|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-581 |
0e+00 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 977.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGA 80
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 81 IHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDAtrIFEIVDEAIRTAYREKGVAV 160
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAEN--LPEIVNQAIRTAYEKKGVAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 161 LTLPNNILNTKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPS 240
Cdd:PRK08611 159 LTIPDDLPAQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 241 KTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVDYLPKKnIPAIQIDENPEAIGHRFDVDAPIVGDSQLA 320
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKK-AKAIQIDTDPANIGKRYPVNVGLVGDAKKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 321 LRALTDAIQPVEKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGV 400
Cdd:PRK08611 318 LHQLTENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 401 NNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGE 480
Cdd:PRK08611 398 NQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 481 LEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIVPEQAINYAKWAYRSLT 560
Cdd:PRK08611 478 LEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
570 580
....*....|....*....|.
gi 505961992 561 EDRKfiFNEMPSLTTAVRRFL 581
Cdd:PRK08611 558 EDKK--LDQMPPLKKALKRFL 576
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
9-543 |
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: 545.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:COG0028 8 ALVEALEAEGVETVFGVPGGAILPLYDAL-RRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTGLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNI 167
Cdd:COG0028 87 DAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVT--DPEDLPEVLRRAFRIATSGRpGPVVLDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 168 LNTKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTIVG 245
Cdd:COG0028 165 QAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAaeELRALAERLGAPVVTTLMGKGAFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 246 DDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVD------YLPKKNIpaIQIDENPEAIGHRFDVDAPIVGDSQL 319
Cdd:COG0028 245 EDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVtgnwdeFAPDAKI--IHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 320 ALRALTDAIQPveKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLG 399
Cdd:COG0028 323 VLAALLEALEP--RADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 400 VNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAG 479
Cdd:COG0028 401 RPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505961992 480 ELEY-GIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKI 543
Cdd:COG0028 481 GGRYsGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATL 545
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-544 |
3.48e-150 |
|
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: 444.28 E-value: 3.48e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 6 ANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLN 85
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 86 GMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREKGVAVLTLPN 165
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTA--MTAESLPHVIDEAIRRAYAHNGVAVVTIPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 166 NILNTKVEDNFPT-----EVEPYVPErrqPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPS 240
Cdd:TIGR02720 159 DFGWQEIPDNDYYassvsYQTPLLPA---PDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 241 KTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPY--VDYLPKKNIPAIQIDENPEAIGHRFDVDAPIVGDSQ 318
Cdd:TIGR02720 236 KGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFaeVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 319 LALRALTDAIQPVEKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNL 398
Cdd:TIGR02720 316 KALAAILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 399 GVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEA 478
Cdd:TIGR02720 396 TPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDT 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505961992 479 GELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAV--QQHKPTIVNVYVdKNAAPLPGKIV 544
Cdd:TIGR02720 476 NQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKaiKQGKPVLIDAKI-TGDRPLPVEKL 542
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
10-551 |
2.47e-148 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 438.49 E-value: 2.47e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK06457 8 IIRVLEDNGIQRIYGIPGDSIDPLVDAIR--KSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDATRIfeIVDEAIRTAYREKGVAVLTLPNNILN 169
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEY--IIRRAIREAISKRGVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 170 TKVEdnfpTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPSKTIVGDDHP 249
Cdd:PRK06457 164 KSSE----YKGSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDLDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 250 YNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVDYLPkKNIPAIQIDENPEAIGHRFDVDAPIVGDSQLALRaltdaIQ 329
Cdd:PRK06457 240 KVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-KSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN-----ID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 330 PVEK-RSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISS 408
Cdd:PRK06457 314 IEEKsDKFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 409 WLGTMGCALPTAI-ASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDF 487
Cdd:PRK06457 394 WLGSMGIGVPGSVgASFAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505961992 488 SDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIVPEQAINY 551
Cdd:PRK06457 474 YNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEY 537
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
5-563 |
5.36e-133 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 400.13 E-value: 5.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 5 KANMA--LVSALKAWDIDHVYGIPGDSIDAVVDGLKVAEnDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIH 82
Cdd:PRK09124 2 KQTVAdyIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMG-TIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 83 LLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREKGVAVLT 162
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELV--SNPEQLPRVLAIAMRKAILNRGVAVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 163 LPNNILNTKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPSKT 242
Cdd:PRK09124 159 LPGDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 243 IVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVDYLPKK-NIpaIQIDENPEAIGHRFDVDAPIVGDSQLAL 321
Cdd:PRK09124 239 HVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDaKI--IQIDINPGSLGRRSPVDLGLVGDVKATL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 322 RALTDAIQPVEKRSFLNEMLDH-RETWKGWMTEDKNNDAS-PIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLN-- 397
Cdd:PRK09124 317 AALLPLLEEKTDRKFLDKALEHyRKARKGLDDLAVPSDGGkPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKmn 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 398 -----LGVNNHfiisswlGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIK 472
Cdd:PRK09124 397 gkrrlLGSFNH-------GSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 473 YEQQEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIVPEQAINYA 552
Cdd:PRK09124 470 MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFS 549
|
570
....*....|.
gi 505961992 553 KWAYRSLTEDR 563
Cdd:PRK09124 550 LYMLRAIISGR 560
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
10-557 |
5.55e-131 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 395.13 E-value: 5.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKVAeNDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK06546 9 LVEQLVAAGVKRIYGIVGDSLNPIVDAVRRT-GGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREKGVAVLTLPNNILN 169
Cdd:PRK06546 88 AHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMV--SSAEQAPRVLHSAIQHAVAGGGVSVVTLPGDIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 170 TKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPSKTIVGDDHP 249
Cdd:PRK06546 166 EPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWIQYDNP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 250 YNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVDYLPKKNIpaIQIDENPEAIGHRFDVDAPIVGDSQLALRALTDAIQ 329
Cdd:PRK06546 246 FDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLPDVRT--AQVDIDPEHLGRRTRVDLAVHGDVAETIRALLPLVK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 330 PVEKRSFLNEMLD-HRETWKGWMTE--DKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFII 406
Cdd:PRK06546 324 EKTDRRFLDRMLKkHARKLEKVVGAytRKVEKHTPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVIG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 407 SSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGID 486
Cdd:PRK06546 404 SFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPDFGTD 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505961992 487 FSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIVPEQAINYAKWAYR 557
Cdd:PRK06546 484 HPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASK 554
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
10-553 |
4.26e-124 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 377.71 E-value: 4.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK08273 9 ILERLREWGVRRVFGYPGDGINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAvYNYQLKESDATRIFEIVDEAIRTAYREKGVAVLTLPNNILN 169
Cdd:PRK08273 89 AKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVILPNDVQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 170 TKVED------NFPTEVePYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPSKTI 243
Cdd:PRK08273 168 LEYEPpphahgTVHSGV-GYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKALLGKAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 244 VGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPYVDYLPKK-NIPAIQIDENPEAIGHRFDVDAPIVGDSQLALR 322
Cdd:PRK08273 247 LPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKEgQARGVQIDIDGRMLGLRYPMEVNLVGDAAETLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 323 ALTDAIQPVEKRSFLNEMLDHRETWkgWMTEDK--NNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNL-- 398
Cdd:PRK08273 327 ALLPLLERKKDRSWRERIEKWVARW--WETLEAraMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDLRMrr 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 399 GVNNHfiISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMV-MQDFSTAVQY-----NLPMVLFVLNNSELSFIK 472
Cdd:PRK08273 405 GMMAS--LSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVLNNRDLNQVT 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 473 YEQQE---AGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIVPEQAI 549
Cdd:PRK08273 483 WEQRVmegDPKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITLEQAK 562
|
....
gi 505961992 550 NYAK 553
Cdd:PRK08273 563 AFAS 566
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
9-540 |
3.39e-110 |
|
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: 340.93 E-value: 3.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:TIGR00118 6 AIIESLKDEGVKTVFGYPGGAILPIYDALY-NDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTGIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEA--IRTAYReKGVAVLTLPNN 166
Cdd:TIGR00118 85 TAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVK--SAEDIPRIIKEAfhIATTGR-PGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 167 ILNTKVEDNFPTEVE-----PYV-PERRQplsheIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTL 238
Cdd:TIGR00118 162 VTTAEIEYPYPEKVNlpgyrPTVkGHPLQ-----IKKAAELINLAKKPVILVGGGVIIAGAseELKELAERIQIPVTTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 239 PSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYP------YVDYLPKKNIpaIQIDENPEAIGHRFDVDAP 312
Cdd:TIGR00118 237 MGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDdrvtgnLAKFAPNAKI--IHIDIDPAEIGKNVRVDIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 313 IVGDSQLALRALTDAIQPVEKR---SFLNEMLDHRETWKGWMTEDKNndasPIRPERLMDAINKVMTDDTVIAADVGTST 389
Cdd:TIGR00118 315 IVGDARNVLEELLKKLFELKERkesAWLEQINKWKKEYPLKMDYTEE----GIKPQQVIEELSRVTKDEAIVTTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 390 VWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELS 469
Cdd:TIGR00118 391 MWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLG 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 470 FIKYEQqeagELEYGIDFSDI------DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLP 540
Cdd:TIGR00118 471 MVRQWQ----ELFYEERYSHThmgslpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLP 543
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
10-533 |
4.77e-98 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 308.68 E-value: 4.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK08322 7 FVKCLENEGVEYIFGIPGEENLDLLEALR--DSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDAtrIFEIVDEAIRTAYREKGVAV-LTLPNNIL 168
Cdd:PRK08322 85 AQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDN--IPEVVREAFRLAEEERPGAVhLELPEDIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 NTKVEDNF--PTEVEPYVPERRQplsheIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSKTIV 244
Cdd:PRK08322 163 AEETDGKPlpRSYSRRPYASPKA-----IERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 245 GDDHPYNLGNLGKigSKPSY--QAMQNADLLILAGtnYPYVDYLPKK-----NIPAIQIDENPEAIGHRFDVDAPIVGDS 317
Cdd:PRK08322 238 PETHPLSLGTAGL--SQGDYvhCAIEHADLIINVG--HDVIEKPPFFmnpngDKKVIHINFLPAEVDPVYFPQVEVVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 318 QLALRALTDAIQPVEKRSFlNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLN 397
Cdd:PRK08322 314 ANSLWQLKERLADQPHWDF-PRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARNYR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 398 LGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQE 477
Cdd:PRK08322 393 AYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQEN 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 505961992 478 AGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD 533
Cdd:PRK08322 473 MGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-548 |
2.43e-96 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 304.78 E-value: 2.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLkvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGA 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDEL--YDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 81 IHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYR-EKGVA 159
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQ--DAKDLPRIIKEAFHIASTgRPGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 160 VLTLPNNILNTKVEDNFPTEVE--PYVPERRQPLsHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTI 235
Cdd:PRK06048 161 LIDLPKDVTTAEIDFDYPDKVElrGYKPTYKGNP-QQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 236 VTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNY------PYVDYLPKKNIpaIQIDENPEAIGHRFDV 309
Cdd:PRK06048 240 TTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFddrvtgKLASFAPNAKI--IHIDIDPAEISKNVKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 310 DAPIVGDSQLALRALTDAIQpvEKRSflNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDdTVIAADVGTST 389
Cdd:PRK06048 318 DVPIVGDAKQVLKSLIKYVQ--YCDR--KEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCPD-AIIVTEVGQHQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 390 VWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELS 469
Cdd:PRK06048 393 MWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 470 FIKYEQqeagELEYGIDFS------DIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPgkI 543
Cdd:PRK06048 473 MVRQWQ----ELFYDKRYShtcikgSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP--M 546
|
....*
gi 505961992 544 VPEQA 548
Cdd:PRK06048 547 VPAGA 551
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-570 |
9.14e-93 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 296.28 E-value: 9.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK06276 6 AIIKALEAEGVKIIFGYPGGALLPFYDALY--DSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNI 167
Cdd:PRK06276 84 TAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIK--KPEEIPEIFRAAFEIAKTGRpGPVHIDLPKDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 168 LNTKVE---DNFPTEVE--PYVPERR-QPLshEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLP 239
Cdd:PRK06276 162 QEGELDlekYPIPAKIDlpGYKPTTFgHPL--QIKKAAELIAEAERPVILAGGGVIISGAseELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 240 SKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYP------YVDYLPKKNIpaIQIDENPEAIGHRFDVDAPI 313
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSdrttgdISSFAPNAKI--IHIDIDPAEIGKNVRVDVPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 314 VGDSQLALRALTDAI---QPVEKRSFLNEMLDHRETWKGWMTEDKnndaSPIRPERLMDAINKVMTD-----DTVIAADV 385
Cdd:PRK06276 318 VGDAKNVLRDLLAELmkkEIKNKSEWLERVKKLKKESIPRMDFDD----KPIKPQRVIKELMEVLREidpskNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 386 GTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNN 465
Cdd:PRK06276 394 GQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 466 SELSFIkYEQQeagELEYGIDFSDI------DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAApL 539
Cdd:PRK06276 474 RTLGMV-YQWQ---NLYYGKRQSEVhlgetpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEA-L 548
|
570 580 590
....*....|....*....|....*....|.
gi 505961992 540 PgKIVPEQAINYAKWAYRSLTEDRKFIFNEM 570
Cdd:PRK06276 549 P-MVPPGGNLTNILGPYRVEPTVKAQCFSEI 578
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
361-538 |
2.25e-85 |
|
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: 263.24 E-value: 2.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 361 PIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGA 440
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 441 FEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAV 520
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|....*...
gi 505961992 521 QQHKPTIVNVYVDKNAAP 538
Cdd:cd02014 161 AADGPVVIDVVTDPNEPP 178
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
10-545 |
3.65e-83 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 270.43 E-value: 3.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK08527 9 VCEALKEEGVKVVFGYPGGAILNIYDEI-YKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTGLAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEA--IRTAYREKGVAVlTLPNNI 167
Cdd:PRK08527 88 AYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVK--SIEELPRILKEAfyIARSGRPGPVHI-DIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 168 LNTKVEDNFPTEV--EPYVPERRQPlSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTI 243
Cdd:PRK08527 165 TATLGEFEYPKEIslKTYKPTYKGN-SRQIKKAAEAIKEAKKPLFYLGGGAILSNAseEIRELVKKTGIPAVETLMARGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 244 VGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYLP------KKNIPAIQIDENPEAIGHRFDVDAPIVGDS 317
Cdd:PRK08527 244 LRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFD--DRVTgklsefAKHAKIIHVDIDPSSISKIVNADYPIVGDL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 318 QLALRALTDAIQPVEKRSFLN--EMLDHRETWKGWMTEDKNNdasPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRY 395
Cdd:PRK08527 322 KNVLKEMLEELKEENPTTYKEwrEILKRYNELHPLSYEDSDE---VLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 396 LNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQ 475
Cdd:PRK08527 399 YPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQ 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505961992 476 QeageLEYGIDFSDID------FAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPgkIVP 545
Cdd:PRK08527 479 T----FFYEERYSETDlstqpdFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP--MVP 548
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
9-536 |
2.58e-80 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 262.89 E-value: 2.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK08199 13 ILVDALRANGVERVFCVPGESYLAVLDALH-DETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASIGVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREK-GVAVLTLPNNI 167
Cdd:PRK08199 92 TAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEI--DDAARIPELVSRAFHVATSGRpGPVVLALPEDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 168 LNTKVEdnfPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGKIPTIVTLPSKTIVG 245
Cdd:PRK08199 170 LSETAE---VPDAPPYRRVAAAPGAADLARLAELLARAERPLVILGGSgwTEAAVADLRAFAERWGLPVACAFRRQDLFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 246 DDHPYNLGNLGkIGSKPSYQA-MQNADLLILAGT--------NYPYVDY-LPKKNIpaIQIDENPEAIGHRFDVDAPIVG 315
Cdd:PRK08199 247 NRHPNYAGDLG-LGINPALAArIREADLVLAVGTrlgevttqGYTLLDIpVPRQTL--VHVHPDAEELGRVYRPDLAIVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 316 DSQLALRALtDAIQPVekrsflnemldHRETWKGWmTEDKNND---ASPIRP-------ERLMDAINKVMTDDTVIAADV 385
Cdd:PRK08199 324 DPAAFAAAL-AALEPP-----------ASPAWAEW-TAAAHADylaWSAPLPgpgavqlGEVMAWLRERLPADAIITNGA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 386 GTSTVWSTRYLNL-GVNNHFIISSwlGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLN 464
Cdd:PRK08199 391 GNYATWLHRFFRFrRYRTQLAPTS--GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVN 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 465 NSELSFIKYEQqeagELEY-----GIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNA 536
Cdd:PRK08199 469 NGMYGTIRMHQ----EREYpgrvsGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEA 541
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
9-533 |
8.65e-79 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 258.63 E-value: 8.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK08617 10 LVVDSLINQGVKYVFGIPGAKIDRVFDALE--DSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATGLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQ---ADSHKLgtkAFQEVDLPKLFEDVAVYNYQLKESDAtrIFEIVDEAIRTAYREK-GVAVLTLP 164
Cdd:PRK08617 88 TATAEGDPVVAIGGQvkrADRLKR---THQSMDNVALFRPITKYSAEVQDPDN--LSEVLANAFRAAESGRpGAAFVSLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 165 NNILNTkvednfPTEVEPYVPERRQPLS----HEIQRAAQLFNESKRPVILVG-KGTDHAKAE-VREFIEKGKIPTIVTL 238
Cdd:PRK08617 163 QDVVDA------PVTSKAIAPLSKPKLGpaspEDINYLAELIKNAKLPVLLLGmRASSPEVTAaIRRLLERTNLPVVETF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 239 PSKTIVGDDHPYNLgnLGKIG---SKPSYQAMQNADLLILAGtnYPYVDYLPK-----KNIPAIQIDENPEAIGHRFDVD 310
Cdd:PRK08617 237 QAAGVISRELEDHF--FGRVGlfrNQPGDELLKKADLVITIG--YDPIEYEPRnwnseGDATIIHIDVLPAEIDNYYQPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 311 APIVGDSQLALRALTDAIQPV----EKRSFLNEMLDHRETWKGwmtEDKNNDASPIRPERLMDAINKVMTDDTVIAADVG 386
Cdd:PRK08617 313 RELIGDIAATLDLLAEKLDGLslspQSLEILEELRAQLEELAE---RPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 387 TSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNS 466
Cdd:PRK08617 390 SHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDG 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505961992 467 ELSFIKYEQqeagELEY----GIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD 533
Cdd:PRK08617 470 HYNMVEFQE----EMKYgrssGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVD 536
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
10-546 |
2.42e-77 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 255.46 E-value: 2.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDglKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK07710 22 LIEALEKEGVEVIFGYPGGAVLPLYD--ALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNIl 168
Cdd:PRK07710 100 AMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVR--KASDLPRIIKEAFHIATTGRpGPVLIDIPKDM- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 nTKVEDNFPTEVEPYVP---ERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTI 243
Cdd:PRK07710 177 -VVEEGEFCYDVQMDLPgyqPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKAskELTSYAEQQEIPVVHTLLGLGG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 244 VGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGT--------NYPYvdYLPKKNIPAIQIDenPEAIGHRFDVDAPIVG 315
Cdd:PRK07710 256 FPADHPLFLGMAGMHGTYTANMALYECDLLINIGArfddrvtgNLAY--FAKEATVAHIDID--PAEIGKNVPTEIPIVA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 316 DSQLALRALtdaIQPVEKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRY 395
Cdd:PRK07710 332 DAKQALQVL---LQQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 396 LNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQ 475
Cdd:PRK07710 409 YPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQ 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 476 QEAGELEYGIDF--SDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYV--DKNAAPL--PGKIVPE 546
Cdd:PRK07710 489 EEFYNQRYSHSLlsCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVlqSEKVMPMvaPGKGLHE 565
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
9-536 |
3.56e-77 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 256.06 E-value: 3.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK07789 36 AVVRSLEELGVDVVFGIPGGAILPVYDPLF-DSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTPIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREKGVAVLT-LPNNI 167
Cdd:PRK07789 115 DANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVT--DADDIPRVIAEAFHIASTGRPGPVLVdIPKDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 168 LNTKVEDNFPTEVE-P-YVPERRqPLSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSKTI 243
Cdd:PRK07789 193 LQAQTTFSWPPRMDlPgYRPVTK-PHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTGIPVVTTLMARGA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 244 VGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYpyvD---------YLPKKNIpaIQIDENPEAIGHRFDVDAPIV 314
Cdd:PRK07789 272 FPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARF---DdrvtgkldsFAPDAKV--IHADIDPAEIGKNRHADVPIV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 315 GDSQLALRALTDAIQPVEK----------RSFLNEMldhRETW-KGWmteDKNNDASpIRPERLMDAINKVMTDDTVIAA 383
Cdd:PRK07789 347 GDVKEVIAELIAALRAEHAaggkpdltawWAYLDGW---RETYpLGY---DEPSDGS-LAPQYVIERLGEIAGPDAIYVA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 384 DVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVL 463
Cdd:PRK07789 420 GVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALI 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 464 NNSELSFIKYEQQeageLEYGIDFSDI----------DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQ-QHKPTIVNVYV 532
Cdd:PRK07789 500 NNGNLGMVRQWQT----LFYEERYSNTdlhthshripDFVKLAEAYGCVGLRCEREEDVDAVIEKARAiNDRPVVIDFVV 575
|
....
gi 505961992 533 DKNA 536
Cdd:PRK07789 576 GKDA 579
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
10-543 |
4.31e-77 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 254.67 E-value: 4.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK06466 10 LVRALRDEGVEYIYGYPGGAVLHIYDAL-FKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGIAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNIL 168
Cdd:PRK06466 89 AYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVK--HASEIPEIIKKAFYIAQSGRpGPVVVDIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 N--TKVEDNFPTEVE--PYVPERRQPlSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSKT 242
Cdd:PRK06466 167 NpaEKFEYEYPKKVKlrSYSPAVRGH-SGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 243 IVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYP-YVDYLPKKNIPA---IQIDENPEAIGHRFDVDAPIVGDSQ 318
Cdd:PRK06466 246 GFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDdRVTNGPAKFCPNakiIHIDIDPASISKTIKADIPIVGPVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 319 LALRALTDAIQPVEKR---SFLNEMLDHRETWKGW--MTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWST 393
Cdd:PRK06466 326 SVLTEMLAILKEIGEKpdkEALAAWWKQIDEWRGRhgLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMFAA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 394 RYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKY 473
Cdd:PRK06466 406 QYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMVRQ 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505961992 474 EQQEAGELEYGIDFSDI--DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQ-QHKPTIVNVYVDKNAAPLPGKI 543
Cdd:PRK06466 486 WQDMQYEGRHSHSYMESlpDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQI 558
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
10-542 |
2.41e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 252.58 E-value: 2.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK06725 21 VIQCLKKLGVTTVFGYPGGAILPVYDAL--YESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGLAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNIL 168
Cdd:PRK06725 99 AYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVR--DVNQLSRIVQEAFYIAESGRpGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 NTKVEDNFPTEVE--PYVPERRqPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTIV 244
Cdd:PRK06725 177 NEKVTSFYNEVVEipGYKPEPR-PDSMKLREVAKAISKAKRPLLYIGGGVIHSGGseELIEFARENRIPVVSTLMGLGAY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 245 GDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYLPKK------NIPAIQIDENPEAIGHRFDVDAPIVGDSQ 318
Cdd:PRK06725 256 PPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFD--DRVTGKlelfspHSKKVHIDIDPSEFHKNVAVEYPVVGDVK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 319 LALRALTDAIQPVEKRSFLNEMldhrETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNL 398
Cdd:PRK06725 334 KALHMLLHMSIHTQTDEWLQKV----KTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 399 GVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEA 478
Cdd:PRK06725 410 KNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMF 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505961992 479 GELEYG-IDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD--KNAAPL--PGK 542
Cdd:PRK06725 490 YENRLSeSKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEegENVFPMvpPNK 558
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
9-542 |
3.59e-76 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 252.70 E-value: 3.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAEND--IDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNG 86
Cdd:CHL00099 15 ALIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKKglIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 87 MYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTA-YREKGVAVLTLPN 165
Cdd:CHL00099 95 IATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVR--DARDISRIVAEAFYIAkHGRPGPVLIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 166 NILNTKVEDNFPTEVEPYV-----PERRQPLSHEIQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGKIPTIVTL 238
Cdd:CHL00099 173 DVGLEKFDYYPPEPGNTIIkilgcRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGaiISDAHQEITELAELYKIPVTTTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 239 PSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYLPKK------NIPAIQIDENPEAIGHRFDVDAP 312
Cdd:CHL00099 253 MGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFD--DRVTGKldefacNAQVIHIDIDPAEIGKNRIPQVA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 313 IVGDSQLALRALTDAIqpveKRSFLNEMLDHRETWKGWMTEDKNN-------DASPIRPERLMDAINKVMTdDTVIAADV 385
Cdd:CHL00099 331 IVGDVKKVLQELLELL----KNSPNLLESEQTQAWRERINRWRKEypllipkPSTSLSPQEVINEISQLAP-DAYFTTDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 386 GTSTVWSTRYLNLGVnNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNN 465
Cdd:CHL00099 406 GQHQMWAAQFLKCKP-RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 466 SELSFIKYEQQEAgeleYGIDFSDI-------DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYV--DKNA 536
Cdd:CHL00099 485 KWQGMVRQWQQAF----YGERYSHSnmeegapDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVieDENC 560
|
....*...
gi 505961992 537 APL--PGK 542
Cdd:CHL00099 561 YPMvaPGK 568
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
9-550 |
4.09e-76 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 251.34 E-value: 4.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSI----DAVVDGlkvaenDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLL 84
Cdd:PRK08978 6 WVVHALRAQGVDTVFGYPGGAImpvyDALYDG------GVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 85 NGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDlpklfedvaVYNYQL---KES----DATRIFEIVDEAIRTAYREKG 157
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIGTDAFQEID---------VLGLSLactKHSflvqSLEELPEIMAEAFEIASSGRP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 158 VAVLT-LPNNILNTkvednfPTEVEPYVPERRQPLSH---EIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGK 231
Cdd:PRK08978 151 GPVLVdIPKDIQLA------EGELEPHLTTVENEPAFpaaELEQARALLAQAKKPVLYVGGGVGMAGAvpALREFLAATG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 232 IPTIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYpyvD---------YLPKKNIpaIQIDENPEA 302
Cdd:PRK08978 225 MPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARF---DdrvtgklntFAPHAKV--IHLDIDPAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 303 IGHRFDVDAPIVGDSQLALRALTdaiQPVEkrsfLNEMLDHRETWK---GWmteDKNNDASPIRPERLMDAINKVMTDDT 379
Cdd:PRK08978 300 INKLRQAHVALQGDLNALLPALQ---QPLN----IDAWRQHCAQLRaehAW---RYDHPGEAIYAPALLKQLSDRKPADT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 380 VIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMV 459
Cdd:PRK08978 370 VVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 460 LFVLNNSELSFIKYEQQEAGELEYG-IDFSD-IDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD--KN 535
Cdd:PRK08978 450 IVLLDNQRLGMVRQWQQLFFDERYSeTDLSDnPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDelEN 529
|
570
....*....|....*
gi 505961992 536 AAPLpgkiVPEQAIN 550
Cdd:PRK08978 530 VWPL----VPPGASN 540
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
10-533 |
9.13e-76 |
|
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: 250.44 E-value: 9.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:TIGR02418 5 VVDQLENQGVRYVFGIPGAKIDRVFDALE--DKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDAtrIFEIVDEAIRTAYR-EKGVAVLTLPNNIL 168
Cdd:TIGR02418 83 ANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDA--LSEVVANAFRAAESgKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 NTKV-EDNFPTEvepYVPERRQPLSHEIQRAAQLFNESKRPVILVG-KGTDHAKAE-VREFIEKGKIPTIVTLPSKTIVG 245
Cdd:TIGR02418 161 DSPVsVKAIPAS---YAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGlRASSPETTEaVRRLLKKTQLPVVETFQGAGAVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 246 DD-HPYNLGNLGKIGSKPSYQAMQNADLLILAGtnYPYVDYLPK---KNIPA--IQIDENPEAIGHRFDVDAPIVGDSQL 319
Cdd:TIGR02418 238 RElEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDPIEYEPRnwnSENDAtiVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 320 ALRALTdaiQPVEKRSFLNEMLDHRETWKGWMTEDKNNDASP----IRPERLMDAINKVMTDDTVIAADVGTSTVWSTRY 395
Cdd:TIGR02418 316 TLDLLA---ERIPGYELPPDALAILEDLKQQREALDRVPATLkqahLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 396 LNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQ 475
Cdd:TIGR02418 393 FRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 505961992 476 QEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD 533
Cdd:TIGR02418 473 EMKYQRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
10-540 |
1.03e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 251.30 E-value: 1.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGL--KVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGM 87
Cdd:PRK06456 8 LVDSLKREGVKVIFGIPGLSNMQIYDAFveDLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 88 YDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDatRIFEIVDEAIRTAYREK-GVAVLTLPNN 166
Cdd:PRK06456 88 ITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRID--EIPQWIKNAFYIATTGRpGPVVIDIPRD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 167 ILNTKVED-NFPT--EVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSK 241
Cdd:PRK06456 166 IFYEKMEEiKWPEkpLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTFPGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 242 TIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAG--------TNYPYVDYLPKKNIpAIQIDenPEAIGHRFDVDAPI 313
Cdd:PRK06456 246 TAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGarfsdrtfTSYDEMVETRKKFI-MVNID--PTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 314 VGDSQLALRALTDAIQPV----EKRSFLNEMLDHRETWKGWMTEDKNNDaspIRPERLMDAINKVMTDDTVIAADVGTST 389
Cdd:PRK06456 323 YGNAKIILRELIKAITELgqkrDRSAWLKRVKEYKEYYSQFYYTEENGK---LKPWKIMKTIRQALPRDAIVTTGVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 390 VWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELS 469
Cdd:PRK06456 400 MWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLG 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505961992 470 FIKYEQQE-AGELEYGIDF-SDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLP 540
Cdd:PRK06456 480 LVRQVQDLfFGKRIVGVDYgPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALP 552
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
9-542 |
3.11e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 251.12 E-value: 3.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDIDFIH--VRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNG 86
Cdd:PRK07418 24 ALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKHilVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 87 MYDAKMDNVPQLVLSGQADSHKLGTKAFQEVD-----LPklfedVAVYNYQLKesDATRIFEIVDEAIRTAYREKGVAVL 161
Cdd:PRK07418 104 IATAQMDSVPMVVITGQVPRPAIGTDAFQETDifgitLP-----IVKHSYVVR--DPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 162 T-LPNNILN-----TKVEdnfPTEVEP--YVPERRqPLSHEIQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGK 231
Cdd:PRK07418 177 IdIPKDVGQeefdyVPVE---PGSVKPpgYRPTVK-GNPRQINAALKLIEEAERPLLYVGGGaiSAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 232 IPTIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYLPKK------NIPAIQIDENPEAIGH 305
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFD--DRVTGKldefasRAKVIHIDIDPAEVGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 306 RFDVDAPIVGDSQLALRALTD-AIQP-VEKRSflNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKvMTDDTVIAA 383
Cdd:PRK07418 331 NRRPDVPIVGDVRKVLVKLLErSLEPtTPPRT--QAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRD-LAPDAYYTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 384 DVGTSTVWSTRYLNLGvNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVL 463
Cdd:PRK07418 408 DVGQHQMWAAQFLRNG-PRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 464 NNSELSFIKYEQQEAGELEYGIdfSDI-----DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYV--DKNA 536
Cdd:PRK07418 487 NNGWQGMVRQWQESFYGERYSA--SNMepgmpDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVrrDENC 564
|
....*...
gi 505961992 537 APL--PGK 542
Cdd:PRK07418 565 YPMvpPGK 572
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
10-545 |
3.58e-74 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 247.04 E-value: 3.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENdIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEG-IRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESdaTRIFEIVDEAIRTAYREK-GVAVLTLPNNIL 168
Cdd:PRK07282 95 AMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRET--ADIPRIITEAVHIATTGRpGPVVIDLPKDVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 NTKV-EDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTIVG 245
Cdd:PRK07282 173 ALETdFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAatELNAFAERYQIPVVTTLLGQGTIA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 246 DDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYL---PK---KNIPAIQIDENPEAIGHRFDVDAPIVGDSQL 319
Cdd:PRK07282 253 TSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFD--DRLtgnPKtfaKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 320 ALRALTDaiqpvekrsfLNEMLDHRETWKGWMTEDKNN------DASPIRPERLMDAINKVMTDDTVIAADVGTSTVWST 393
Cdd:PRK07282 331 ALQMLLA----------EPTVHNNTEKWIEKVTKDKNRvrsydkKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 394 RYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKY 473
Cdd:PRK07282 401 QYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505961992 474 EQQEAGELEYGIDFSDI--DFAKFAEACGGVGYTLKDPKDIDSIVQTaVQQHKPTIVNVYVDKNAAPLPgkIVP 545
Cdd:PRK07282 481 WQESFYEGRTSESVFDTlpDFQLMAQAYGIKHYKFDNPETLAQDLEV-ITEDVPMLIEVDISRKEHVLP--MVP 551
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
6-548 |
1.11e-73 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 246.16 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 6 ANMaLVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLN 85
Cdd:PRK09107 14 AEM-VVQALKDQGVEHIFGYPGGAVLPIYDEIF-QQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 86 GMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLP 164
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVK--DVNDLARVIHEAFHVATSGRpGPVVVDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 165 NNIlntkvedNFPTEVepYVPERRQPLSH-----------EIQRAAQLFNESKRPVILVGKGT----DHAKAEVREFIEK 229
Cdd:PRK09107 170 KDV-------QFATGT--YTPPQKAPVHVsyqpkvkgdaeAITEAVELLANAKRPVIYSGGGVinsgPEASRLLRELVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 230 GKIPTIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYP------YVDYLPKKNIpaIQIDENPEAI 303
Cdd:PRK09107 241 TGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDdritgrLDAFSPNSKK--IHIDIDPSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 304 GHRFDVDAPIVGDsqlALRALTDAIQ--PVEKRSFLNEMLD----HRETWKGWMTEDKNNDASPIRP----ERLMDAINK 373
Cdd:PRK09107 319 NKNVRVDVPIIGD---VGHVLEDMLRlwKARGKKPDKEALAdwwgQIARWRARNSLAYTPSDDVIMPqyaiQRLYELTKG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 374 VmtdDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQ 453
Cdd:PRK09107 396 R---DTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 454 YNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSDI--DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVY 531
Cdd:PRK09107 473 YNLPVKIFILNNQYMGMVRQWQQLLHGNRLSHSYTEAmpDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCR 552
|
570 580
....*....|....*....|....*.
gi 505961992 532 VDKNAAPLP----GK-----IVPEQA 548
Cdd:PRK09107 553 VANLENCFPmipsGKahnemLLPDEA 578
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-543 |
1.50e-73 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 245.50 E-value: 1.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGA 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALH-EKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 81 IHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVA 159
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVK--DAEDIPEIIKKAFYIASTGRpGPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 160 VLTLPNNILNtkvednfPTEVEPYV-PERRQPLSH---------EIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFI 227
Cdd:PRK08979 158 VIDLPKDCLN-------PAILHPYEyPESIKMRSYnpttsghkgQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 228 EKGKIPTIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAG------TNYPYVDYLPKKNIPAIQIDenPE 301
Cdd:PRK08979 231 EKLNLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGvrfddrTTNNLEKYCPNATILHIDID--PS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 302 AIGHRFDVDAPIVGDSQLALR---ALTDAIQPVEKRSFLNEMLDHRETWKG--WMTEDKNNDAspIRPERLMDAINKVMT 376
Cdd:PRK08979 309 SISKTVRVDIPIVGSADKVLDsmlALLDESGETNDEAAIASWWNEIEVWRSrnCLAYDKSSER--IKPQQVIETLYKLTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 377 DDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNL 456
Cdd:PRK08979 387 GDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 457 PMVLFVLNNSELSFIKYEQQ--EAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAV-QQHKPTIVNVYVD 533
Cdd:PRK08979 467 PVKIINLNNRFLGMVKQWQDmiYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALaMKDRLVFVDINVD 546
|
570
....*....|
gi 505961992 534 KNAAPLPGKI 543
Cdd:PRK08979 547 ETEHVYPMQI 556
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
3-538 |
2.55e-73 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 245.16 E-value: 2.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 3 KVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAenDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIH 82
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPA--GIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 83 LLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAvyNYQLKESDATRIFEIVDEAIRTAYREKGVAVLT 162
Cdd:TIGR03457 79 CVTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFT--KYQGHVRHPSRMAEVLNRCFERAWREMGPAQLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 163 LPNNILNTKVEDNFPtevEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPS 240
Cdd:TIGR03457 157 IPRDYFYGEIDVEIP---RPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAveECKALAERLGAPVVNSYLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 241 KTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNY-PY-------VDYLPkKNIPAIQIDENPEAIGHRFDVDAP 312
Cdd:TIGR03457 234 NDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFgtlpqygIDYWP-KNAKIIQVDANAKMIGLVKKVTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 313 IVGDSQLALRALTDAIQPV---------------EKRSFLNEM--LDHRETWKG--WMTEDKNNDASPIRPERLMDAINK 373
Cdd:TIGR03457 313 ICGDAKAAAAEILQRLAGKagdanraerkakiqaERSAWEQELseMTHERDPFSldMIVEQRQEEGNWLHPRQVLRELEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 374 VMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQ 453
Cdd:TIGR03457 393 AMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 454 YNLPMVLFVLNNSELSFIKYEQQE-------AGELEygidfSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQ---QH 523
Cdd:TIGR03457 473 HDIPVTAVVFRNRQWGAEKKNQVDfynnrfvGTELE-----SELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaqaEG 547
|
570
....*....|....*
gi 505961992 524 KPTIVNVYVDKNAAP 538
Cdd:TIGR03457 548 KTTVIEIVCTRELGD 562
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
10-519 |
8.46e-73 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 243.94 E-value: 8.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK06965 27 LMKALAAEGVEFIWGYPGGAVLYIYDEL-YKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGIAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNIL 168
Cdd:PRK06965 106 AYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVK--DVRDLAETVKKAFYIARTGRpGPVVVDIPKDVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 NTKVEDNFPTEVE--PYVPERRQPlSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSKTIV 244
Cdd:PRK06965 184 KTPCEYEYPKSVEmrSYNPVTKGH-SGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTLMGLGAY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 245 GDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGT--------NYPYVDYLPKKnipAIQIDENPEAIGHRFDVDAPIVGD 316
Cdd:PRK06965 263 PASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGArfddrvigNPAHFASRPRK---IIHIDIDPSSISKRVKVDIPIVGD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 317 SQLALRALTDAIQPVEKRSFLNEMLDHRETWKGWMTED---KNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWST 393
Cdd:PRK06965 340 VKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDclkYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 394 RYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKY 473
Cdd:PRK06965 420 QFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVRQ 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 505961992 474 EQqeagELEYGIDFSDI------DFAKFAEACGGVGYTLKDPKDIDSIVQTA 519
Cdd:PRK06965 500 WQ----EIEYSKRYSHSymdalpDFVKLAEAYGHVGMRIEKTSDVEPALREA 547
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-530 |
2.00e-72 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 242.60 E-value: 2.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKanM----ALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAenDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIG 76
Cdd:PRK07525 1 MGKMK--MtpseAFVETLQAHGITHAFGIIGSAFMDASDLFPPA--GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 77 GPGAIHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVynYQLKESDATRIFEIVDEAIRTAYREK 156
Cdd:PRK07525 77 GPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTK--YQEEVRDPSRMAEVLNRVFDKAKRES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 157 GVAVLTLPNNILNTKVEDNFPtevEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPT 234
Cdd:PRK07525 155 GPAQINIPRDYFYGVIDVEIP---QPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 235 IVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPY--------VDYLPkKNIPAIQIDENPEAIGHR 306
Cdd:PRK07525 232 ACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPfgtlpqygIDYWP-KDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 307 FDVDAPIVGDSQLALRALTDAIQPV----------------EKRSFLNEM--LDHRETWKG--WMTEDKNNDASPIRPER 366
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERlagdagreerkaliaaEKSAWEQELssWDHEDDDPGtdWNEEARARKPDYMHPRQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 367 LMDAINKVMTDDTVIAADVGTSTVWSTRYLNL-GVNNHFIISSWlGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVM 445
Cdd:PRK07525 391 ALREIQKALPEDAIVSTDIGNNCSIANSYLRFeKGRKYLAPGSF-GNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 446 QDFSTAVQYNLPMVLFVLNNSELSFIKYEQQE-------AGELEygidfSDIDFAKFAEACGGVGYTLKDPKDIDSIVQT 518
Cdd:PRK07525 470 NEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDfynnrfvGTELD-----NNVSYAGIAEAMGAEGVVVDTQEELGPALKR 544
|
570
....*....|....*
gi 505961992 519 AV---QQHKPTIVNV 530
Cdd:PRK07525 545 AIdaqNEGKTTVIEI 559
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
19-550 |
5.18e-72 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 241.15 E-value: 5.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 19 IDHVYGIPGDSIDAVVDGLKVAENdIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYDAKMDNVPQL 98
Cdd:PRK08155 28 IRIVTGIPGGAILPLYDALSQSTQ-IRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 99 VLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREKGVAVLT-LPNNILNTKVE-DNF 176
Cdd:PRK08155 107 CITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVR--DIEELPQVISDAFRIAQSGRPGPVWIdIPKDVQTAVIElEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 177 PTEVEPYVPErrQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTIVGDDHPYNLGN 254
Cdd:PRK08155 185 PAPAEKDAAP--AFDEESIRDAAAMINAAKRPVLYLGGGVINSGApaRARELAEKAQLPTTMTLMALGMLPKAHPLSLGM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 255 LGKIGSKPSYQAMQNADLLILAGTNYpyvD---------YLPKKNIpaIQIDENPEAIGHRFDVDAPIVGDSQLALRALT 325
Cdd:PRK08155 263 LGMHGARSTNYILQEADLLIVLGARF---DdraigkteqFCPNAKI--IHVDIDRAELGKIKQPHVAIQADVDDVLAQLL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 326 DAIQPVEKRSFLNEMLDHRETWKGWMTEDKNndasPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFI 405
Cdd:PRK08155 338 PLVEAQPRAEWHQLVADLQREFPCPIPKADD----PLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 406 ISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIkYEQQEA--GELEY 483
Cdd:PRK08155 414 TSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLV-HQQQSLfyGQRVF 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505961992 484 GIDFS-DIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPgkIVPEQAIN 550
Cdd:PRK08155 493 AATYPgKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP--MVPPGAAN 558
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
19-543 |
1.17e-71 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 240.52 E-value: 1.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 19 IDHVYGIPGDSIDAVVDGLKVAeNDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYDAKMDNVPQL 98
Cdd:PRK07979 19 VKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 99 VLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKESDatRIFEIVDEAIRTAYREK-GVAVLTLPNNILNtkvednfP 177
Cdd:PRK07979 98 VLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTE--DIPQVLKKAFWLAASGRpGPVVVDLPKDILN-------P 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 178 TEVEPYV-PERRQPLSH---------EIQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGKIPTIVTLPSKTIVG 245
Cdd:PRK07979 169 ANKLPYVwPESVSMRSYnpttqghkgQIKRALQTLVAAKKPVVYVGGGaiNAACHQQLKELVEKLNLPVVSSLMGLGAFP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 246 DDHPYNLGNLGKIGSKPSYQAMQNADLLILAG------TNYPYVDYLPkkNIPAIQIDENPEAIGHRFDVDAPIVGDSQL 319
Cdd:PRK07979 249 ATHRQSLGMLGMHGTYEANMTMHNADVIFAVGvrfddrTTNNLAKYCP--NATVLHIDIDPTSISKTVTADIPIVGDARQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 320 ALRALTDAIQPVEKRSFLNEMLD---HRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYL 396
Cdd:PRK07979 327 VLEQMLELLSQESAHQPLDEIRDwwqQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 397 NLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQ- 475
Cdd:PRK07979 407 PFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQd 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505961992 476 -QEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTA---VQQHKPTIVNVYVDKNAAPLPGKI 543
Cdd:PRK07979 487 mIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEAleqVRNNRLVFVDVTVDGSEHVYPMQI 558
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
9-167 |
2.89e-71 |
|
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: 225.89 E-value: 2.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:cd07039 5 VIVETLENWGVKRVYGIPGDSINGLMDALR-REGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGLY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREKGVAVLTLPNNI 167
Cdd:cd07039 84 DAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETV--TSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
9-544 |
2.15e-67 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 228.36 E-value: 2.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK08266 9 AIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGAALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGtKAFQEvdLPKLFEDVAVYNYQLKESDatRIfEIVDEA---IRTAYRE-----KGVAV 160
Cdd:PRK08266 89 TAYGCNSPVLCLTGQIPSALIG-KGRGH--LHEMPDQLATLRSFTKWAE--RI-EHPSEApalVAEAFQQmlsgrPRPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 161 LTLPNNILNTKVEDNFPTEVEPyvPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTLPS 240
Cdd:PRK08266 163 LEMPWDVFGQRAPVAAAPPLRP--APPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 241 KTIVGDDHPYNLGNLGkigskpSYQAMQNADLLILAGTN----YPYVDYLPKkNIPAIQIDENPEAIGhRFDVDAPIVGD 316
Cdd:PRK08266 241 RGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRlelpTFRWPWRPD-GLKVIRIDIDPTEMR-RLKPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 317 SQLALRALTDAI-QPVEKRSFLNEMLdhREtwkgwMTEDKNNDASPIRPER-LMDAINKVMTDDTVIAADVgtSTVWSTR 394
Cdd:PRK08266 313 AKAGTAALLDALsKAGSKRPSRRAEL--RE-----LKAAARQRIQAVQPQAsYLRAIREALPDDGIFVDEL--SQVGFAS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 395 YLNLGVN--NHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIK 472
Cdd:PRK08266 384 WFAFPVYapRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505961992 473 YEQQEA-GELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGKIV 544
Cdd:PRK08266 464 RDQKRRfGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASPWPFI 536
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
9-538 |
1.90e-66 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 226.57 E-value: 1.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYG--IPgdsiDAVVdgLKVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNG 86
Cdd:PRK06112 19 AIARALKRHGVEQIFGqsLP----SALF--LAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 87 MYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREK-GVAVLTLPN 165
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRV--TVAERIDDYVDQAFTAATSGRpGPVVLLLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 166 NILNTKVEDNFP---TEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTdH---AKAEVREFIEKGKIPTIVTLP 239
Cdd:PRK06112 171 DLLTAAAAAPAAprsNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGV-HisgASAALAALQSLAGLPVATTNM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 240 SKTIVGDDHPYNLGNLG-----KIGSKPSYQAMQNADLLILAG--TNYPYVD--YLPKKNIPAIQIDENPEAIGHRFDVd 310
Cdd:PRK06112 250 GKGAVDETHPLSLGVVGslmgpRSPGRHLRDLVREADVVLLVGtrTNQNGTDswSLYPEQAQYIHIDVDGEEVGRNYEA- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 311 APIVGDSQLALRALTDAIQPVE------KRSFLNEML-DHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAA 383
Cdd:PRK06112 329 LRLVGDARLTLAALTDALRGRDlaaragRRAALEPAIaAGREAHREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 384 DVGTSTVWSTRYLN-LGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFV 462
Cdd:PRK06112 409 DASYSSIWVANFLTaRRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVV 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 463 LNNSELSFikyeQQEAGELEYG-----IDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAA 537
Cdd:PRK06112 489 LNNGILGF----QKHAETVKFGthtdaCHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDPSAF 564
|
.
gi 505961992 538 P 538
Cdd:PRK06112 565 P 565
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-543 |
2.69e-66 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 225.95 E-value: 2.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENdIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGA 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGG-IEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 81 IHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVA 159
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVK--NAEDIPSTIKKAFYIASTGRpGPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 160 VLTLPNNILN--TKVEDNFPTEVE--PYVPERrQPLSHEIQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGKIP 233
Cdd:PRK06882 158 VIDIPKDMVNpaNKFTYEYPEEVSlrSYNPTV-QGHKGQIKKALKALLVAKKPVLFVGGGviTAECSEQLTQFAQKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 234 TIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAG------TNYPYVDYLPkkNIPAIQIDENPEAIGHRF 307
Cdd:PRK06882 237 VTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGvrfddrTTNNLAKYCP--NAKVIHIDIDPTSISKNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 308 DVDAPIVGDSQLALR---ALTDAIQPVEKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAAD 384
Cdd:PRK06882 315 PAYIPIVGSAKNVLEeflSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 385 VGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLN 464
Cdd:PRK06882 395 VGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 465 NSELSFIKYEQqeagELEYGIDFSDI------DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQ-QHKPTIVNVYVDKNAA 537
Cdd:PRK06882 475 NRFLGMVKQWQ----DLIYSGRHSQVymnslpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSiKDKLVFVDVNVDETEH 550
|
....*.
gi 505961992 538 PLPGKI 543
Cdd:PRK06882 551 VYPMQI 556
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-533 |
3.34e-58 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 204.44 E-value: 3.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 1 MGKVKANMALVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLT-GKIAVSLAIGGPG 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMR-KHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 80 AIHLLNGMYDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKE-SDATRIFEivdEAIRTAyRE--K 156
Cdd:PRK11269 80 GTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREpALVPRVFQ---QAFHLM-RSgrP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 157 GVAVLTLPNNILNTKVEdnF-PTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIP 233
Cdd:PRK11269 156 GPVLIDLPFDVQVAEIE--FdPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADAsdLLVEFAELTGVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 234 TIVTLPSKTIVGDDHPYNLGNLGkIGSKPSY--QAMQNADLLILAGTNYP-----YVD-YlpKKNIPAIQIDENPEAIGH 305
Cdd:PRK11269 234 VIPTLMGWGAIPDDHPLMAGMVG-LQTSHRYgnATLLASDFVLGIGNRWAnrhtgSVEvY--TKGRKFVHVDIEPTQIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 306 RFDVDAPIVGDSQLALRALTDAIQPVEKRSFLNEmldhRETW-------KGWMTEDKNNDASPIRPERLMDAINKVMTDD 378
Cdd:PRK11269 311 VFGPDLGIVSDAKAALELLVEVAREWKAAGRLPD----RSAWvadcqerKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 379 TVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPM 458
Cdd:PRK11269 387 TCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 459 VLFVLNNSELSFIK---------------YEQQEAGELE-YGidfsdIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQ 522
Cdd:PRK11269 467 IHVLVNNAYLGLIRqaqrafdmdycvqlaFENINSPELNgYG-----VDHVKVAEGLGCKAIRVFKPEDIAPALEQAKAL 541
|
570
....*....|.
gi 505961992 523 HKPTIVNVYVD 533
Cdd:PRK11269 542 MAEFRVPVVVE 552
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
11-537 |
1.16e-56 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 199.18 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 11 VSALKAWDIDHVYGIPGDSIDAVVDGLKvaENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYDA 90
Cdd:PRK05858 12 ARRLKAHGVDTMFTLSGGHLFPLYDGAR--EEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 91 KMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYR-EKGVAVLTLPNNILN 169
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATA--QSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 170 TKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGT--DHAKAEVREFIEKGKIPTIVTLPSKTIVGDD 247
Cdd:PRK05858 168 SMADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVwwGHAEAALLRLAEELGIPVLMNGMGRGVVPAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 248 HPYNLgnlgkigSKPSYQAMQNADLLILAGTnyP------YVDYLPKKniPAIQIDENPEAIGHRFDVDAPIVGDSQLAL 321
Cdd:PRK05858 248 HPLAF-------SRARGKALGEADVVLVVGV--PmdfrlgFGVFGGTA--QLVHVDDAPPQRAHHRPVAAGLYGDLSAIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 322 RALTDAI-QPVEKRSFLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGV 400
Cdd:PRK05858 317 SALAGAGgDRTDHQGWIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 401 NNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQeage 480
Cdd:PRK05858 397 PGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPME---- 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505961992 481 LEYGIDFS-----DIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAA 537
Cdd:PRK05858 473 ALYGYDVAadlrpGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSVA 534
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
10-540 |
7.76e-52 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 187.25 E-value: 7.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PLN02470 19 LVEALEREGVDTVFAYPGGASMEIHQAL-TRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEA--IRTAYREKGVAV------- 160
Cdd:PLN02470 98 ALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVM--DVEDIPRVIREAffLASSGRPGPVLVdipkdiq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 161 --LTLPNniLNTKVEDNFPTEVEPYVPERRQplsheIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVTL 238
Cdd:PLN02470 176 qqLAVPN--WNQPMKLPGYLSRLPKPPEKSQ-----LEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 239 PSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADLLILAGTNYPyvDYLPKK------NIPAIQIDENPEAIGHRFDVDAP 312
Cdd:PLN02470 249 MGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFD--DRVTGKleafasRASIVHIDIDPAEIGKNKQPHVS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 313 IVGDSQLALRALT-----DAIQPVEKRSFLNEMLDHRETWKgwMTEDKNNDAspIRPERLMDAINKVMTDDTVIAADVGT 387
Cdd:PLN02470 327 VCADVKLALQGLNklleeRKAKRPDFSAWRAELDEQKEKFP--LSYPTFGDA--IPPQYAIQVLDELTDGNAIISTGVGQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 388 STVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSE 467
Cdd:PLN02470 403 HQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQH 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 468 LSFIKYEQQEAGELEYGIDF-------SDI--DFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAP 538
Cdd:PLN02470 483 LGMVVQWEDRFYKANRAHTYlgdpdaeAEIfpDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHV 562
|
..
gi 505961992 539 LP 540
Cdd:PLN02470 563 LP 564
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
9-539 |
8.98e-49 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 177.47 E-value: 8.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLkvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK07524 7 ALVRLLEAYGVETVFGIPGVHTVELYRGL--AGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSG--QADSHKLGTKAFQEvdLPK---LFEDVAVYNYQLKESDA-----TRIFEIVDEA-IRTAYREKG 157
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHE--LPDqraMVAGVAAFSHTLMSAEDlpevlARAFAVFDSArPRPVHIEIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 158 VAVLTLPNNILNTKvednfptevEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGKIPTIVT 237
Cdd:PRK07524 163 LDVLAAPADHLLPA---------PPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 238 LPSKTIVGDDHPYNlgnlgkIGSKPSYQA----MQNADLLILAGTNYPYVDY-------LPkknIPA--IQIDENPEAIG 304
Cdd:PRK07524 234 INAKGLLPAGHPLL------LGASQSLPAvralIAEADVVLAVGTELGETDYdvyfdggFP---LPGelIRIDIDPDQLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 305 HRFDVDAPIVGDSQLALRALTDAIQPVEKRSF--------LNEMLdhRETWKGWMtedknndaspiRPE-RLMDAINKVM 375
Cdd:PRK07524 305 RNYPPALALVGDARAALEALLARLPGQAAAADwgaarvaaLRQAL--RAEWDPLT-----------AAQvALLDTILAAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 376 TDDTViaadVGTST--VWSTrylNLGVNNH-----FIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDF 448
Cdd:PRK07524 372 PDAIF----VGDSTqpVYAG---NLYFDADaprrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPEL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 449 STAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIV 528
Cdd:PRK07524 445 ASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLI 524
|
570
....*....|.
gi 505961992 529 NVYVDKNAAPL 539
Cdd:PRK07524 525 EVDQACWFAAV 535
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
9-530 |
6.15e-48 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 175.56 E-value: 6.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPgdSI------DAVVdglkvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIH 82
Cdd:PRK07064 8 LIAAFLEQCGVKTAFGVI--SIhnmpilDAIG-----RRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 83 LLNGMYDAKMDNVPQLVLSGQADSHKLGTKA--FQEV-DLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREK-GV 158
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRV--RSAETALATIREAVRVALTAPtGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 159 AVLTLPNNILNTKVEdnFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKAEVREFIEKGkIPTIVTL 238
Cdd:PRK07064 159 VSVEIPIDIQAAEIE--LPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLG-FGVVTST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 239 PSKTIVGDDHPYNLGNLGkiGSKPSYQAMQNADLLILAGTNY------PYVDYLPKkniPAIQIDENPEAIGHRFDVDAP 312
Cdd:PRK07064 236 QGRGVVPEDHPASLGAFN--NSAAVEALYKTCDLLLVVGSRLrgnetlKYSLALPR---PLIRVDADAAADGRGYPNDLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 313 IVGDSQLALRALTDAIQPVEK--RSFLNEMLDHRETWKGWMTEDKNNDAspirpeRLMDAINKVMTDDTVIAADVGTS-T 389
Cdd:PRK07064 311 VHGDAARVLARLADRLEGRLSvdPAFAADLRAAREAAVADLRKGLGPYA------KLVDALRAALPRDGNWVRDVTISnS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 390 VWSTRYLNLGVNNHFIiSSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELS 469
Cdd:PRK07064 385 TWGNRLLPIFEPRANV-HALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505961992 470 FIKYEQQEA-GELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNV 530
Cdd:PRK07064 464 VIRNIQDAQyGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
366-532 |
6.26e-48 |
|
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: 164.74 E-value: 6.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 366 RLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVM 445
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 446 QDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGEL-EYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHK 524
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 505961992 525 PTIVNVYV 532
Cdd:cd00568 161 PALIEVKT 168
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
19-538 |
6.85e-48 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 175.35 E-value: 6.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 19 IDHVYGIPGDSI----DAVVDGlkvaeNDIDFIHVRHEEVASLAAAAYTKLTGkIAVSLAIGGPGAIHLLNGMYDAKMDN 94
Cdd:COG3961 20 IRHIFGVPGDYNlpflDAIEAH-----PGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 95 VPQLVLSG------QAD----SHKLGTKAFqEVDLpKLFEDVAVYNYQLKESDATRifEIvDEAIRTAYREKGVAVLTLP 164
Cdd:COG3961 94 VPVVHIVGapgtraQRRgpllHHTLGDGDF-DHFL-RMFEEVTVAQAVLTPENAAA--EI-DRVLAAALREKRPVYIELP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 165 NNILNTKVEDNFPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTD--HAKAEVREFIEKGKIPTIVTLPSKT 242
Cdd:COG3961 169 RDVADAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHrfGLQEELLALAEKTGIPVATTLLGKS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 243 IVGDDHPYNLGN-LGKIGSKPSYQAMQNADLLILAGTNYpyVDY--------LPKKNIpaiqIDENPEAI---GHRFdvd 310
Cdd:COG3961 249 VLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF--TDTntggftaqLDPERT----IDIQPDSVrvgGHIY--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 311 API-VGDsqlALRALTDAiqpVEKRSFlnemldHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADVGTST 389
Cdd:COG3961 320 PGVsLAD---FLEALAEL---LKKRSA------PLPAPAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 390 VWSTRyLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSels 469
Cdd:COG3961 388 FGAAD-LRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNND--- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 470 fikyeqqeaGeleYGI---------DFSDI---DFAKFAEACGG---VGYTLKDPKDIDSIVQTAVQQHK-PTIVNVYVD 533
Cdd:COG3961 464 ---------G---YTIeraihgpdgPYNDIanwDYAKLPEAFGGgnaLGFRVTTEGELEEALAAAEANTDrLTLIEVVLD 531
|
....*
gi 505961992 534 KNAAP 538
Cdd:COG3961 532 KMDAP 536
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
384-530 |
4.22e-47 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 161.98 E-value: 4.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 384 DVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVL 463
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505961992 464 NNSELSFIKYEQQEAGE----LEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNV 530
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGgrysGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-524 |
1.11e-45 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 169.61 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 5 KANMALVSALKAWDIDHVYGIPGDS-IDAVvdglkvAENDIDFIHVRHEEVASLAAAAYTKLTG--KIAVSLAIGGPGAI 81
Cdd:PRK06154 21 KVAEAVAEILKEEGVELLFGFPVNElFDAA------AAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 82 HLLNGMYDAKMDNVPQLVLSGQADSHKlgtkafqeVDLPKLFEDVAVYNYQLKESDATRIFEIVDEAIRTAYRE-----K 156
Cdd:PRK06154 95 NAFGGVAQAYGDSVPVLFLPTGYPRGS--------TDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRlrngrP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 157 GVAVLTLPNNILNTKVEDNfPTEVEPYVPERRQPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPT 234
Cdd:PRK06154 167 GPVVLELPVDVLAEELDEL-PLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQAtpELKELAELLEIPV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 235 IVTLPSKTIVGDDHPYNLGNLGKigSKPSYQA--MQNADLLILAGTNYPYVDY---LPK-KNIpaIQIDENPEAIGHRFD 308
Cdd:PRK06154 246 MTTLNGKSAFPEDHPLALGSGGR--ARPATVAhfLREADVLFGIGCSLTRSYYglpMPEgKTI--IHSTLDDADLNKDYP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 309 VDAPIVGDSQLALRALTDAI------QPVEKRSFLNEMLDHRETW-KGWMTEDKNNDAsPIRPER----LMDAINKvmtD 377
Cdd:PRK06154 322 IDHGLVGDAALVLKQMIEELrrrvgpDRGRAQQVAAEIEAVRAAWlAKWMPKLTSDST-PINPYRvvweLQHAVDI---K 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 378 DTVIAADVGT-----STVWSTR----YLNLGVNNHfiisswlgtMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDF 448
Cdd:PRK06154 398 TVIITHDAGSprdqlSPFYVASrpgsYLGWGKTTQ---------LGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDF 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505961992 449 STAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSDiDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHK 524
Cdd:PRK06154 469 ETAVRERIPILTILLNNFSMGGYDKVMPVSTTKYRATDISG-DYAAIARALGGYGERVEDPEMLVPALLRALRKVK 543
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
10-543 |
1.22e-44 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 166.70 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIdavVDGLKVAE-NDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPI---TDLARLAQaEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKlgtkafqeVDLPK-LFEDVAVYNYQ---LKEsdATRIFEIVD------EAIRTAY--REK 156
Cdd:PRK09259 93 NATTNCFPMIMISGSSEREI--------VDLQQgDYEELDQLNAAkpfCKA--AFRVNRAEDigigvaRAIRTAVsgRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 157 GVaVLTLPNNILNTKV--EDNFPTEVEPYVPERRQPLSHE-IQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGK 231
Cdd:PRK09259 163 GV-YLDLPAKVLAQTMdaDEALTSLVKVVDPAPAQLPAPEaVDRALDLLKKAKRPLIILGKGAAYAQAdeQIREFVEKTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 232 IPTIVTLPSKTIVGDDHPYNlgnlgkIGSKPSYqAMQNADLLILAGTNypyVDYL------PKKNIPA--IQIDENPEAI 303
Cdd:PRK09259 242 IPFLPMSMAKGLLPDTHPQS------AAAARSL-ALANADVVLLVGAR---LNWLlshgkgKTWGADKkfIQIDIEPQEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 304 GHRFDVDAPIVGDSQLALRALTDAI--QPVEKRS-FLNEMLDHRETWKGWMTEDKNNDASPIRPERLMDAINKVMTDD-T 379
Cdd:PRK09259 312 DSNRPIAAPVVGDIGSVMQALLAGLkqNTFKAPAeWLDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKENpD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 380 VIAADVGTSTvwstryLNLGVNnhfIIS-----------SWlGTMGCALPTAIASRIAfPGRQVIGITGDGAFEMVMQDF 448
Cdd:PRK09259 392 IYLVNEGANT------LDLARN---IIDmykprhrldcgTW-GVMGIGMGYAIAAAVE-TGKPVVAIEGDSAFGFSGMEV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 449 STAVQYNLPMVLFVLNNSELsfikYEQQEAgELEYGIDFSDIDFA------KFAEACGGVGYTLKDPKDIDSIVQTAVQQ 522
Cdd:PRK09259 461 ETICRYNLPVTVVIFNNGGI----YRGDDV-NLSGAGDPSPTVLVhharydKMMEAFGGVGYNVTTPDELRHALTEAIAS 535
|
570 580
....*....|....*....|.
gi 505961992 523 HKPTIVNVYVDKNAAPLPGKI 543
Cdd:PRK09259 536 GKPTLINVVIDPAAGTESGHI 556
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
362-545 |
8.80e-44 |
|
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: 154.19 E-value: 8.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 362 IRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAF 441
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 442 EMVMQDFSTAVQYNLPMVLFVLNNSELSFIKyeQQEagELEYGIDFS------DIDFAKFAEACGGVGYTLKDPKDIDSI 515
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVR--QWQ--ELFYEGRYShttldsNPDFVKLAEAYGIKGLRVEKPEELEAA 156
|
170 180 190
....*....|....*....|....*....|
gi 505961992 516 VQTAVQQHKPTIVNVYVDKNAAPLPgkIVP 545
Cdd:cd02015 157 LKEALASDGPVLLDVLVDPEENVLP--MVP 184
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
9-164 |
2.13e-41 |
|
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: 146.52 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLkvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDAL--ARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYRE-KGVAVLTLP 164
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVT--SPEEIPEALRRAFRIALSGrPGPVALDLP 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
9-174 |
3.07e-41 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 146.61 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMY 88
Cdd:pfam02776 4 ALADVLKALGVDTVFGVPGGHILPLLDAL-AKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 89 DAKMDNVPQLVLSGQADSHKLGTKAFQ-EVDLPKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTA-YREKGVAVLTLPNN 166
Cdd:pfam02776 83 NAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRV--TSADEIPEVLRRAFRAAlSGRPGPVYLEIPLD 160
|
....*...
gi 505961992 167 ILNTKVED 174
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
9-534 |
1.19e-40 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 155.54 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 9 ALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAENDI----DFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLL 84
Cdd:PRK08327 12 LFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 85 NGMYDAKMDNVPQLVLSGQA---DSHKLGTKA-----FQEV-DLPKLFEDVAVYNYQLKESDatRIFEIVDEAIRTAYRE 155
Cdd:PRK08327 92 GGVHNAARSRIPVLVFAGRSpytEEGELGSRNtrihwTQEMrDQGGLVREYVKWDYEIRRGD--QIGEVVARAIQIAMSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 156 -KGVAVLTLPNNILNTKVEDNFPTEvEPYVPERRQPLSHE-IQRAAQLFNESKRPVILVGKG--TDHAKAEVREFIEKGK 231
Cdd:PRK08327 170 pKGPVYLTLPREVLAEEVPEVKADA-GRQMAPAPPAPDPEdIARAAEMLAAAERPVIITWRAgrTAEGFASLRRLAEELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 232 IPTI------VTLPSktivgdDHPYNLGNLGKIGskpsyqaMQNADLLILAGTNYPYVdylPKKNIPA-----IQIDENP 300
Cdd:PRK08327 249 IPVVeyagevVNYPS------DHPLHLGPDPRAD-------LAEADLVLVVDSDVPWI---PKKIRPDadarvIQIDVDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 301 --EAIGHR-FDVDAPIVGDSQLALRALTDAIQPV------EKRSFLNEMLDHRETW-KGWMTE-DKNNDASPIRPERLMD 369
Cdd:PRK08327 313 lkSRIPLWgFPCDLCIQADTSTALDQLEERLKSLasaerrRARRRRAAVRELRIRQeAAKRAEiERLKDRGPITPAYLSY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 370 AINKVMTDDTVIAADVGTstVWstRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEmvmqdFS 449
Cdd:PRK08327 393 CLGEVADEYDAIVTEYPF--VP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFI-----FG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 450 T-------AVQYNLPMVLFVLNNSELSFIK------YEQQEAGELEY--GIDFS-DIDFAKFAEACGGVGYTLKDPKDID 513
Cdd:PRK08327 464 VpeaahwvAERYGLPVLVVVFNNGGWLAVKeavlevYPEGYAARKGTfpGTDFDpRPDFAKIAEAFGGYGERVEDPEELK 543
|
570 580
....*....|....*....|....*
gi 505961992 514 SIVQTAV----QQHKPTIVNVYVDK 534
Cdd:PRK08327 544 GALRRALaavrKGRRSAVLDVIVDR 568
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
195-324 |
3.42e-40 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 142.70 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 195 IQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTIVTLPSKTIVGDDHPYNLGNLGKIGSKPSYQAMQNADL 272
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGAseELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 505961992 273 LILAGTNY-------PYVDYLPKKNIpaIQIDENPEAIGHRFDVDAPIVGDSQLALRAL 324
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAPDAKI--IHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
364-533 |
7.72e-39 |
|
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: 140.50 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 364 PERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEM 443
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 444 VMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQH 523
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|
gi 505961992 524 KPTIVNVYVD 533
Cdd:cd02010 161 GVHVIDCPVD 170
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
364-533 |
3.77e-35 |
|
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: 130.34 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 364 PERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEM 443
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 444 VMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELE--YGIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQ 521
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGlpVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 505961992 522 QHKPTIVNVYVD 533
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
360-536 |
4.54e-27 |
|
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: 108.37 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 360 SPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDG 439
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 440 AFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQE-------AGELEygidfsDIDFAKFAEACGGVGYTLKDPKDI 512
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDfynnrfvGTELE------SESFAKIAEACGAKGITVDKPEDV 155
|
170 180
....*....|....*....|....*..
gi 505961992 513 DSIVQTAVQQH---KPTIVNVYVDKNA 536
Cdd:cd02013 156 GPALQKAIAMMaegKTTVIEIVCDQEL 182
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-164 |
1.09e-23 |
|
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: 97.42 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 8 MALVSALKAWDIDHVYGIPGDSIDAVVDGLKVAEnDIDFIHVRHEEVASLAAAAYTKLTGKIAVsLAIGGPGAIHLLNGM 87
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGD-KRIIDTVIHELGAAGAAAGYARAGGPPVV-IVTSGTGLLNAINGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 88 YDAKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKeSDATRIFEIvDEAIRTAYREKGVAVLTLP 164
Cdd:cd06586 79 ADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSP-SPAELPAGI-DHAIRTAYASQGPVVVRLP 153
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
14-533 |
6.78e-23 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 102.34 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 14 LKAWDIDHVYGIPGDSIDAVVDGLKvaeNDIDFIHVRHEEVASLAAAAYTKLTGKIA-VSL-AIGGPGaiHLLNGMYDAK 91
Cdd:PRK07092 22 LRRFGITTVFGNPGSTELPFLRDFP---DDFRYVLGLQEAVVVGMADGYAQATGNAAfVNLhSAAGVG--NAMGNLFTAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 92 MDNVPQLVLSGQADSHKLGTKAF----QEVDLPKLFedvavynyqLKESDATRIFEIVDEAIRTAYRE-----KGVAVLT 162
Cdd:PRK07092 97 KNHTPLVITAGQQARSILPFEPFlaavQAAELPKPY---------VKWSIEPARAEDVPAAIARAYHIamqppRGPVFVS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 163 LPnnilntkvEDNFPTEVEPyVPERR-----QPLSHEIQRAAQLFNESKRPVILVGKGTDHAKA--EVREFIEKGKIPTI 235
Cdd:PRK07092 168 IP--------YDDWDQPAEP-LPARTvssavRPDPAALARLGDALDAARRPALVVGPAVDRAGAwdDAVRLAERHRAPVW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 236 VT-LPSKTIVGDDHPYNLGNLGKIGSKPSyQAMQNADLLILAGTN-YPYVDYLPKKNIPA----IQIDENPEAIGhRFDV 309
Cdd:PRK07092 239 VApMSGRCSFPEDHPLFAGFLPASREKIS-ALLDGHDLVLVIGAPvFTYHVEGPGPHLPEgaelVQLTDDPGEAA-WAPM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 310 DAPIVGDSQLALRALTDAIQPVeKRSflneMLDHREtwkgwMTEDKNNDASPIRPERLMDAINKVMTDDTVIAADV-GTS 388
Cdd:PRK07092 317 GDAIVGDIRLALRDLLALLPPS-ARP----APPARP-----MPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEApSTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 389 TVWSTRYLNLGVNNHFIISSwlGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSel 468
Cdd:PRK07092 387 PAMQEHLPMRRQGSFYTMAS--GGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNG-- 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505961992 469 sfiKYE--QQEAGELEY----GIDFSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD 533
Cdd:PRK07092 463 ---RYGalRWFAPVFGVrdvpGLDLPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
362-532 |
1.85e-21 |
|
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: 91.89 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 362 IRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLG-VNNHFIISSwlGTMGCALPTAIASRIAFPGRQVIGITGDGA 440
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTrPGSYFTLRG--GGLGWGLPAAVGAALANPDRKVVAIIGDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 441 FEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQ--------EAGELEYGIDFSDIDFAKFAEACGGVGYTLKDPKDI 512
Cdd:cd02002 79 FMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKrvgpegpgENAPDGLDLLDPGIDFAAIAKAFGVEAERVETPEEL 158
|
170 180
....*....|....*....|
gi 505961992 513 DSIVQTAVQQHKPTIVNVYV 532
Cdd:cd02002 159 DEALREALAEGGPALIEVVV 178
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-538 |
6.19e-21 |
|
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: 90.29 E-value: 6.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 361 PIRPERLMDAINKVMTDDTVIAADVGTSTvWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGA 440
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 441 FEMVMQDFSTAVQYNLPMVLFVLNNSELS---FIKYEQQEageleygidFSDI---DFAKFAEACG----GVGYTLKDPK 510
Cdd:cd02005 80 FQMTVQELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS---------YNDIanwNYTKLPEVFGggggGLSFRVKTEG 150
|
170 180
....*....|....*....|....*....
gi 505961992 511 DIDSIVQTAVQQH-KPTIVNVYVDKNAAP 538
Cdd:cd02005 151 ELDEALKDALFNRdKLSLIEVILPKDDAP 179
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
358-534 |
5.54e-20 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 88.49 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 358 DASPIRPERLMDAINKVMTDDTVIAADVGTSTVWSTRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITG 437
Cdd:cd02006 4 DDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 438 DGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKyEQQEAGELEYGID--FSDI----------DFAKFAEACGGVGYT 505
Cdd:cd02006 84 DYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIR-QAQRAFDMDYQVNlaFENInsselggygvDHVKVAEGLGCKAIR 162
|
170 180 190
....*....|....*....|....*....|...
gi 505961992 506 LKDPKDIDSIVQTA---VQQHK-PTIVNVYVDK 534
Cdd:cd02006 163 VTKPEELAAAFEQAkklMAEHRvPVVVEAILER 195
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
370-542 |
4.00e-16 |
|
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: 77.35 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 370 AINKVMTDDTVIAADVGT-----STVWSTRYLNlGVNNHFIISswlgTMGCALPTAIASRIAFPGRQVIGITGDGAFEMV 444
Cdd:cd02003 7 ALNEAIGDDDVVINAAGSlpgdlHKLWRARTPG-GYHLEYGYS----CMGYEIAAGLGAKLAKPDREVYVLVGDGSYLML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 445 MQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYGIDFSD--------------IDFAKFAEACGGVGYTLKDPK 510
Cdd:cd02003 82 HSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDrdqesgqldgallpVDFAANARSLGARVEKVKTIE 161
|
170 180 190
....*....|....*....|....*....|..
gi 505961992 511 DIDSIVQTAVQQHKPTIVNVYVDKNAAPLPGK 542
Cdd:cd02003 162 ELKAALAKAKASDRTTVIVIKTDPKSMTPGYG 193
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
22-465 |
6.28e-15 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 77.82 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 22 VYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKL--TGKIAVSLAIGGPGAIHLLNGMYDakmDNVPQLV 99
Cdd:PLN02573 34 VFSVPGDFNLTLLDHL-IAEPGLNLIGCCNELNAGYAADGYARArgVGACVVTFTVGGLSVLNAIAGAYS---ENLPVIC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 100 LSGQADSHKLGT-----------------KAFQEVDLPKlfedvAVYNYQlkeSDAtriFEIVDEAIRTAYREKGVAVLT 162
Cdd:PLN02573 110 IVGGPNSNDYGTnrilhhtiglpdfsqelRCFQTVTCYQ-----AVINNL---EDA---HELIDTAISTALKESKPVYIS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 163 LPNNILNTkVEDNFPTEVEPYV--PERRQPLSHE--IQRAAQLFNESKRPVILVGKGTDHAKAeVREFIEKGKIP--TIV 236
Cdd:PLN02573 179 VSCNLAAI-PHPTFSREPVPFFltPRLSNKMSLEaaVEAAAEFLNKAVKPVLVGGPKLRVAKA-CKAFVELADASgyPVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 237 TLPS-KTIVGDDHPYNLGNL-GKIGSKPSYQAMQNADLLILAG---TNYPYVDY--LPKKNiPAIQIDENPEAIGHRfdv 309
Cdd:PLN02573 257 VMPSaKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGpifNDYSSVGYslLLKKE-KAIIVQPDRVTIGNG--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 310 daPIVGDSQLA--LRALTDAIQPVE------KRSFLNEmldhRETWKGWMTEdknndasPIRPERLMDAINKVMTDDTVI 381
Cdd:PLN02573 333 --PAFGCVLMKdfLEALAKRVKKNTtayenyKRIFVPE----GEPLKSEPGE-------PLRVNVLFKHIQKMLSGDTAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 382 AADVGTStvW-STRYLNLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVL 460
Cdd:PLN02573 400 IAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSII 477
|
....*
gi 505961992 461 FVLNN 465
Cdd:PLN02573 478 FLINN 482
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
10-156 |
1.80e-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: 62.51 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLkVAENDIDFIHVRHEEVASLAAAAYTKLTGkIAVSLAIGGPGAIHLLNGMYD 89
Cdd:cd07038 3 LLERLKQLGVKHVFGVPGDYNLPLLDAI-EENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 90 AKMDNVPQLVLSGQADS----------HKLGTKAFQeVDLpKLFEDVAVYNYQLkeSDATRIFEIVDEAIRTAYREK 156
Cdd:cd07038 81 AYAEHVPVVHIVGAPSTkaqasglllhHTLGDGDFD-VFL-KMFEEITCAAARL--TDPENAAEEIDRVLRTALRES 153
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
51-500 |
6.72e-11 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 64.87 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 51 HEEVASLAAAAYTKLTGKIAVSLAIGGPGaihLLNG---MYDAKMDNVPQLVLSGQ-ADSHKlgtkafqEVDLPkLFEDV 126
Cdd:PRK07586 47 FEGVATGAADGYARMAGKPAATLLHLGPG---LANGlanLHNARRARTPIVNIVGDhATYHR-------KYDAP-LTSDI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 127 A-----VYNYQLKESDATRIFEIVDEAIRTAYREKG-VAVLTLPnniLNTKVEDNFPTEVEPYVPERRQPLSHEIQRAAQ 200
Cdd:PRK07586 116 EalarpVSGWVRRSESAADVAADAAAAVAAARGAPGqVATLILP---ADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 201 LFNESKRPVILVGKGTDHAKAE-----------VREFIEkgkiptivTLPSKTIVGDDHPYnlgnLGKIG--SKPSYQAM 267
Cdd:PRK07586 193 ALRSGEPTVLLLGGRALRERGLaaaariaaatgARLLAE--------TFPARMERGAGRPA----VERLPyfAEQALAQL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 268 QNADLLILAGTNYP--YVDYLPKKNIPAiqidenPEaiGHRFDVDAPIVGDSQLALRALTDAIQPVEKRSFLnemldhre 345
Cdd:PRK07586 261 AGVRHLVLVGAKAPvaFFAYPGKPSRLV------PE--GCEVHTLAGPGEDAAAALEALADALGAKPAAPPL-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 346 twkgwmtedknndASPIRPER---------LMDAINKVMTDDTVIAADVGTSTVWSTRYLnLGVNNHFIISSWLGTMGCA 416
Cdd:PRK07586 325 -------------AAPARPPLptgaltpeaIAQVIAALLPENAIVVDESITSGRGFFPAT-AGAAPHDWLTLTGGAIGQG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 417 LPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVLFVLNNSELSFIKYEQQEAGELEYG--------IDFS 488
Cdd:PRK07586 391 LPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmldLDDP 470
|
490
....*....|..
gi 505961992 489 DIDFAKFAEACG 500
Cdd:PRK07586 471 DLDWVALAEGMG 482
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
10-500 |
7.77e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 58.35 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 10 LVSALKAWDIDHVYGIPGDSIDAVVDGLKvAENDIDFIHVRHEEVASLAAAAYTKLTGKIAVSLAIGGPGAIHLLNGMYD 89
Cdd:PRK12474 11 VVDTLLNCGVEVCFANPGTSEMHFVAALD-RVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLANLHN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 90 AKMDNVPQLVLSGQADSHKLGTKAFQEVDLPKLFEDVAVYNYQLKesDATRIFEIVDEAIRTAYREK-GVAVLTLPNNIL 168
Cdd:PRK12474 90 ARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSA--SAGAVDSDVARAVQAAQSAPgGIATLIMPADVA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 169 -NTKVEDNFPteVEPYVPERRQPLSheIQRAAQLFNESKRPVILV-----------GKGTDHAKAEVREFIE-------- 228
Cdd:PRK12474 168 wNEAAYAAQP--LRGIGPAPVAAET--VERIAALLRNGKKSALLLrgsalrgapleAAGRIQAKTGVRLYCDtfaprier 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 229 -KGKIPtIVTLP--SKTIVGddhpynlgnlgkigskpsyqAMQNADLLILAGTNYPyVDYLPKKNIPAIQIDENPEaigh 305
Cdd:PRK12474 244 gAGRVP-IERIPyfHEQITA--------------------FLKDVEQLVLVGAKPP-VSFFAYPGKPSWGAPPGCE---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 306 rFDVDAPIVGDSQLALRALTDAI----QPVEKRSFLNEMLDhretwKGWMTEDKNNDAspirperlmdaINKVMTDDTVI 381
Cdd:PRK12474 298 -IVYLAQPDEDLAQALQDLADAVdapaEPAARTPLALPALP-----KGALNSLGVAQL-----------IAHRTPDQAIY 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 382 AADVGTSTV-WSTRYLNLGVNNHFIISSwlGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLPMVL 460
Cdd:PRK12474 361 ADEALTSGLfFDMSYDRARPHTHLPLTG--GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 505961992 461 FVLNNSELSFIKYEQQEAGELEYG--------IDFSDIDFAKFAEACG 500
Cdd:PRK12474 439 VIFANRSYAILNGELQRVGAQGAGrnalsmldLHNPELNWMKIAEGLG 486
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
411-541 |
1.17e-07 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 52.32 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 411 GTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAVQYNLP-MVLFVLNNSelsfiKYE----QQEAGeleygi 485
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNG-----AHDsvggQPTVS------ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 486 dfSDIDFAKFAEACG-GVGYTLKDPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPG 541
Cdd:cd03371 117 --FDVSLPAIAKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKVRPGSRSDLG 171
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
358-536 |
9.78e-07 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 51.20 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 358 DASPIRPERLMDAINKVMTDDTVIAadvgtSTVWSTRYL-------NLGVNNHFIIsswLGTMGCALPTAIASRIAFPGR 430
Cdd:TIGR03297 169 ATLMTREEAIAAILDHLPDNTVIVS-----TTGKTSRELyelrdriGQGHARDFLT---VGSMGHASQIALGLALARPDQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 431 QVIGITGDGAFEMVMQDFSTAVQYNLP-MVLFVLNNSelsfiKYEQQeAGELEYGidfSDIDFAKFAEACG-GVGYTLKD 508
Cdd:TIGR03297 241 RVVCLDGDGAALMHMGGLATIGTQGPAnLIHVLFNNG-----AHDSV-GGQPTVS---QHLDFAQIAKACGyAKVYEVST 311
|
170 180
....*....|....*....|....*...
gi 505961992 509 PKDIDSIVQTAVQQHKPTIVNVYVDKNA 536
Cdd:TIGR03297 312 LEELETALTAASSANGPRLIEVKVRPGS 339
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
410-533 |
4.00e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 47.90 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 410 LGTMGCALPTAIASRIAFPGRQVIGITGDGAFEMVMQDFSTAV---QYNLPMVlfVLNNSELSFIKYEQQEAGELeygid 486
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAalaPKNLTII--VMDNGVYQITGGQPTLTSQT----- 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505961992 487 fsdIDFAKFAEACGGV-GYTLKDPKDIDSIVQTAVQQHKPTIVNVYVD 533
Cdd:PRK06163 129 ---VDVVAIARGAGLEnSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
364-466 |
3.51e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 41.88 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 364 PERLM-DAINKVMTDDTVIAADVGTSTvwstrylnLGVNNHFIISSWLGTMGCALPTAIASRIAFPGRQVIGITGDGAF- 441
Cdd:cd02008 11 PHRPSfYALRKAFKKDSIVSGDIGCYT--------LGALPPLNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFf 82
|
90 100
....*....|....*....|....*
gi 505961992 442 EMVMQDFSTAVQYNLPMVLFVLNNS 466
Cdd:cd02008 83 HSGILGLINAVYNKANITVVILDNR 107
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
402-528 |
4.34e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 40.93 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 402 NHFIIsswLGTMGCALPTAIASRIAFPgRQVIGITGDGAFEMVMQDFSTAVQYN-LPMVLFVLNNSELSfikyeqQEAGE 480
Cdd:cd02001 36 GHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQ 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505961992 481 LEYGidfSDIDFAKFAEACGGVGYTLKDPKDIDSIVQTAVQQHKPTIV 528
Cdd:cd02001 106 PTPS---SNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
410-550 |
3.34e-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: 38.81 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 410 LGTMGCALPTAIASRIAFPgRQVIGITGDGAFEMVMQDFSTAVQY---NLPMVlfVLNNSElsfikYeqQEAGELEYGID 486
Cdd:cd03372 41 LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIAAEkpkNLIIV--VLDNGA-----Y--GSTGNQPTHAG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505961992 487 fSDIDFAKFAEACG-GVGYTLKDPKDIDSIVQTAvqQHKPTIVNVYVD-KNA-APLPGKiVPEQAIN 550
Cdd:cd03372 111 -KKTDLEAVAKACGlDNVATVASEEAFEKAVEQA--LDGPSFIHVKIKpGNTdVPNIPR-DPVEIKN 173
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
488-555 |
6.31e-03 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461353 Cd Length: 161 Bit Score: 37.54 E-value: 6.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505961992 488 SDIDFAKFAEACgGVGYTLKdPKDIDSIVQTAVQQHKPTIVNVYVDKNAAPLPG--KIVPEQainyaKWA 555
Cdd:pfam04558 97 EPIDVAEFEKAC-GVGVVVT-PEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGevRKLPEL-----KWA 159
|
|
| |
