAAfRVNRAEDigigvaRAIRTAVSGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 155 VATVI-VPNDV--QQMAAPKRQphehghvMSAVGFVQPRPY---ARDAdLEAAAAILNRGRRVAILAGAGALGAH--RQL 226
Cdd:PRK09259 162 GGVYLdLPAKVlaQTMDADEAL-------TSLVKVVDPAPAqlpAPEA-VDRALDLLKKAKRPLIILGKGAAYAQadEQI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 227 EAVAER-----LAAGVAKALLgkaavSDDLPYVTGSigllgtrASSMLMEHCDTLLIVGS----TFPYSEFLPKAGQARA 297
Cdd:PRK09259 234 REFVEKtgipfLPMSMAKGLL-----PDTHPQSAAA-------ARSLALANADVVLLVGArlnwLLSHGKGKTWGADKKF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 298 VQIDLYPRNIGIRYPIDQALLGDAGETLERLLPLLEQ---KKHGAWRRRV-ERAVTASREEARRQAEEPaDPINPQRVFR 373
Cdd:PRK09259 302 IQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLDALaERKEKNAAKMAEKLSTDT-QPMNFYNALG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 374 SLSEQLPD--DAILCGDsGSHTNWYARDI--------RMRPGMLGslsgklaTMGSGVPYAIAAKLAyPQRPVVAMVGDG 443
Cdd:PRK09259 381 AIRDVLKEnpDIYLVNE-GANTLDLARNIidmykprhRLDCGTWG-------VMGIGMGYAIAAAVE-TGKPVVAIEGDS 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 444 AMQMNGnAELVTVQQYwqrwDSPTFIVlVLNNGDLNQVTWEQRALAGDPefSPAQEVIDFPYARYADMLGFKGIRVDRPE 523
Cdd:PRK09259 452 AFGFSG-MEVETICRY----NLPVTVV-IFNNGGIYRGDDVNLSGAGDP--SPTVLVHHARYDKMMEAFGGVGYNVTTPD 523
|
570 580
....*....|....*....|....
gi 15597304 524 DIDAAWAEAFAADRPVLLEVVTDP 547
Cdd:PRK09259 524 ELRHALTEAIASGKPTLINVVIDP 547
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
76-445 |
3.33e-22 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 100.30 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 76 GPGaihLLNG---LYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVAVG- 151
Cdd:PRK07586 73 GPG---LANGlanLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 152 ERQVATVIVPNDVQQmaapkrqphEHGHVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAGAGALGAhRQLEAvAE 231
Cdd:PRK07586 150 PGQVATLILPADVAW---------SEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRE-RGLAA-AA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 232 RLAAGVAKALL------------GKAAVsDDLPYvtgsiglLGTRASSMLmEHCDTLLIVGSTFPYSEFLpkagqaravq 299
Cdd:PRK07586 219 RIAAATGARLLaetfparmergaGRPAV-ERLPY-------FAEQALAQL-AGVRHLVLVGAKAPVAFFA---------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 300 idlYPRNIGIRYPIDQALL------GDAGETLERLLPLLeqkkhGAWRrrvERAVTASREEARRqaeePADPINPQRVFR 373
Cdd:PRK07586 280 ---YPGKPSRLVPEGCEVHtlagpgEDAAAALEALADAL-----GAKP---AAPPLAAPARPPL----PTGALTPEAIAQ 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597304 374 SLSEQLPDDAILCGDSG-SHTNWYARDIRMRPGMLGSLSGklATMGSGVPYAIAAKLAYPQRPVVAMVGDG-AM 445
Cdd:PRK07586 345 VIAALLPENAIVVDESItSGRGFFPATAGAAPHDWLTLTG--GAIGQGLPLATGAAVACPDRKVLALQGDGsAM 416
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
366-545 |
7.86e-19 |
|
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: 84.18 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 366 INPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRM-RPGM-LGSLSGKLatmGSGVPYAIAAKLAYPQRPVVAMVGDG 443
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLtRPGSyFTLRGGGL---GWGLPAAVGAALANPDRKVVAIIGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 444 AMqMNGNAELVTvqqyWQRWDSPtFIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDF--P---YARYADMLGFKGIR 518
Cdd:cd02002 78 SF-MYTIQALWT----AARYGLP-VTVVILNNRGYGALRSFLKRVGPEGPGENAPDGLDLldPgidFAAIAKAFGVEAER 151
|
170 180
....*....|....*....|....*..
gi 15597304 519 VDRPEDIDAAWAEAFAADRPVLLEVVT 545
Cdd:cd02002 152 VETPEELDEALREALAEGGPALIEVVV 178
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
364-547 |
1.29e-18 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 84.10 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 364 DPINPQRVFRSLSEQLPDDAILCGDSG---SHTNWYARDIRMR----PGMLGSLsgklatmGSGVPYAIAAKLAYPQRPV 436
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGnicSVANSYLRFEKPRsfiaPLSFGNC-------GYALPAIIGAKAAAPDRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 437 VAMVGDGAMQMNGNaELVTVQQYwqrwDSPTFIVLVLNNG----DLNQVTWEQRALAGdpefspaQEVIDFPYARYADML 512
Cdd:cd02013 75 VAIAGDGAWGMSMM-EIMTAVRH----KLPVTAVVFRNRQwgaeKKNQVDFYNNRFVG-------TELESESFAKIAEAC 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 15597304 513 GFKGIRVDRPEDIDAA---WAEAFAADRPVLLEVVTDP 547
Cdd:cd02013 143 GAKGITVDKPEDVGPAlqkAIAMMAEGKTTVIEIVCDQ 180
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
2-460 |
3.29e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 84.92 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 2 SSTVADQLLERLSQWGVKRVFGYPGDGINGIMGAMGRRAeAFDYIRVRHEEMAAFMAGAHAKFTGEVGVCLATSGPGAIH 81
Cdd:PRK12474 4 TMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVP-RMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 82 LLNGLYDARMDHQPVLAIVGQQAATALGSDYQQEVDLQSLFKDVSAYVETVVSPAQLLHVLDRALRVA-VGERQVATVIV 160
Cdd:PRK12474 83 GLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAqSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 161 PNDVQQmaapkrqpHEHGHVMSAVGFVQPRPYARDAdLEAAAAILNRGRRVAILAGAGALGAHrQLEAvAERLAAGVAKA 240
Cdd:PRK12474 163 PADVAW--------NEAAYAAQPLRGIGPAPVAAET-VERIAALLRNGKKSALLLRGSALRGA-PLEA-AGRIQAKTGVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 241 LL------------GKAAVSdDLPYVTGSIGllgtrassMLMEHCDTLLIVGSTFPYSEFLPKAGQARavqidLYPRNIG 308
Cdd:PRK12474 232 LYcdtfapriergaGRVPIE-RIPYFHEQIT--------AFLKDVEQLVLVGAKPPVSFFAYPGKPSW-----GAPPGCE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 309 IRYpidqalLGDAGETLERLLplleqkkhgawrRRVERAVTASREEARRQ----AEEPADPINPQRVFRSLSEQLPDDAI 384
Cdd:PRK12474 298 IVY------LAQPDEDLAQAL------------QDLADAVDAPAEPAARTplalPALPKGALNSLGVAQLIAHRTPDQAI 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597304 385 LCGDSGSHTNWYARDI-RMRPGMLGSLSGklATMGSGVPYAIAAKLAYPQRPVVAMVGDGamqmngnAELVTVQQYW 460
Cdd:PRK12474 360 YADEALTSGLFFDMSYdRARPHTHLPLTG--GSIGQGLPLAAGAAVAAPDRKVVCPQGDG-------GAAYTMQALW 427
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
370-550 |
2.00e-13 |
|
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: 69.26 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 370 RVFRSLSEQLPDDAILCGDSGS-----HTNWYARDIR---MRPGmlgslsgkLATMGSGVPYAIAAKLAYPQRPVVAMVG 441
Cdd:cd02003 3 EVLGALNEAIGDDDVVINAAGSlpgdlHKLWRARTPGgyhLEYG--------YSCMGYEIAAGLGAKLAKPDREVYVLVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 442 DGAMQMNgNAELVTVQQYWQRwdsptFIVLVLNN------GDLNQVTWEQR-----------ALAGDPEFSPaqevIDFp 504
Cdd:cd02003 75 DGSYLML-HSEIVTAVQEGLK-----IIIVLFDNhgfgciNNLQESTGSGSfgtefrdrdqeSGQLDGALLP----VDF- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15597304 505 yARYADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTDPNVP 550
Cdd:cd02003 144 -AANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTDPKSM 188
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
365-551 |
2.05e-11 |
|
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: 62.94 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 365 PINPQRVFRSLSEQLPDDAILCGDSGshTNWY-ARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDG 443
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETG--TSWFgALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 444 AMQMNGNaELVTVQQYwqRWDSptfIVLVLNNgdlNQVTWEqRALAGDPefSPAQEVIDFPYARYADMLGF----KGIRV 519
Cdd:cd02005 79 SFQMTVQ-ELSTMIRY--GLNP---IIFLINN---DGYTIE-RAIHGPE--ASYNDIANWNYTKLPEVFGGggggLSFRV 146
|
170 180 190
....*....|....*....|....*....|...
gi 15597304 520 DRPEDIDAA-WAEAFAADRPVLLEVVTDPNVPP 551
Cdd:cd02005 147 KTEGELDEAlKDALFNRDKLSLIEVILPKDDAP 179
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
9-154 |
2.45e-11 |
|
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: 62.13 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 9 LLERLSQWGVKRVFGYPGDGINGIMGAMgrraEAFDYIRV---RHEEMAAFMAGAHAKFTGeVGVCLATSGPGAIHLLNG 85
Cdd:cd07038 3 LLERLKQLGVKHVFGVPGDYNLPLLDAI----EENPGLRWvgnCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 86 LYDARMDHQPVLAIVGQQAATALGS-------------DYQQEVdlqslFKDVSAYVETVVSPAQLLHVLDRALRVAVGE 152
Cdd:cd07038 78 IAGAYAEHVPVVHIVGAPSTKAQASglllhhtlgdgdfDVFLKM-----FEEITCAAARLTDPENAAEEIDRVLRTALRE 152
|
..
gi 15597304 153 RQ 154
Cdd:cd07038 153 SR 154
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
2-476 |
2.79e-08 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 56.63 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 2 SSTVADQLLERLSQWGVKRVFGYPGDgINGIMgamgrraeaFDY---------IRVRHEEMAAFMAGAHAKFTGeVGVCL 72
Cdd:PLN02573 15 DATLGRHLARRLVEIGVTDVFSVPGD-FNLTL---------LDHliaepglnlIGCCNELNAGYAADGYARARG-VGACV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 73 ATSGPGAIHLLNGLYDARMDHQPVLAIVGQQAATALGS-----------DYQQEVdlqSLFKDVSAYvETVVSPAQLLH- 140
Cdd:PLN02573 84 VTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYGTnrilhhtiglpDFSQEL---RCFQTVTCY-QAVINNLEDAHe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 141 VLDRALRVAVGERQVATVIVPNDVQQMAAP--KRQPhehghVMSAVGFVQPRPYARDADLEAAAAILNRGRRVAILAG-- 216
Cdd:PLN02573 160 LIDTAISTALKESKPVYISVSCNLAAIPHPtfSREP-----VPFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPVLVGGpk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 217 ---AGALGAHRQLeavAErlAAGVAKALL--GKAAVSDDLPYVTGSI-GLLGTRASSMLMEHCDTLLIVG------STFP 284
Cdd:PLN02573 235 lrvAKACKAFVEL---AD--ASGYPVAVMpsAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGpifndySSVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 285 YSeFLPKAGQARAVQIDlypR-NIGIRYPIDQALLGDAGETLERLLplleqKKHGAWRRRVERAVTASREEARRqaeEPA 363
Cdd:PLN02573 310 YS-LLLKKEKAIIVQPD---RvTIGNGPAFGCVLMKDFLEALAKRV-----KKNTTAYENYKRIFVPEGEPLKS---EPG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 364 DPINPQRVFRSLSEQL-PDDAILC--GDSgshtnWY-----------ARDIRMRPGMLGSLSGklATMGsgvpYAIAAkl 429
Cdd:PLN02573 378 EPLRVNVLFKHIQKMLsGDTAVIAetGDS-----WFncqklklpegcGYEFQMQYGSIGWSVG--ATLG----YAQAA-- 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15597304 430 ayPQRPVVAMVGDGAMQMNGNaELVTVQQYWQRwdsptFIVLVLNNG 476
Cdd:PLN02573 445 --PDKRVIACIGDGSFQVTAQ-DVSTMIRCGQK-----SIIFLINNG 483
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
365-544 |
2.09e-06 |
|
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: 48.82 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 365 PINPQRVFRSLSEQLPDDAILCGDSGSHTNWYARDIRMRPGMLGSLSGKLATMGSGVPYAIAAKLAYPQRPVVAMVGDGA 444
Cdd:cd02006 7 PIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 445 MQMNGNaELVTVQQYwqrwdSPTFIVLVLNNGDLNQVTWEQRALAGDPEFSPAQEVIDFP--------YARYADMLGFKG 516
Cdd:cd02006 87 FQFMIE-ELAVGAQH-----RIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSSelggygvdHVKVAEGLGCKA 160
|
170 180 190
....*....|....*....|....*....|..
gi 15597304 517 IRVDRPEDI----DAAWAEAFAADRPVLLEVV 544
Cdd:cd02006 161 IRVTKPEELaaafEQAKKLMAEHRVPVVVEAI 192
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-491 |
1.04e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 43.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 406 MLGSlsgklatMGSGVPYAIAAKLAYPQRPVVAMVGDGAMQMNGNAeLVTVQQYWQRwdspTFIVLVLNNGdLNQVTWEQ 485
Cdd:PRK06163 55 MLGS-------MGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGA-LGTIAALAPK----NLTIIVMDNG-VYQITGGQ 121
|
....*.
gi 15597304 486 RALAGD 491
Cdd:PRK06163 122 PTLTSQ 127
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
368-443 |
2.47e-03 |
|
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: 39.18 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597304 368 PQR-VFRSLSEQLPDDAILCGDSGSHTNWYARDIRMrpgMLGSLsgklaTMGSGVPYAIAAKLAYPQRPVVAMVGDG 443
Cdd:cd02008 11 PHRpSFYALRKAFKKDSIVSGDIGCYTLGALPPLNA---IDTCT-----CMGASIGVAIGMAKASEDKKVVAVIGDS 79
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
371-554 |
2.85e-03 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 39.19 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 371 VFRSLSEQLPDDAILCG-DSGSHTNWYARDIRMRPGMLGSlsgklatMGSGVPYAIAAKLAYPqRPVVAMVGDGAMQMNG 449
Cdd:cd03372 4 AIKTLIADLKDELVVSNiGFPSKELYAAGDRPLNFYMLGS-------MGLASSIGLGLALAQP-RKVIVIDGDGSLLMNL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 450 NAeLVTVQQywqrwDSP-TFIVLVLNNGdlnqvtweQRALAGDPEfSPAQEVIDFpyARYADMLGFKGIR-VDRPEDIDa 527
Cdd:cd03372 76 GA-LATIAA-----EKPkNLIIVVLDNG--------AYGSTGNQP-THAGKKTDL--EAVAKACGLDNVAtVASEEAFE- 137
|
170 180 190
....*....|....*....|....*....|..
gi 15597304 528 aWAEAFAADRPVLLEVVTDPN-----VPPLPP 554
Cdd:cd03372 138 -KAVEQALDGPSFIHVKIKPGntdvpNIPRDP 168
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
424-546 |
3.41e-03 |
|
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: 38.73 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 424 AIAAKLAYPQrPVVAMVGDGAMQ--MNGnaeLVTVQQYWQRwdsptFIVLVLNNG-----DLNQVTWEQRALagDPEFSP 496
Cdd:cd02009 60 ALGIALATDK-PTVLLTGDLSFLhdLNG---LLLGKQEPLN-----LTIVVINNNgggifSLLPQASFEDEF--ERLFGT 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15597304 497 AQEViDFPYAryADMLGFKGIRVDRPEDIDAAWAEAFAADRPVLLEVVTD 546
Cdd:cd02009 129 PQGL-DFEHL--AKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
375-476 |
4.98e-03 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 38.45 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597304 375 LSEQLPDDAILCGdsgshTNWYARD---IRMRPG--------MLGSlsgklatMG--SGVPYAIAakLAYPQRPVVAMVG 441
Cdd:cd03371 9 LSRAPATAAVVST-----TGMTSRElfeLRDRPGgghaqdflTVGS-------MGhaSQIALGIA--LARPDRKVVCIDG 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 15597304 442 DGA--MQMNGnaeLVTVQQYwqrwDSPTFIVLVLNNG 476
Cdd:cd03371 75 DGAalMHMGG---LATIGGL----APANLIHIVLNNG 104
|
|
| |
