|
Name |
Accession |
Description |
Interval |
E-value |
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
92-668 |
0e+00 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 953.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPV 331
Cdd:TIGR00118 161 DVTTAEIEYPYPEKVNLPGYRPTVKGHPLQ-------IKKAAELINLAKKPVILVGGGVI-IAGASEELKELAERIQIPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGIIHFEVSPK 411
Cdd:TIGR00118 233 TTTLMGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAP---------NAKIIHIDIDPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSE--WFAQINKWKKEYPYAyMEETPGSkIKPQTVIKKLSKVANDtgr 489
Cdd:TIGR00118 304 EIGKNVRVDIPIVGDARNVLEELLKKLFELKERKEsaWLEQINKWKKEYPLK-MDYTEEG-IKPQQVIEELSRVTKD--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 490 HVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTP 569
Cdd:TIGR00118 379 EAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 570 VKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK 648
Cdd:TIGR00118 459 VKILILNNRYLGMVRQWQELFYEERYSHTHMGSlPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKP 538
|
570 580
....*....|....*....|
gi 151946264 649 VPVLPMVAGGSGLDEFINFD 668
Cdd:TIGR00118 539 ENVLPMVAPGGGLDEMIGEK 558
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
92-654 |
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: 682.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAilrnPIPTKTTLPSNALNQLTSRAQDEfvmqSINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPV 331
Cdd:COG0028 163 DVQAA----EAEEEPAPPELRGYRPRPAPDPE----AIEEAAELLAAAKRPVILAGGGA-RRAGAAEELRALAERLGAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFapearraaaEGRGGIIHFEVSPK 411
Cdd:COG0028 234 VTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEF---------APDAKIIHIDIDPA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPVK-ERSEWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKVandTGRH 490
Cdd:COG0028 305 EIGKNYPVDLPIVGDAKAVLAALLEALEPRAdDRAAWLARIAAWRAEYLAAY--AADDGPIKPQRVIAALREA---LPDD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 491 VIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPV 570
Cdd:COG0028 380 AIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 571 KILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVP 650
Cdd:COG0028 460 KVVVLNNGGLGMVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539
|
....
gi 151946264 651 VLPM 654
Cdd:COG0028 540 PPGA 543
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
92-665 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 653.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAilrnpiPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNhaDGP---RLLKELSDRAQ 328
Cdd:PRK09107 171 DVQFA------TGTYTPPQKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVIN--SGPeasRLLRELVELTG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 329 IPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEV 408
Cdd:PRK09107 243 FPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSK---------KIHIDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 409 SPKNINKVVQTQIAVEGDATTNLGKMMS------KIFPVKERSEWFAQINKWKKEYPYAYMEEtpGSKIKPQTVIKKLSK 482
Cdd:PRK09107 314 DPSSINKNVRVDVPIIGDVGHVLEDMLRlwkargKKPDKEALADWWGQIARWRARNSLAYTPS--DDVIMPQYAIQRLYE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 483 VANdtGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSS 562
Cdd:PRK09107 392 LTK--GRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMST 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 563 AVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH-QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL 641
Cdd:PRK09107 470 AVQYNLPVKIFILNNQYMGMVRQWQQLLHGNRLSHSYtEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIF 549
|
570 580
....*....|....*....|....
gi 151946264 642 EVEVDKKVPVLPMVAGGSGLDEFI 665
Cdd:PRK09107 550 DCRVANLENCFPMIPSGKAHNEML 573
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
92-665 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 628.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPV 331
Cdd:PRK08527 163 DVTATLGEFEYPKEISLKTYKPTYKGNSRQ-------IKKAAEAIKEAKKPLFYLGGGAI-LSNASEEIRELVKKTGIPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGIIHFEVSPK 411
Cdd:PRK08527 235 VETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAK---------HAKIIHVDIDPS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMM--SKIFPVKERSEWFAQINKWKKEYPYAYMEETpgSKIKPQTVIKKLSKVANDTGr 489
Cdd:PRK08527 306 SISKIVNADYPIVGDLKNVLKEMLeeLKEENPTTYKEWREILKRYNELHPLSYEDSD--EVLKPQWVIERVGELLGDDA- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 490 hvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTP 569
Cdd:PRK08527 383 --IISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 570 VKILILNNEEQGMVTQWQSLFYEHRYSHTH-QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK 648
Cdd:PRK08527 461 VINIILNNNFLGMVRQWQTFFYEERYSETDlSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRF 540
|
570
....*....|....*..
gi 151946264 649 VPVLPMVAGGSGLDEFI 665
Cdd:PRK08527 541 ENVLPMVPAGGALYNMI 557
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
85-668 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 620.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 85 MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSG 164
Cdd:PRK06048 1 MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 165 PGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGP 244
Cdd:PRK06048 80 PGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 245 VLVDLPKDVTAAILRNPIPTKTTL----PSNALNQltsraqdefvmQSINKAADLINLAKKPVLYVGAGILNhADGPRLL 320
Cdd:PRK06048 160 VLIDLPKDVTTAEIDFDYPDKVELrgykPTYKGNP-----------QQIKRAAELIMKAERPIIYAGGGVIS-SNASEEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 321 KELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegr 400
Cdd:PRK06048 228 VELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAK------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 401 ggIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMsKIFPVKERSEWFAQINKWKKEYPYAYMEETPGskIKPQTVIKKL 480
Cdd:PRK06048 301 --IIHIDIDPAEISKNVKVDVPIVGDAKQVLKSLI-KYVQYCDRKEWLDKINQWKKEYPLKYKEREDV--IKPQYVIEQI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 481 SKVANDTgrhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTEL 560
Cdd:PRK06048 376 YELCPDA----IIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQEL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 561 SSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPV 639
Cdd:PRK06048 452 ATAVQNDIPVIVAILNNGYLGMVRQWQELFYDKRYSHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPV 531
|
570 580
....*....|....*....|....*....
gi 151946264 640 LLEVEVDKKVPVLPMVAGGSGLDEFINFD 668
Cdd:PRK06048 532 VIDFIVECEENVSPMVPAGAAINEILDLE 560
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
63-663 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 608.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 63 VDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGA 142
Cdd:PRK07789 2 SPPTPAAAASAAPPPAAPAARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 143 GHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKS 222
Cdd:PRK07789 82 GHAAEGYAQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 223 VEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSnalNQLTSRAQDEFVMQsinkAADLINLAKKP 302
Cdd:PRK07789 162 ADDIPRVIAEAFHIASTGRPGPVLVDIPKDALQAQTTFSWPPRMDLPG---YRPVTKPHGKQIRE----AAKLIAAARRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 303 VLYVGAGILNhADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVT 382
Cdd:PRK07789 235 VLYVGGGVIR-AEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 383 GNISKFAPEARraaaegrggIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKI------FPVKERSEWFAQINKWKK 456
Cdd:PRK07789 314 GKLDSFAPDAK---------VIHADIDPAEIGKNRHADVPIVGDVKEVIAELIAALraehaaGGKPDLTAWWAYLDGWRE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 457 EYPYAYMEETPGSkIKPQTVIKKLSKVAndtGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQ 536
Cdd:PRK07789 385 TYPLGYDEPSDGS-LAPQYVIERLGEIA---GPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 537 VAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHT-----HQLNPDFIKLAEA 611
Cdd:PRK07789 461 VGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVRQWQTLFYEERYSNTdlhthSHRIPDFVKLAEA 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 151946264 612 MGLKGLRVKKQEELDAKLKEFVSTKG-PVLLEVEVDKKVPVLPMVAGGSGLDE 663
Cdd:PRK07789 541 YGCVGLRCEREEDVDAVIEKARAINDrPVVIDFVVGKDAMVWPMVAAGTSNDE 593
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
93-660 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 605.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:PRK08978 2 NGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKD 252
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 253 VTAAilrnPIPTKTTLPSNAlnqltsrAQDEFVMQSINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPVT 332
Cdd:PRK08978 161 IQLA----EGELEPHLTTVE-------NEPAFPAAELEQARALLAQAKKPVLYVGGGV-GMAGAVPALREFLAATGMPAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 333 TTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSPKN 412
Cdd:PRK08978 229 ATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAK---------VIHLDIDPAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 413 INKVVQTQIAVEGDattnlgkmMSKIFPVKERS----EWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKVANDTG 488
Cdd:PRK08978 300 INKLRQAHVALQGD--------LNALLPALQQPlnidAWRQHCAQLRAEHAWRY--DHPGEAIYAPALLKQLSDRKPADT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 489 rhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGT 568
Cdd:PRK08978 370 ---VVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 569 PVKILILNNEEQGMVTQWQSLFYEHRYSHThQL--NPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK08978 447 PVKIVLLDNQRLGMVRQWQQLFFDERYSET-DLsdNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSID 525
|
570
....*....|....
gi 151946264 647 KKVPVLPMVAGGSG 660
Cdd:PRK08978 526 ELENVWPLVPPGAS 539
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
93-658 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 600.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDK---FNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATN 169
Cdd:PRK07418 20 TGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAegwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 170 VVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDL 249
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 250 PKDVTAAILR-NPI-PTKTTLPSNalnQLTSRAQDefvmQSINKAADLINLAKKPVLYVGAGILN---HADgprlLKELS 324
Cdd:PRK07418 180 PKDVGQEEFDyVPVePGSVKPPGY---RPTVKGNP----RQINAALKLIEEAERPLLYVGGGAISagaHAE----LKELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 325 DRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGII 404
Cdd:PRK07418 249 ERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFAS---------RAKVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 405 HFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIF--PVKER-SEWFAQINKWKKEYPYayMEETPGSKIKPQTVIKKLS 481
Cdd:PRK07418 320 HIDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLepTTPPRtQAWLERINRWKQDYPL--VVPPYEGEIYPQEVLLAVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 482 KVANdtgrHVIVTTGVGQHQMWAAQHWtwRN-PHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTEL 560
Cdd:PRK07418 398 DLAP----DAYYTTDVGQHQMWAAQFL--RNgPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 561 SSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN--PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGP 638
Cdd:PRK07418 472 GTLAQYGINVKTVIINNGWQGMVRQWQESFYGERYSASNMEPgmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGP 551
|
570 580
....*....|....*....|
gi 151946264 639 VLLEVEVDKKVPVLPMVAGG 658
Cdd:PRK07418 552 VLIDVHVRRDENCYPMVPPG 571
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
92-669 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 599.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNfVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPH-ILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK07710 95 TGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPV 331
Cdd:PRK07710 175 DMVVEEGEFCYDVQMDLPGYQPNYEPNLLQ-------IRKLVQAVSVAKKPVILAGAGVL-HAKASKELTSYAEQQEIPV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSPK 411
Cdd:PRK07710 247 VHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEAT---------VAHIDIDPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGskIKPQTVIKKLSKVANDTGrhv 491
Cdd:PRK07710 318 EIGKNVPTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWKEKYPLSYKRNSES--IKPQKAIEMLYEITKGEA--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 492 IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVK 571
Cdd:PRK07710 393 IVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 572 ILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVP 650
Cdd:PRK07710 473 VVILNNEALGMVRQWQEEFYNQRYSHSLLSCqPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEK 552
|
570
....*....|....*....
gi 151946264 651 VLPMVAGGSGLDEFINFDP 669
Cdd:PRK07710 553 VMPMVAPGKGLHEMVGVKK 571
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
100-658 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 568.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV---LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMAD 176
Cdd:CHL00099 18 DSLVRHGVKHIFGYPGGAILPIYDELYAWEKKGLIkhiLVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIAT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 177 AFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAA 256
Cdd:CHL00099 98 AQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 257 ILRNPIPTKttlPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPVTTTLQ 336
Cdd:CHL00099 178 KFDYYPPEP---GNTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAII-SDAHQEITELAELYKIPVTTTLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 337 GLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSPKNINKV 416
Cdd:CHL00099 254 GKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQ---------VIHIDIDPAEIGKN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 417 VQTQIAVEGDATTNLGKMM-----SKIFPVKERSE-WFAQINKWKKEYPyaYMEETPGSKIKPQTVIKKLSKVANDTgrh 490
Cdd:CHL00099 325 RIPQVAIVGDVKKVLQELLellknSPNLLESEQTQaWRERINRWRKEYP--LLIPKPSTSLSPQEVINEISQLAPDA--- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 491 vIVTTGVGQHQMWAAQ-------HWtwrnphtfITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSA 563
Cdd:CHL00099 400 -YFTTDVGQHQMWAAQflkckprKW--------LSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 564 VQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH--QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL 641
Cdd:CHL00099 471 AQYNLPIKIIIINNKWQGMVRQWQQAFYGERYSHSNmeEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLI 550
|
570
....*....|....*..
gi 151946264 642 EVEVDKKVPVLPMVAGG 658
Cdd:CHL00099 551 DCQVIEDENCYPMVAPG 567
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
92-665 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 563.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK06466 4 LSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNP--IPTKTTLPSnalNQLTSRAQDefvmQSINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQI 329
Cdd:PRK06466 164 DMTNPAEKFEyeYPKKVKLRS---YSPAVRGHS----GQIRKAVEMLLAAKRPVIYSGGGVV-LGNASALLTELAHLLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 330 PVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVS 409
Cdd:PRK06466 236 PVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAK---------IIHIDID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 410 PKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKER------SEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKV 483
Cdd:PRK06466 307 PASISKTIKADIPIVGPVESVLTEMLAILKEIGEKpdkealAAWWKQIDEWRGRHGLFPYDKGDGGIIKPQQVVETLYEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 484 andTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSA 563
Cdd:PRK06466 387 ---TNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 564 VQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKE-FVSTKGPVLL 641
Cdd:PRK06466 464 LQYGLPVKIINLNNGALGMVRQWQDMQYEGRHSHSYMESlPDFVKLAEAYGHVGIRITDLKDLKPKLEEaFAMKDRLVFI 543
|
570 580
....*....|....*....|....*
gi 151946264 642 EVEVDKKVPVLPM-VAGGSGLDEFI 665
Cdd:PRK06466 544 DIYVDRSEHVYPMqIADGSMRDMWL 568
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
92-665 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 563.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-LIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAA---ILRNPIPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQ 328
Cdd:PRK06276 160 DVQEGeldLEKYPIPAKIDLPGYKPTTFGHPLQ-------IKKAAELIAEAERPVILAGGGVI-ISGASEELIELSELVK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 329 IPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEV 408
Cdd:PRK06276 232 IPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAK---------IIHIDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 409 SPKNINKVVQTQIAVEGDATTNLGKMMSKI--FPVKERSEWFAQINKWKKE-YPYAYMEETPgskIKPQTVIKKLSKVAN 485
Cdd:PRK06276 303 DPAEIGKNVRVDVPIVGDAKNVLRDLLAELmkKEIKNKSEWLERVKKLKKEsIPRMDFDDKP---IKPQRVIKELMEVLR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 486 D--TGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSA 563
Cdd:PRK06276 380 EidPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 564 VQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLE 642
Cdd:PRK06276 460 AEYDIPVVICIFDNRTLGMVYQWQNLYYGKRQSEVHLGEtPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLD 539
|
570 580
....*....|....*....|...
gi 151946264 643 VEVDKKvPVLPMVAGGSGLDEFI 665
Cdd:PRK06276 540 IIIDPA-EALPMVPPGGNLTNIL 561
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
92-665 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 553.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK06725 94 TGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPV 331
Cdd:PRK06725 174 DVQNEKVTSFYNEVVEIPGYKPEPRPDSMK-------LREVAKAISKAKRPLLYIGGGVI-HSGGSEELIEFARENRIPV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRaaaegrggiIHFEVSPK 411
Cdd:PRK06725 246 VSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKK---------VHIDIDPS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPVKERsEWFAQINKWKKEYPYAYMEETpgSKIKPQTVIKKLSKVANDtgrHV 491
Cdd:PRK06725 317 EFHKNVAVEYPVVGDVKKALHMLLHMSIHTQTD-EWLQKVKTWKEEYPLSYKQKE--SELKPQHVINLVSELTNG---EA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 492 IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVK 571
Cdd:PRK06725 391 IVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 572 ILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPV 651
Cdd:PRK06725 471 VFIINNKFLGMVRQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENV 550
|
570
....*....|....
gi 151946264 652 LPMVAGGSGLDEFI 665
Cdd:PRK06725 551 FPMVPPNKGNNEMI 564
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
94-666 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 545.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 94 GGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTP 173
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 174 MADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDV 253
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 254 TAAIlrnPIP---TKTTLPSNaLNQLTSRAQDEFVMQSInkaaDLINLAKKPVLYVGAGILNHADGprlLKELSDRAQIP 330
Cdd:PLN02470 175 QQQL---AVPnwnQPMKLPGY-LSRLPKPPEKSQLEQIV----RLISESKRPVVYVGGGCLNSSEE---LREFVELTGIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 331 VTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGIIHFEVSP 410
Cdd:PLN02470 244 VASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFAS---------RASIVHIDIDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 411 KNINKVVQTQIAVEGD---ATTNLGKMMSKIfPVK--ERSEWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKVan 485
Cdd:PLN02470 315 AEIGKNKQPHVSVCADvklALQGLNKLLEER-KAKrpDFSAWRAELDEQKEKFPLSY--PTFGDAIPPQYAIQVLDEL-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 486 dTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQ 565
Cdd:PLN02470 390 -TDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 566 AGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH--------QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKG 637
Cdd:PLN02470 469 ENLPVKIMVLNNQHLGMVVQWEDRFYKANRAHTYlgdpdaeaEIFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPG 548
|
570 580
....*....|....*....|....*....
gi 151946264 638 PVLLEVEVDKKVPVLPMVAGGSGLDEFIN 666
Cdd:PLN02470 549 PYLLDVIVPHQEHVLPMIPGGGTFKDIIT 577
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
92-665 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 541.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK08155 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILrnpipTKTTLPSNALNQltsrAQDEFVMQSINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPV 331
Cdd:PRK08155 173 DVQTAVI-----ELEALPAPAEKD----AAPAFDEESIRDAAAMINAAKRPVLYLGGGVI-NSGAPARARELAEKAQLPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGIIHFEVSPK 411
Cdd:PRK08155 243 TMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCP---------NAKIIHVDIDRA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPvKERSEWFAQINKWKKEYPYaymeETPGSKiKPQTVIKKLSKVANDTGRHV 491
Cdd:PRK08155 314 ELGKIKQPHVAIQADVDDVLAQLLPLVEA-QPRAEWHQLVADLQREFPC----PIPKAD-DPLSHYGLINAVAACVDDNA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 492 IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVK 571
Cdd:PRK08155 388 IITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 572 ILILNNEEQGMVTQWQSLFYEHR-YSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVP 650
Cdd:PRK08155 468 IILMNNEALGLVHQQQSLFYGQRvFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEK 547
|
570
....*....|....*
gi 151946264 651 VLPMVAGGSGLDEFI 665
Cdd:PRK08155 548 VYPMVPPGAANTEMI 562
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
92-663 |
1.84e-179 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 522.84 E-value: 1.84e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQDEfvmqsINKAADLINLAKKPVLYVGAG-ILNHADGPRLlkELSDRAQIP 330
Cdd:PRK08979 164 DCLNPAILHPYEYPESIKMRSYNPTTSGHKGQ-----IKRGLQALLAAKKPVLYVGGGaIISGADKQIL--QLAEKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 331 VTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSP 410
Cdd:PRK08979 237 VVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNAT---------ILHIDIDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 411 KNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSE------WFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKVA 484
Cdd:PRK08979 308 SSISKTVRVDIPIVGSADKVLDSMLALLDESGETNDeaaiasWWNEIEVWRSRNCLAY--DKSSERIKPQQVIETLYKLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 485 NDTGrhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAV 564
Cdd:PRK08979 386 NGDA---YVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 565 QAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGP-VLLE 642
Cdd:PRK08979 463 QYDIPVKIINLNNRFLGMVKQWQDMIYQGRHSHSYMDSvPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRlVFVD 542
|
570 580
....*....|....*....|.
gi 151946264 643 VEVDKKVPVLPMVAGGSGLDE 663
Cdd:PRK08979 543 INVDETEHVYPMQIRGGAMNE 563
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
92-665 |
3.73e-176 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 515.12 E-value: 3.73e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPS-NALNQLTSraqdefvmQSINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIP 330
Cdd:PRK06965 181 DVSKTPCEYEYPKSVEMRSyNPVTKGHS--------GQIRKAVSLLLSAKRPYIYTGGGVI-LANASRELRQLADLLGYP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 331 VTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRaaaegrggIIHFEVSP 410
Cdd:PRK06965 252 VTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPRK--------IIHIDIDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 411 KNINKVVQTQIAVEGDATTNLGKMMSKIFPVKER------SEWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLskvA 484
Cdd:PRK06965 324 SSISKRVKVDIPIVGDVKEVLKELIEQLQTAEHGpdadalAQWWKQIEGWRSRDCLKY--DRESEIIKPQYVVEKL---W 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 485 NDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAV 564
Cdd:PRK06965 399 ELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 565 QAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH-QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKG-PVLLE 642
Cdd:PRK06965 479 QYDTPVKIISLNNRYLGMVRQWQEIEYSKRYSHSYmDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDrTVFLD 558
|
570 580
....*....|....*....|...
gi 151946264 643 VEVDKKVPVLPMVAGGSGLDEFI 665
Cdd:PRK06965 559 FQTDPTENVWPMVQAGKGITEML 581
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
93-665 |
7.47e-175 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 510.90 E-value: 7.47e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKD 252
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 253 VTAAILRNPIPTKTTLPSnalNQLTSRAQDEfvmqSINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPVT 332
Cdd:PRK07282 171 VSALETDFIYDPEVNLPS---YQPTLEPNDM----QIKKILKQLSKAKKPVILAGGGI-NYAEAATELNAFAERYQIPVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 333 TTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSPKN 412
Cdd:PRK07282 243 TTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAK---------VAHIDIDPAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 413 INKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPyAYmeETPGSKIKPQTVIKKLSKVANDTGrhvI 492
Cdd:PRK07282 314 IGKIIKTDIPVVGDAKKALQMLLAEPTVHNNTEKWIEKVTKDKNRVR-SY--DKKERVVQPQAVIERIGELTNGDA---I 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 493 VTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKI 572
Cdd:PRK07282 388 VVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 573 LILNNEEQGMVTQWQSLFYEHRYSH-THQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKgPVLLEVEVDKKVPV 651
Cdd:PRK07282 468 VMLNNHSLGMVRQWQESFYEGRTSEsVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-PMLIEVDISRKEHV 546
|
570
....*....|....
gi 151946264 652 LPMVAGGSGLDEFI 665
Cdd:PRK07282 547 LPMVPAGKSNHEML 560
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
92-663 |
3.52e-166 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 488.98 E-value: 3.52e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTTLPSNALNQLTSRAQDEfvmqsINKAADLINLAKKPVLYVGAGILNHADGPRLLkELSDRAQIPV 331
Cdd:PRK07979 164 DILNPANKLPYVWPESVSMRSYNPTTQGHKGQ-----IKRALQTLVAAKKPVVYVGGGAINAACHQQLK-ELVEKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARraaaegrggIIHFEVSPK 411
Cdd:PRK07979 238 VSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNAT---------VLHIDIDPT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIF------PVKERSEWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKVan 485
Cdd:PRK07979 309 SISKTVTADIPIVGDARQVLEQMLELLSqesahqPLDEIRDWWQQIEQWRARQCLKY--DTHSEKIKPQAVIETLWRL-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 486 dTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQ 565
Cdd:PRK07979 385 -TKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 566 AGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLN-PDFIKLAEAMGLKGLRVKKQEELDAKLKEF---VSTKGPVLL 641
Cdd:PRK07979 464 YELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPDELESKLSEAleqVRNNRLVFV 543
|
570 580
....*....|....*....|..
gi 151946264 642 EVEVDKKVPVLPMVAGGSGLDE 663
Cdd:PRK07979 544 DVTVDGSEHVYPMQIRGGGMDE 565
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
92-670 |
6.70e-164 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 483.26 E-value: 6.70e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNP--IPTKTTLPSNALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQI 329
Cdd:PRK06882 164 DMVNPANKFTyeYPEEVSLRSYNPTVQGHKGQ-------IKKALKALLVAKKPVLFVGGGVIT-AECSEQLTQFAQKLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 330 PVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPearraaaegRGGIIHFEVS 409
Cdd:PRK06882 236 PVTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCP---------NAKVIHIDID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 410 PKNINKVVQTQIAVEGDATTNLGKMMSKIFP---VKERS---EWFAQINKWKKEYPYAYmeETPGSKIKPQTVIKKLSKV 483
Cdd:PRK06882 307 PTSISKNVPAYIPIVGSAKNVLEEFLSLLEEenlAKSQTdltAWWQQINEWKAKKCLEF--DRTSDVIKPQQVVEAIYRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 484 ANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSA 563
Cdd:PRK06882 385 TNG---DAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 564 VQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHqLN--PDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGP-VL 640
Cdd:PRK06882 462 KQYDIPVVIVSLNNRFLGMVKQWQDLIYSGRHSQVY-MNslPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKlVF 540
|
570 580 590
....*....|....*....|....*....|
gi 151946264 641 LEVEVDKKVPVLPMVAGGSGLDEFINFDPE 670
Cdd:PRK06882 541 VDVNVDETEHVYPMQIRGGAMNEMILSKPE 570
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
93-669 |
1.76e-131 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 399.60 E-value: 1.76e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAI---HNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATN 169
Cdd:PRK06456 3 TGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 170 VVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDL 249
Cdd:PRK06456 83 LVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 250 PKDvtaaiLRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLkELSDRAQI 329
Cdd:PRK06456 163 PRD-----IFYEKMEEIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVL-ELAELLHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 330 PVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEarraaaegRGGIIHFEVS 409
Cdd:PRK06456 237 PIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVET--------RKKFIMVNID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 410 PKNINKVVQTQIAVEGDATTNLGKMMSKIFPV---KERSEWFAQINKWKKEYPYAYMEETPGsKIKPQTVIKKlskVAND 486
Cdd:PRK06456 309 PTDGEKAIKVDVGIYGNAKIILRELIKAITELgqkRDRSAWLKRVKEYKEYYSQFYYTEENG-KLKPWKIMKT---IRQA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 487 TGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQA 566
Cdd:PRK06456 385 LPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 567 GTPVKILILNNEEQGMVTQWQSLFYEHR-YSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEV 645
Cdd:PRK06456 465 HIPVISVIFDNRTLGLVRQVQDLFFGKRiVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPV 544
|
570 580
....*....|....*....|....
gi 151946264 646 DKKVPVLPMVAGGSGLDEFINFDP 669
Cdd:PRK06456 545 DKEELALPTLPPGGRLKQVILRDP 568
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
107-646 |
6.32e-112 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 348.36 E-value: 6.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 107 VDTVFGYPGGAILPVYDAIHNSdKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVV 186
Cdd:PRK08322 16 VEYIFGIPGEENLDLLEALRDS-SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 187 FTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAA-ILRNPIP-- 263
Cdd:PRK08322 95 ITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDIAAEeTDGKPLPrs 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 264 -TKTTLPSNAlnqltsraqdefvmqSINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPVTTTLQGLGSFD 342
Cdd:PRK08322 175 ySRRPYASPK---------------AIERAAEAIQAAKNPLILIGAGA-NRKTASKALTEFVDKTGIPFFTTQMGKGVIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 343 QEDPKSLDMLGMHGCATANLAVQNADLIIAVG------ARFDDRVTGNISkfapearraaaegrggIIHFEVSPKNINKV 416
Cdd:PRK08322 239 ETHPLSLGTAGLSQGDYVHCAIEHADLIINVGhdviekPPFFMNPNGDKK----------------VIHINFLPAEVDPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 417 VQTQIAVEGDATTNLGKMMSKIFPVKERS-EWFAQINKWKKEYpYAYMEETPGSKIKPQTVIKKLSKVANDTGrhvIVTT 495
Cdd:PRK08322 303 YFPQVEVVGDIANSLWQLKERLADQPHWDfPRFLKIREAIEAH-LEEGADDDRFPMKPQRIVADLRKVMPDDD---IVIL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 496 GVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILIL 575
Cdd:PRK08322 379 DNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLIL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151946264 576 NNEEQGMVtQW--QSLFYEHRYshTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK08322 459 NDNAYGMI-RWkqENMGFEDFG--LDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
471-658 |
2.98e-110 |
|
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: 330.61 E-value: 2.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 471 IKPQTVIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGD 550
Cdd:cd02015 1 IKPQEVIKELSELTPG---DAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 551 ASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH-QLNPDFIKLAEAMGLKGLRVKKQEELDAKL 629
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTlDSNPDFVKLAEAYGIKGLRVEKPEELEAAL 157
|
170 180
....*....|....*....|....*....
gi 151946264 630 KEFVSTKGPVLLEVEVDKKVPVLPMVAGG 658
Cdd:cd02015 158 KEALASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
100-673 |
3.45e-104 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 329.63 E-value: 3.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARAS-GKPGVVLVTSGPGATNVVTPMADAF 178
Cdd:PRK11269 12 LVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGLYSAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 179 ADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAIL 258
Cdd:PRK11269 92 ADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQVAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 259 RNPIPTKTTLPSNAlnQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPVTTTLQGL 338
Cdd:PRK11269 172 EFDPDTYEPLPVYK--PAATRAQ-------IEKALEMLNAAERPLIVAGGGVIN-ADASDLLVEFAELTGVPVIPTLMGW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 339 GSFDQEDPKsldMLGMHGCATA----NLAVQNADLIIAVGARFDDRVTGNISKFapearraaaegRGG--IIHFEVSPKN 412
Cdd:PRK11269 242 GAIPDDHPL---MAGMVGLQTShrygNATLLASDFVLGIGNRWANRHTGSVEVY-----------TKGrkFVHVDIEPTQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 413 INKVVQTQIAVEGDATTNL------GKMMSKIFPVKERSEWFAQINKWKKEYPY-AYMEETPgskIKPQTVIKKLSKVan 485
Cdd:PRK11269 308 IGRVFGPDLGIVSDAKAALellvevAREWKAAGRLPDRSAWVADCQERKRTLLRkTHFDNVP---IKPQRVYEEMNKA-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 486 dTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQ 565
Cdd:PRK11269 383 -FGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 566 AGTPVKILILNNEEQGMVTQWQSLF---YEHRYSHTHQLNP-------DFIKLAEAMGLKGLRVKKQEELDAKL----KE 631
Cdd:PRK11269 462 FNLPYIHVLVNNAYLGLIRQAQRAFdmdYCVQLAFENINSPelngygvDHVKVAEGLGCKAIRVFKPEDIAPALeqakAL 541
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 151946264 632 FVSTKGPVLLEVEVDkKVPVLPMvagGSGLDEFINFDPEVER 673
Cdd:PRK11269 542 MAEFRVPVVVEVILE-RVTNISM---GTEIDAVNEFEELADN 579
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
100-673 |
5.18e-93 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 300.05 E-value: 5.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARA-SGKPGVVLVTSGPGATNVVTPMADAF 178
Cdd:COG3960 11 AVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAkAGNIGVCIGTSGPAGTDMITGLYSAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 179 ADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAIL 258
Cdd:COG3960 91 ADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLIDLPIDVQMAEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 259 RNPIPTKTTLPsnALNQLTSRAQdefvmqsINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPVTTTLQGL 338
Cdd:COG3960 171 EFDIDTYEPLP--VYKPAATRAQ-------IEKALDMLNAAERPLIVAGGGIIN-ADASDLLVEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 339 GSFDQEDPKsldMLGMHGCATA----NLAVQNADLIIAVGARFDDRVTGNISKFapearraaAEGRgGIIHFEVSPKNIN 414
Cdd:COG3960 241 GSIPDDHPL---MAGMVGLQTShrygNATLLASDFVLGIGNRWANRHTGSLDVY--------TKGR-KFVHVDIEPTQIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 415 KVVQTQIAVEGDATTNL------GKMMSKIFPVKERSEWFAQINKWKKE-YPYAYMEETPgskIKPQTVIKKLSKVandT 487
Cdd:COG3960 309 RVFAPDLGIVSDAKAALelfvevARERKAAGKLPDRSAWAAECQERKRTmLRKTHFDNVP---IKPQRVYEEMNKA---F 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 488 GRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAG 567
Cdd:COG3960 383 GRDTRYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 568 TPVKILILNNEEQGMVTQWQSLF---YEHRYSHTHQLNP-------DFIKLAEAMGLKGLRVKKQEELDAKLKE----FV 633
Cdd:COG3960 463 LPYIHVVVNNSYLGLIRQAQRGFdmdYCVQLAFENINAPelggygvDHVKVAEGLGCKAIRVTDPEEIAPAFEEakalMA 542
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 151946264 634 STKGPVLLEVeVDKKVPVLPMvagGSGLDEFINFDPEVER 673
Cdd:COG3960 543 EHRVPVVVEV-ILERVTNISM---GTEIDNVNEFEELAES 578
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
85-646 |
4.22e-91 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 294.09 E-value: 4.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 85 MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSG 164
Cdd:PRK08199 1 MTSTPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 165 PGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGP 244
Cdd:PRK08199 81 PGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 245 VLVDLPKDV-----TAAILRNPIPTKTTlPSNAlnqltsraqdefvmqSINKAADLINLAKKPVLYVGAGILNhADGPRL 319
Cdd:PRK08199 161 VVLALPEDVlsetaEVPDAPPYRRVAAA-PGAA---------------DLARLAELLARAERPLVILGGSGWT-EAAVAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 320 LKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMhGCATANLA-VQNADLIIAVGARFDDRVTGNISKFAPEARraaae 398
Cdd:PRK08199 224 LRAFAERWGLPVACAFRRQDLFDNRHPNYAGDLGL-GINPALAArIREADLVLAVGTRLGEVTTQGYTLLDIPVP----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 399 gRGGIIHFEVSPKNINKVVQTQIAVEGDAtTNLGKMMSKIFPVkERSEWFAqinkWKKEYPYAYMEETPgSKIKPQTVIk 478
Cdd:PRK08199 298 -RQTLVHVHPDAEELGRVYRPDLAIVADP-AAFAAALAALEPP-ASPAWAE----WTAAAHADYLAWSA-PLPGPGAVQ- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 479 kLSKVANDTGRHV----IVTTGVGQHQMWAAQHWTWRNPHTFI--TSgglGTMGYGLPAAIGAQVAKPESLVIDIDGDAS 552
Cdd:PRK08199 369 -LGEVMAWLRERLpadaIITNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGC 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 553 FNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEF 632
Cdd:PRK08199 445 FLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQEREYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERA 524
|
570
....*....|....
gi 151946264 633 VSTKGPVLLEVEVD 646
Cdd:PRK08199 525 LASGKPALIEIRID 538
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
93-667 |
6.66e-90 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 291.52 E-value: 6.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAI-HNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEadvVGISRSCTK---WNVMVKSVEELPLRINEAFEIATSGRpGPVLVD 248
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGTDFFQE---VNLEKMFEDvavYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 249 LPKDvtaaILRNPIPTKTTLPSNALNQLTSRAQDEfvmqSINKAADLINLAKKPVLYVGAGiLNHAdGPRLLkELSDRAQ 328
Cdd:PRK08611 161 IPDD----LPAQKIKDTTNKTVDTFRPTVPSPKPK----DIKKAAKLINKAKKPVILAGLG-AKHA-KEELL-AFAEKAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 329 IPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDdrVTGNISKFAPEarraaaegrggiIHFEV 408
Cdd:PRK08611 230 IPIIHTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYP--YVDYLPKKAKA------------IQIDT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 409 SPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSewFAQ-----INKWKKEypyayMEE------TPgskIKPQTVI 477
Cdd:PRK08611 296 DPANIGKRYPVNVGLVGDAKKALHQLTENIKHVEDRR--FLEacqenMAKWWKW-----MEEdennasTP---IKPERVM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 478 KKLSKVANDTGrhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTL 557
Cdd:PRK08611 366 AAIQKIADDDA---VLSVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 558 TELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYShTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKG 637
Cdd:PRK08611 443 QDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYA-IDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDK 521
|
570 580 590
....*....|....*....|....*....|
gi 151946264 638 PVLLEVEVDKKVPVLPmvaGGSGLDEFINF 667
Cdd:PRK08611 522 PVIIDVYVDPNAAPLP---GKIVNDEALGY 548
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
92-647 |
8.34e-90 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 290.37 E-value: 8.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNS-DKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNV 170
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAgDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 171 VTPMADAFADGIPMVVFTGQVPTSAIGTDAFQ--E-ADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLV 247
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEmPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 248 DLPKDVTAAilrnpipTKTTLPSNALNQLTSRAQDEfvmQSINKAADLINLAKKPVLYVGAGILNHADgprLLKELSDRA 327
Cdd:PRK08266 164 EMPWDVFGQ-------RAPVAAAPPLRPAPPPAPDP---DAIAAAAALIAAAKNPMIFVGGGAAGAGE---EIRELAEML 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 328 QIPVTTTLQGLGSFDQEDPksldmLGMHgCATANLAVQNADLIIAVGARFDDRVTgniskfapeaRRAAAEGRGGIIHFE 407
Cdd:PRK08266 231 QAPVVAFRSGRGIVSDRHP-----LGLN-FAAAYELWPQTDVVIGIGSRLELPTF----------RWPWRPDGLKVIRID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 408 VSPKNINKvVQTQIAVEGDA---TTNLGKMMSKIFPVKE-RSEWFAQINKWKKEYPyaymeetpgSKIKPQ-TVIKKLSK 482
Cdd:PRK08266 295 IDPTEMRR-LKPDVAIVADAkagTAALLDALSKAGSKRPsRRAELRELKAAARQRI---------QAVQPQaSYLRAIRE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 483 VANDTGRHVIVTTGVGqhqmwaaqHWTW-----RNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTL 557
Cdd:PRK08266 365 ALPDDGIFVDELSQVG--------FASWfafpvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 558 TELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKG 637
Cdd:PRK08266 437 QELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGG 516
|
570
....*....|
gi 151946264 638 PVLLEVEVDK 647
Cdd:PRK08266 517 PVLIEVPVPR 526
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
94-646 |
2.48e-84 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 275.86 E-value: 2.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 94 GGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTP 173
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 174 MADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDV 253
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 254 TAAilrnPIPTKtTLPSNALNQLTSRAQDEfvmqsINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPVTT 333
Cdd:TIGR02418 160 VDS----PVSVK-AIPASYAPKLGAAPDDA-----IDEVAEAIQNAKLPVLLLGLRA-SSPETTEAVRRLLKKTQLPVVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 334 TLQGLGSFDQE-DPKSLDMLGMHGCATANLAVQNADLIIAVGarFD----DRVTGNISkfapearraaaeGRGGIIHFEV 408
Cdd:TIGR02418 229 TFQGAGAVSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDpieyEPRNWNSE------------NDATIVHIDV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 409 SPKNINKVVQTQIAVEGDATTNLGKMMSKIfPVKERSEWFAQINKWKKeypyAYMEETPGSKIKPQ-------TVIKKLS 481
Cdd:TIGR02418 295 EPAQIDNNYQPDLELVGDIASTLDLLAERI-PGYELPPDALAILEDLK----QQREALDRVPATLKqahlhplEIIKAMQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 482 KVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELS 561
Cdd:TIGR02418 370 AIVTD---DVTVTVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 562 SAVQAGTPVKILILNNEEQGMVtQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL 641
Cdd:TIGR02418 447 TAVRLKLNIVHIIWNDNGYNMV-EFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVV 525
|
....*
gi 151946264 642 EVEVD 646
Cdd:TIGR02418 526 DIPVD 530
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
92-649 |
8.95e-84 |
|
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: 275.59 E-value: 8.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDaIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:TIGR03457 2 MTPSEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRpGPVLVDLPK 251
Cdd:TIGR03457 81 TAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DVTAAILRNPIPTKTtlpsnalnQLTSRAQDEfvmQSINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPV 331
Cdd:TIGR03457 160 DYFYGEIDVEIPRPV--------RLDRGAGGA---TSLAQAARLLAEAKFPVIISGGGVVM-GDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 332 TTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDdrVTGNISKFAPEARRAAAEgrggIIHFEVSPK 411
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLG--PFGTLPQYGIDYWPKNAK----IIQVDANAK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPV--------------KERSEWFAQINKWKKEYP------YAYMEETPGSKI 471
Cdd:TIGR03457 302 MIGLVKKVTVGICGDAKAAAAEILQRLAGKagdanraerkakiqAERSAWEQELSEMTHERDpfsldmIVEQRQEEGNWL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 472 KPQTVIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDA 551
Cdd:TIGR03457 382 HPRQVLRELEKAMPE---DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 552 SFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHThQLNPD--FIKLAEAMGLKGLRVKKQEELDAKL 629
Cdd:TIGR03457 459 AWGMSMNEIMTAVRHDIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGT-ELESElsFAGIADAMGAKGVVVDKPEDVGPAL 537
|
570 580
....*....|....*....|...
gi 151946264 630 KEFVSTKG---PVLLEVEVDKKV 649
Cdd:TIGR03457 538 KKAIAAQAegkTTVIEIVCTREL 560
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
93-646 |
6.23e-83 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 272.50 E-value: 6.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKfNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGP-ELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKD 252
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 253 VTAAILRNPIPTKTTLPsnalnQLTSRAQDEfvmqsINKAADLINLAKKPVLYVGagilNHADGP---RLLKELSDRAQI 329
Cdd:PRK08617 165 VVDAPVTSKAIAPLSKP-----KLGPASPED-----INYLAELIKNAKLPVLLLG----MRASSPevtAAIRRLLERTNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 330 PVTTTLQGLG--SFDQEDpkslDMLGMHGC---ATANLAVQNADLIIAVGarFD----DRVTGNiskfapearraaAEGR 400
Cdd:PRK08617 231 PVVETFQAAGviSRELED----HFFGRVGLfrnQPGDELLKKADLVITIG--YDpieyEPRNWN------------SEGD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 401 GGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEY-----PYAYMEETPgskIKPQT 475
Cdd:PRK08617 293 ATIIHIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQLeelaeRPARLEEGA---VHPLR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 476 VIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNM 555
Cdd:PRK08617 370 IIRALQDIVTD---DTTVTVDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 556 TLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYeHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVST 635
Cdd:PRK08617 447 SAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKY-GRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALAT 525
|
570
....*....|.
gi 151946264 636 KGPVLLEVEVD 646
Cdd:PRK08617 526 DGPVVIDIPVD 536
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
107-646 |
6.02e-75 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 251.29 E-value: 6.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 107 VDTVFGYPGGAILPVYDAIHNSdKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVV 186
Cdd:PRK06457 17 IQRIYGIPGDSIDPLVDAIRKS-KVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 187 FTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRpGPVLVDLPKDvtaaILRNPIPTKt 266
Cdd:PRK06457 96 LTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVD----ILRKSSEYK- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 267 tlpsnaLNQLTSRAQDEFVMqSINKAADLINLAKKPVLYVGAGILNHADgprLLKELSDRAQIPVTTTLQGLGSFDQEDP 346
Cdd:PRK06457 170 ------GSKNTEVGKVKYSI-DFSRAKELIKESEKPVLLIGGGTRGLGK---EINRFAEKIGAPIIYTLNGKGILPDLDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 347 KSLDMLGMHGCATANLAVQNADLIIAVGARFDdrvtgnISKFAPEARRaaaegrggIIHFEVSPKNINKVVQTQIAVEGD 426
Cdd:PRK06457 240 KVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP------YVNFLNKSAK--------VIQVDIDNSNIGKRLDVDLSYPIP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 427 ATTNLGkmmskiFPVKERSEWF-----AQINKWKKEYPYAymEETPGSKIKPQTVIKKLSKVANDTGrhvIVTTGVGQHQ 501
Cdd:PRK06457 306 VAEFLN------IDIEEKSDKFyeelkGKKEDWLDSISKQ--ENSLDKPMKPQRVAYIVSQKCKKDA---VIVTDTGNVT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 502 MWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVA-KPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQ 580
Cdd:PRK06457 375 MWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKL 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151946264 581 GMVTQWQSLFYEHRYShTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK06457 455 GMIKFEQEVMGYPEWG-VDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
98-643 |
1.02e-74 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 251.84 E-value: 1.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 98 FNEMMSRQNVDTVFGYPGGAILPVydaihnSDKF-----NFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:PRK07525 12 FVETLQAHGITHAFGIIGSAFMDA------SDLFppagiRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRpGPVLVDLPKD 252
Cdd:PRK07525 86 AVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 253 VTAAILRNPIPTKTTLPSNALNQltsraqdefvmQSINKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPVT 332
Cdd:PRK07525 165 YFYGVIDVEIPQPVRLERGAGGE-----------QSLAEAAELLSEAKFPVILSGAGVVL-SDAIEECKALAERLDAPVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 333 TTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGAR---FDDRVTGNISKFAPEARraaaegrggIIHFEVS 409
Cdd:PRK07525 233 CGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRlnpFGTLPQYGIDYWPKDAK---------IIQVDIN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 410 PKNINKVVQTQIAVEGDA---TTNLGKMMSKIFP------------VKERSEWFAQINKWKKE---YPYAYMEETPGSK- 470
Cdd:PRK07525 304 PDRIGLTKKVSVGICGDAkavARELLARLAERLAgdagreerkaliAAEKSAWEQELSSWDHEdddPGTDWNEEARARKp 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 471 --IKPQTVIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDID 548
Cdd:PRK07525 384 dyMHPRQALREIQKALPE---DAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 549 GDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTH-QLNPDFIKLAEAMGLKGLRVKKQEELDA 627
Cdd:PRK07525 461 GDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTElDNNVSYAGIAEAMGAEGVVVDTQEELGP 540
|
570
....*....|....*....
gi 151946264 628 KLKEFVSTKG---PVLLEV 643
Cdd:PRK07525 541 ALKRAIDAQNegkTTVIEI 559
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
92-647 |
5.09e-74 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 248.35 E-value: 5.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSdKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK07524 2 TTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGS-GIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGT---------DafQEADVVGISR-SCTKWnvmvkSVEELPLRINEAFEIATSGR 241
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSVNRRASLGKgrgklhelpD--QRAMVAGVAAfSHTLM-----SAEDLPEVLARAFAVFDSAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 242 PGPVLVDLPKDVTAAILRNPIPTKTTLPSNAlnqltsRAQDEfvmqSINKAADLINLAKKPVLYVGAGILNHADGprlLK 321
Cdd:PRK07524 154 PRPVHIEIPLDVLAAPADHLLPAPPTRPARP------GPAPA----ALAQAAERLAAARRPLILAGGGALAAAAA---LR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 322 ELSDRAQIPVTTTLQGLGSFDQEDPKSLDmlgmhgcATANLA-----VQNADLIIAVG---ARFDDRVTGNiskfapear 393
Cdd:PRK07524 221 ALAERLDAPVALTINAKGLLPAGHPLLLG-------ASQSLPavralIAEADVVLAVGtelGETDYDVYFD--------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 394 raaaeGR----GGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFA-QINKWKKEypyayMEETPG 468
Cdd:PRK07524 285 -----GGfplpGELIRIDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAADWGAaRVAALRQA-----LRAEWD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 469 SKIKPQTVIkkLSKVANDTGRHVIV---TTGV--GQHQMWAAQHWTWRNPHTfitsgGLGTMGYGLPAAIGAQVAKPESL 543
Cdd:PRK07524 355 PLTAAQVAL--LDTILAALPDAIFVgdsTQPVyaGNLYFDADAPRRWFNAST-----GYGTLGYGLPAAIGAALGAPERP 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 544 VIDIDGDASFNMTLTELSSAVQAGTPVKILILNNeeQGmvtqwqslfYEH--RYSHTHQL--------NPDFIKLAEAMG 613
Cdd:PRK07524 428 VVCLVGDGGLQFTLPELASAVEADLPLIVLLWNN--DG---------YGEirRYMVARDIepvgvdpyTPDFIALARAFG 496
|
570 580 590
....*....|....*....|....*....|....
gi 151946264 614 LKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDK 647
Cdd:PRK07524 497 CAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
96-251 |
1.35e-70 |
|
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: 226.26 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 96 QIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMA 175
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151946264 176 DAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
93-646 |
2.05e-65 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 226.18 E-value: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFG--YPGGAILPVyDAIhnsdKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNV 170
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGqsLPSALFLAA-EAI----GIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 171 VTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWnvmVKSVEElPLRINE----AFEIATSGRPGPVL 246
Cdd:PRK06112 90 VAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTV-AERIDDyvdqAFTAATSGRPGPVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 247 VDLPKDVTAAILRNPIPTKttlpSNALNQLT---SRAQDefvmQSINKAADLINLAKKPVLYVGAGIlnHADGP-RLLKE 322
Cdd:PRK06112 166 LLLPADLLTAAAAAPAAPR----SNSLGHFPldrTVPAP----QRLAEAASLLAQAQRPVVVAGGGV--HISGAsAALAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 323 LSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGmHGCATANLA------VQNADLIIAVGARFDDRVTGNISKFAPEARraa 396
Cdd:PRK06112 236 LQSLAGLPVATTNMGKGAVDETHPLSLGVVG-SLMGPRSPGrhlrdlVREADVVLLVGTRTNQNGTDSWSLYPEQAQ--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 397 aegrggIIHFEVSPKNINKVVQTqIAVEGDATTNLGKMMSKIFPV------KERSEWFAQINKWKKEY-----PYAYMEE 465
Cdd:PRK06112 312 ------YIHIDVDGEEVGRNYEA-LRLVGDARLTLAALTDALRGRdlaaraGRRAALEPAIAAGREAHredsaPVALSDA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 466 TPgskIKPQTVIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHT-FITSGGLGTMGYGLPAAIGAQVAKPESLV 544
Cdd:PRK06112 385 SP---IRPERIMAELQAVLTG---DTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 545 IDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQ-SLFYEHRySHTHQLNPDFIKLAEAMGLKGLRVKKQE 623
Cdd:PRK06112 459 ICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGILGFQKHAEtVKFGTHT-DACHFAAVDHAAIARACGCDGVRVEDPA 537
|
570 580
....*....|....*....|...
gi 151946264 624 ELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK06112 538 ELAQALAAAMAAPGPTLIEVITD 560
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
94-253 |
3.41e-65 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 212.48 E-value: 3.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 94 GGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTP 173
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 174 MADAFADGIPMVVFTGQVPTSAIGTDAFQ-EADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKD 252
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
.
gi 151946264 253 V 253
Cdd:pfam02776 161 V 161
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
496-643 |
1.12e-64 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 210.52 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 496 GVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILIL 575
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151946264 576 NNEEQGMVTQWQSLFYEHRYSHTH---QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEV 643
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
100-643 |
1.04e-63 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 221.22 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPggaILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARA-SGKP-GVVLVTSGPGATNVVTPMADA 177
Cdd:PRK06154 28 EILKEEGVELLFGFP---VNELFDAAAAAG-IRPVIARTERVAVHMADGYARAtSGERvGVFAVQYGPGAENAFGGVAQA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 178 FADGIPMVVFTGQVPTSAIGTDAFQEADVVgiSRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVtaai 257
Cdd:PRK06154 104 YGDSVPVLFLPTGYPRGSTDVAPNFESLRN--YRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVDV---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 258 LRNPIPTkttLPSNALNQLTSRAQDEFVmqSINKAADLINLAKKPVLYVGAGILnHADGPRLLKELSDRAQIPVTTTLQG 337
Cdd:PRK06154 178 LAEELDE---LPLDHRPSRRSRPGADPV--EVVEAAALLLAAERPVIYAGQGVL-YAQATPELKELAELLEIPVMTTLNG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 338 LGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGniskfapearRAAAEGRGgIIHFEVSPKNINKVV 417
Cdd:PRK06154 252 KSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYG----------LPMPEGKT-IIHSTLDDADLNKDY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 418 QTQIAVEGDATTNLGKMMSKI------------FPVKE----RSEWFAQinkWkkeYPYAYMEETPgskIKPQTVIKKLS 481
Cdd:PRK06154 321 PIDHGLVGDAALVLKQMIEELrrrvgpdrgraqQVAAEieavRAAWLAK---W---MPKLTSDSTP---INPYRVVWELQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 482 KVANDtgRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELS 561
Cdd:PRK06154 392 HAVDI--KTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 562 SAVQAGTPVKILILNNEEQGMVTQWQSLFYE-HRyshTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLK---EFVSTKG 637
Cdd:PRK06154 470 TAVRERIPILTILLNNFSMGGYDKVMPVSTTkYR---ATDISGDYAAIARALGGYGERVEDPEMLVPALLralRKVKEGT 546
|
....*.
gi 151946264 638 PVLLEV 643
Cdd:PRK06154 547 PALLEV 552
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
93-645 |
8.96e-61 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 212.93 E-value: 8.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDA--FQEA-DVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDL 249
Cdd:PRK07064 84 ALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 250 PKDVTAAILrnPIPTKTTLPsnalnQLTSRAQDEfvmQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSdraqI 329
Cdd:PRK07064 164 PIDIQAAEI--ELPDDLAPV-----HVAVPEPDA---AAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLG----F 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 330 PVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLavQNADLIIAVGARFDDRVTGNIS-KFAPEarraaaegrggIIHFEV 408
Cdd:PRK07064 230 GVVTSTQGRGVVPEDHPASLGAFNNSAAVEALY--KTCDLLLVVGSRLRGNETLKYSlALPRP-----------LIRVDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 409 SPKNINKVVQTQIAVEGDATTNLGKMMSKifpVKERS----EWFAQINKWKKEypyayMEETPGSKIKPQTVI-KKLSKV 483
Cdd:PRK07064 297 DAAADGRGYPNDLFVHGDAARVLARLADR---LEGRLsvdpAFAADLRAAREA-----AVADLRKGLGPYAKLvDALRAA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 484 ANDTG---RHVIVTTGVgqhqmWAAQHWTWRNPHTFITSGGlGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTEL 560
Cdd:PRK07064 369 LPRDGnwvRDVTISNST-----WGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 561 SSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVL 640
Cdd:PRK07064 443 ATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVL 522
|
....*
gi 151946264 641 LEVEV 645
Cdd:PRK07064 523 VEVDM 527
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
96-251 |
3.61e-56 |
|
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: 187.94 E-value: 3.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 96 QIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGkPGVVLVTSGPGATNVVTPMA 175
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151946264 176 DAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGrPGPVLVDLPK 251
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
475-645 |
3.59e-54 |
|
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: 183.23 E-value: 3.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 475 TVIKKLSKVANDTgrhVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFN 554
Cdd:cd00568 1 RVLAALRAALPED---AIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 555 MTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVS 634
Cdd:cd00568 78 MTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALA 157
|
170
....*....|.
gi 151946264 635 TKGPVLLEVEV 645
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
107-653 |
4.15e-50 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 184.34 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 107 VDTVFGYPGGAILPVYDAIHNS-DKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMV 185
Cdd:PRK08273 18 VRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLDHVPVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 186 VFTGQVPTSAIGTDAFQEADVVGISRS-CTKWNVMVKSVEELPLRINEAFEIATSGRpGPVLVDLPKDVTAAILRNPIPT 264
Cdd:PRK08273 98 AIVGQQARAALGGHYQQEVDLQSLFKDvAGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPNDVQELEYEPPPHA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 265 KTTLPSN---ALNQLTSRAQDefvmqsINKAADLINLAKKPVLYVGAGILNHADGprlLKELSDRAQIPVTTTLQGLGSF 341
Cdd:PRK08273 177 HGTVHSGvgyTRPRVVPYDED------LRRAAEVLNAGRKVAILVGAGALGATDE---VIAVAERLGAGVAKALLGKAAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 342 DQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDdrvtgnISKFapearrAAAEGRGGIIHFEVSPKNINKVVQTQI 421
Cdd:PRK08273 248 PDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEF------LPKEGQARGVQIDIDGRMLGLRYPMEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 422 AVEGDATTNLGKMMSKIfPVKERSEWFAQINKWKKEYpYAYMEE---TPGSKIKPQTVIKKLSKVANDtgrHVIVTTGVG 498
Cdd:PRK08273 316 NLVGDAAETLRALLPLL-ERKKDRSWRERIEKWVARW-WETLEAramVPADPVNPQRVFWELSPRLPD---NAILTADSG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 499 QHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMT-LTELSSAVQ-----AGTPVKI 572
Cdd:PRK08273 391 SCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKywrqwSDPRLIV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 573 LILNNEEQGMVTqwqslfYEHR-------YSHTHQLnPDF--IKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEV 643
Cdd:PRK08273 471 LVLNNRDLNQVT------WEQRvmegdpkFEASQDL-PDVpyARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEV 543
|
570
....*....|
gi 151946264 644 EVDKKVPVLP 653
Cdd:PRK08273 544 KTDPNVPPLP 553
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
471-650 |
2.50e-49 |
|
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: 170.40 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 471 IKPQTVIKKLSKVANDTGrhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGD 550
Cdd:cd02014 2 IHPERVAAELNKRAPDDA---IFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 551 ASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYShTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLK 630
Cdd:cd02014 79 GGFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFG-VDLPNPDFAKIAEAMGIKGIRVEDPDELEAALD 157
|
170 180
....*....|....*....|
gi 151946264 631 EFVSTKGPVLLEVEVDKKVP 650
Cdd:cd02014 158 EALAADGPVVIDVVTDPNEP 177
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
94-649 |
2.29e-48 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 178.38 E-value: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 94 GGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDkFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTP 173
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 174 MADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDV 253
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 254 TAAILRNPIPTKTTLPSNALNQLTSRAqdefvmqsINKAADLINLAKKPVLYVGAGI-LNHADGPrlLKELSDRAQIPVT 332
Cdd:PRK05858 166 AFSMADDDGRPGALTELPAGPTPDPDA--------LARAAGLLAEAQRPVIMAGTDVwWGHAEAA--LLRLAEELGIPVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 333 TTLQGLGSFDQEDPKSLdmlgmhgCATANLAVQNADLIIAVGARFDDRVtgNISKFapearraaaEGRGGIIHFEVSPKN 412
Cdd:PRK05858 236 MNGMGRGVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVF---------GGTAQLVHVDDAPPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 413 INKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEE--TPGSKIKPQTVIKKLSKVANdtgRH 490
Cdd:PRK05858 298 RAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARARDAAElaDDRDPIHPMRVYGELAPLLD---RD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 491 VIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPV 570
Cdd:PRK05858 375 AIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 571 KILILNNEEQGMVTQWQSLFYEhrYSHTHQLNPD--FIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK 648
Cdd:PRK05858 455 VSVIGNNGIWGLEKHPMEALYG--YDVAADLRPGtrYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPS 532
|
.
gi 151946264 649 V 649
Cdd:PRK05858 533 V 533
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
107-653 |
1.61e-47 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 176.72 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 107 VDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVV 186
Cdd:PRK09124 18 VKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 187 FTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGR-------PGPV-LVDLPKDVTAAIL 258
Cdd:PRK09124 98 IAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRgvavvvlPGDVaLKPAPERATPHWY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 259 RNPIPTktTLPSnalnqltsraqdefvMQSINKAADLINLAKKPVLYVGAGIlnhADGPRLLKELSDRAQIPVTTTLQGL 338
Cdd:PRK09124 178 HAPQPV--VTPA---------------EEELRKLAALLNGSSNITLLCGSGC---AGAHDELVALAETLKAPIVHALRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 339 GSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRvtgnisKFAPEarraaaegRGGIIHFEVSPKNINKVVQ 418
Cdd:PRK09124 238 EHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR------QFYPT--------DAKIIQIDINPGSLGRRSP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 419 TQIAVEGDATTNLGKMMSKIFPVKERsewfAQINKWKKEYPYAYME------ETPGSK-IKPQTVIKKLSKVANDTGrhv 491
Cdd:PRK09124 304 VDLGLVGDVKATLAALLPLLEEKTDR----KFLDKALEHYRKARKGlddlavPSDGGKpIHPQYLARQISEFAADDA--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 492 IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVK 571
Cdd:PRK09124 377 IFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 572 ILILNNEEQGMVT--QWQSLFYEHrysHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKV 649
Cdd:PRK09124 457 IVVFNNSVLGFVAmeMKAGGYLTD---GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQE 533
|
....
gi 151946264 650 PVLP 653
Cdd:PRK09124 534 LAMP 537
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
100-653 |
1.89e-46 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 173.64 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFA 179
Cdd:PRK06546 11 EQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYDAHR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 180 DGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATsGRPGPVLVDLPKDVTAailr 259
Cdd:PRK06546 91 SGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTLPGDIAD---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 260 NPIPTKTTlPSNALNQLTSRAQDEfvmQSINKAADLINLAKKPVLYVGAGILN-HADgprlLKELSDRAQIPVTTTLQGL 338
Cdd:PRK06546 166 EPAPEGFA-PSVISPRRPTVVPDP---AEVRALADAINEAKKVTLFAGAGVRGaHAE----VLALAEKIKAPVGHSLRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 339 GSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARF-------DDRVtgniskfapearraaaegrggiIHFEVSPK 411
Cdd:PRK06546 238 EWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpydqflpDVRT----------------------AQVDIDPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 NINKVVQTQIAVEGDATTNLGKMMSKIFPVKERS-------EWFAQINKWKKEYPYAYMEETPgskIKPQTVIKKLSKVA 484
Cdd:PRK06546 296 HLGRRTRVDLAVHGDVAETIRALLPLVKEKTDRRfldrmlkKHARKLEKVVGAYTRKVEKHTP---IHPEYVASILDELA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 485 NDTGrhvIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAV 564
Cdd:PRK06546 373 ADDA---VFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 565 QAGTPVKILILNNEEQGMVtQWQSL---FYEHRYSHTHqlnPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL 641
Cdd:PRK06546 450 LYDLPVKVVVFNNSTLGMV-KLEMLvdgLPDFGTDHPP---VDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALV 525
|
570
....*....|..
gi 151946264 642 EVEVDKKVPVLP 653
Cdd:PRK06546 526 DVVTDPNALSIP 537
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
93-253 |
1.01e-43 |
|
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: 154.63 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 93 TGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVT 172
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 173 PMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRpGPVLVDLPKD 252
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
.
gi 151946264 253 V 253
Cdd:cd07039 160 V 160
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
100-646 |
1.73e-43 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 164.36 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 100 EMMSRQNVDTVFGYPGGAILPVYDAIhnSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFA 179
Cdd:PRK07092 20 DLLRRFGITTVFGNPGSTELPFLRDF--PDDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAFK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 180 DGIPMVVFTGQVPTSAIGTDAFQEA-DVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAil 258
Cdd:PRK07092 98 NHTPLVITAGQQARSILPFEPFLAAvQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDQ-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 259 rnPIPtkttlPSNALNQLTSRAQDEFVMQSInkaADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPV-TTTLQG 337
Cdd:PRK07092 176 --PAE-----PLPARTVSSAVRPDPAALARL---GDALDAARRPALVVGPAV-DRAGAWDDAVRLAERHRAPVwVAPMSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 338 LGSFDQEDP-----------KSLDMLGMHgcatanlavqnaDLIIAVGA---RFDDRVTGNIskfapearraaAEGRGGI 403
Cdd:PRK07092 245 RCSFPEDHPlfagflpasreKISALLDGH------------DLVLVIGApvfTYHVEGPGPH-----------LPEGAEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 404 IHFevspknINKVVQTQIAVEGDA-TTNLGKMMSKIFPVKERSEWFAqinkwKKEYPYAYMEETPGSKIKPQTVIKKLSK 482
Cdd:PRK07092 302 VQL------TDDPGEAAWAPMGDAiVGDIRLALRDLLALLPPSARPA-----PPARPMPPPAPAPGEPLSVAFVLQTLAA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 483 VAndtGRHVIV------TTGVgqhqMWaaQHWTWRNPHTFIT--SGGLGtmgYGLPAAIGAQVAKPESLVIDIDGDASFN 554
Cdd:PRK07092 371 LR---PADAIVveeapsTRPA----MQ--EHLPMRRQGSFYTmaSGGLG---YGLPAAVGVALAQPGRRVIGLIGDGSAM 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 555 MTLTELSSAVQAGTPVKILILNNEEQGMVtQWqslfyehrYSHTHQLNP---------DFIKLAEAMGLKGLRVKKQEEL 625
Cdd:PRK07092 439 YSIQALWSAAQLKLPVTFVILNNGRYGAL-RW--------FAPVFGVRDvpgldlpglDFVALARGYGCEAVRVSDAAEL 509
|
570 580
....*....|....*....|.
gi 151946264 626 DAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK07092 510 ADALARALAADGPVLVEVEVA 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
289-431 |
3.09e-42 |
|
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: 149.64 E-value: 3.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 289 INKAADLINLAKKPVLYVGAGILNhADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNAD 368
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRR-SGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151946264 369 LIIAVGARFDD-RVTGNISKFAPearraaaegRGGIIHFEVSPKNINKVVQTQIAVEGDATTNL 431
Cdd:pfam00205 80 LVLAVGARFDDiRTTGKLPEFAP---------DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETL 134
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
473-646 |
6.53e-41 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 147.43 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 473 PQTVIKKLSKVandTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDAS 552
Cdd:cd02010 1 PQRIVHDLRAV---MGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 553 FNMTLTELSSAVQAGTPVKILILNNEEQGMVtQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEF 632
Cdd:cd02010 78 FMMNSQELETAVRLKIPLVVLIWNDNGYGLI-KWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERA 156
|
170
....*....|....
gi 151946264 633 VSTKGPVLLEVEVD 646
Cdd:cd02010 157 LAADGVHVIDCPVD 170
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
106-648 |
6.52e-40 |
|
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: 154.55 E-value: 6.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 106 NVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGkPGVVLVTSGPGATNVVTPMADAFADGIPMV 185
Cdd:COG3961 19 GIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAERVPVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 186 VFTGQVPTSA----------IGT---DAFQEadvvgisrsctkwnvMVKSV---------EELPLRINEAFEIATSGRPg 243
Cdd:COG3961 98 HIVGAPGTRAqrrgpllhhtLGDgdfDHFLR---------------MFEEVtvaqavltpENAAAEIDRVLAAALREKR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 244 PVLVDLPKDVTAAilrnPIPTKTTLPSNALNQLTSRAQDEFVmqsiNKAADLINLAKKPVLYvgAGILNHADGPR-LLKE 322
Cdd:COG3961 162 PVYIELPRDVADA----PIEPPEAPLPLPPPASDPAALAAAV----AAAAERLAKAKRPVIL--AGVEVHRFGLQeELLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 323 LSDRAQIPVTTTLQGLGSFDQEDPKSLdmlGMHGCATANLAVQ----NADLIIAVGARFDDRVTGNIS-KFAPEARRAaa 397
Cdd:COG3961 232 LAEKTGIPVATTLLGKSVLDESHPQFI---GTYAGAASSPEVReyveNADCVLCLGVVFTDTNTGGFTaQLDPERTID-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 398 egrggIIHFEVSpknINKVVQTQIAVEgDATTNLGKMMSK---IFPVKERS---------------EWFAQINKWkkeyp 459
Cdd:COG3961 307 -----IQPDSVR---VGGHIYPGVSLA-DFLEALAELLKKrsaPLPAPAPPpppppaapdapltqdRLWQRLQAF----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 460 yaymeetpgskIKPQTVIkklskVAnDTGrhvivTT--GVGQHQMwaaqhwtwrnPH--TFITSGGLGTMGYGLPAAIGA 535
Cdd:COG3961 373 -----------LDPGDIV-----VA-DTG-----TSlfGAADLRL----------PEgaTFIAQPLWGSIGYTLPAALGA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 536 QVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNE----EQGMVTQwqslfyEHRYSHTHQLnpDFIKLAEA 611
Cdd:COG3961 421 ALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDgytiERAIHGP------DGPYNDIANW--DYAKLPEA 492
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 151946264 612 MG---LKGLRVKKQEELDAKLKE-FVSTKGPVLLEVEVDKK 648
Cdd:COG3961 493 FGggnALGFRVTTEGELEEALAAaEANTDRLTLIEVVLDKM 533
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
91-647 |
3.94e-37 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 146.68 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 91 GLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPK-----HEQGAGHMAEGYARASGKPGVVLVTSGP 165
Cdd:PRK08327 6 MYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRPLPEfvicpHEIVAISMAHGYALVTGKPQAVMVHVDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 166 GATNVVTPMADAFADGIPMVVFTGQVPTS---AIGT-DAF----QEA-DVVGISRSCTKWNVMVKSVEELPLRINEAFEI 236
Cdd:PRK08327 86 GTANALGGVHNAARSRIPVLVFAGRSPYTeegELGSrNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 237 ATSGRPGPVLVDLPKDVTAAilrnpiPTKTTLPSNALNQLTSR-AQDEfvmQSINKAADLINLAKKPVLYVGAGILNHAd 315
Cdd:PRK08327 166 AMSEPKGPVYLTLPREVLAE------EVPEVKADAGRQMAPAPpAPDP---EDIARAAEMLAAAERPVIITWRAGRTAE- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 316 GPRLLKELSDRAQIPVtttLQGLGS---FDQEDPksldmlgMHGCATANLAVQNADLIIAVGAR---FDDRVTGNISKFa 389
Cdd:PRK08327 236 GFASLRRLAEELAIPV---VEYAGEvvnYPSDHP-------LHLGPDPRADLAEADLVLVVDSDvpwIPKKIRPDADAR- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 390 pearraaaegrggIIHFEVSP----------------KNINKVVQTQIAVEGDATTNLGKMMskifpVKERSEWFAQINK 453
Cdd:PRK08327 305 -------------VIQIDVDPlksriplwgfpcdlciQADTSTALDQLEERLKSLASAERRR-----ARRRRAAVRELRI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 454 WKKEYPYAYMEETPGSK-IKPQTVIKKLSKVANDTGrhVIVTT-GVGQHQMWAAQhwtwrnPHTFITSGGLGTMGYGLPA 531
Cdd:PRK08327 367 RQEAAKRAEIERLKDRGpITPAYLSYCLGEVADEYD--AIVTEyPFVPRQARLNK------PGSYFGDGSAGGLGWALGA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 532 AIGAQVAKPESLVIDIDGDASFNMTLTE--LSSAVQAGTPVKILILNNEEQGMVTQWQSLFY-------EHRYSHTHQL- 601
Cdd:PRK08327 439 ALGAKLATPDRLVIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaarKGTFPGTDFDp 518
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 151946264 602 NPDFIKLAEAMGLKGLRVKKQEELDAKLKEFV----STKGPVLLEVEVDK 647
Cdd:PRK08327 519 RPDFAKIAEAFGGYGERVEDPEELKGALRRALaavrKGRRSAVLDVIVDR 568
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
106-646 |
1.48e-31 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 130.11 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 106 NVDTVFGYPGgaiLPVYD--AIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP 183
Cdd:PRK09259 24 GIDTIYGVVG---IPITDlaRLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANATTNCFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 184 MVVFTGQVPTSAIGTDA--FQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNP 261
Cdd:PRK09259 101 MIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLAQTMDAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 262 IPTKT--TLPSNALNQLTSRAqdefvmqSINKAADLINLAKKPVLYVGAGIlNHADGPRLLKELSDRAQIPVTTTLQGLG 339
Cdd:PRK09259 181 EALTSlvKVVDPAPAQLPAPE-------AVDRALDLLKKAKRPLIILGKGA-AYAQADEQIREFVEKTGIPFLPMSMAKG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 340 SFDQEDPKSldmlgmhGCATANLAVQNADLIIAVGARF-------DDRVTGNISKFapearraaaegrggiIHFEVSPKN 412
Cdd:PRK09259 253 LLPDTHPQS-------AAAARSLALANADVVLLVGARLnwllshgKGKTWGADKKF---------------IQIDIEPQE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 413 INKVVQTQIAVEGDATTNLGKMMSKI--FPVKERSEWFAQINKwKKEYPYAYMEETPGSKIKP----------QTVIKK- 479
Cdd:PRK09259 311 IDSNRPIAAPVVGDIGSVMQALLAGLkqNTFKAPAEWLDALAE-RKEKNAAKMAEKLSTDTQPmnfynalgaiRDVLKEn 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 480 -----LSKVAN--DTGRHVIvttgvGQHQmwaaqhwtwrnPHTFITSGGLGTMGYGLPAAIGAQVA--KPeslVIDIDGD 550
Cdd:PRK09259 390 pdiylVNEGANtlDLARNII-----DMYK-----------PRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 551 ASFNMTLTELSSAVQAGTPVKILILNNeeqGMVtqwqslfY---EHRYSHTHQ-----LNPD--FIKLAEAMGLKGLRVK 620
Cdd:PRK09259 451 SAFGFSGMEVETICRYNLPVTVVIFNN---GGI-------YrgdDVNLSGAGDpsptvLVHHarYDKMMEAFGGVGYNVT 520
|
570 580
....*....|....*....|....*.
gi 151946264 621 KQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK09259 521 TPDELRHALTEAIASGKPTLINVVID 546
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
468-647 |
1.93e-31 |
|
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: 121.46 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 468 GSKIKPQTVIKKLSKVANDtgrHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDI 547
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPE---DAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 548 DGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDA 627
Cdd:cd02013 78 AGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|...
gi 151946264 628 KLKEFVSTKG---PVLLEVEVDK 647
Cdd:cd02013 158 ALQKAIAMMAegkTTVIEIVCDQ 180
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
473-645 |
5.50e-30 |
|
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: 116.54 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 473 PQTVIKKLSKVANDTGrhVIVTTGVGQHQMwAAQHWTWRNPHTFITSGGlGTMGYGLPAAIGAQVAKPESLVIDIDGDAS 552
Cdd:cd02002 3 PEYLAAALAAALPEDA--IIVDEAVTNGLP-LRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 553 FNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQL-------NPDFIKLAEAMGLKGLRVKKQEEL 625
Cdd:cd02002 79 FMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPDgldlldpGIDFAAIAKAFGVEAERVETPEEL 158
|
170 180
....*....|....*....|
gi 151946264 626 DAKLKEFVSTKGPVLLEVEV 645
Cdd:cd02002 159 DEALREALAEGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
503-646 |
7.92e-26 |
|
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: 104.54 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 503 WAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGM 582
Cdd:cd02004 28 WARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQ 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151946264 583 VTQWQSLFYEHRYSHTHQL-NPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:cd02004 108 GLDGQQLSYGLGLPVTTLLpDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGKPALINVIID 172
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
500-653 |
1.62e-21 |
|
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: 93.14 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 500 HQMWAAqhwtwRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEE 579
Cdd:cd02003 30 HKLWRA-----RTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 580 QG------MVTQWQSLFYEHRYSHTHQLNP-------DFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:cd02003 105 FGcinnlqESTGSGSFGTEFRDRDQESGQLdgallpvDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
....*..
gi 151946264 647 KKVPVLP 653
Cdd:cd02003 185 PKSMTPG 191
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
471-647 |
4.58e-21 |
|
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: 91.57 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 471 IKPQTVIKKLSKVandTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGD 550
Cdd:cd02006 8 IKPQRVYEEMNKA---FGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 551 ASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLF---YEHRYSHTHQLNP-------DFIKLAEAMGLKGLRVK 620
Cdd:cd02006 85 YDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFdmdYQVNLAFENINSSelggygvDHVKVAEGLGCKAIRVT 164
|
170 180 190
....*....|....*....|....*....|.
gi 151946264 621 KQEELDAKLKE----FVSTKGPVLLEVEVDK 647
Cdd:cd02006 165 KPEELAAAFEQakklMAEHRVPVVVEAILER 195
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
515-647 |
3.95e-19 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 85.66 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 515 TFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNE----E---QGM----- 582
Cdd:cd02005 42 RFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDgytiEraiHGPeasyn 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151946264 583 -VTQWqslfyehryshthqlnpDFIKLAEAMGL----KGLRVKKQEELDAKLKEFVST-KGPVLLEVEVDK 647
Cdd:cd02005 122 dIANW-----------------NYTKLPEVFGGggggLSFRVKTEGELDEALKDALFNrDKLSLIEVILPK 175
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
106-200 |
1.40e-16 |
|
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: 77.53 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 106 NVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGkPGVVLVTSGPGATNVVTPMADAFADGIPMV 185
Cdd:cd07038 11 GVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEHVPVV 89
|
90
....*....|....*
gi 151946264 186 VFTGQVPTSAIGTDA 200
Cdd:cd07038 90 HIVGAPSTKAQASGL 104
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
92-645 |
2.00e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 79.53 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 92 LTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVV 171
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 172 TPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPK 251
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 252 DV-------TAAILRNPIPTKttlpsnalnqltsraqdeFVMQSINKAADLINLAKKPVLYV-GAGILNHAdgprllKEL 323
Cdd:PRK12474 165 DVawneaayAAQPLRGIGPAP------------------VAAETVERIAALLRNGKKSALLLrGSALRGAP------LEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 324 SDRAQIPVTTTLQGLGSFDQEDpksldmLGMHGCATANLA---------VQNADLIIAVGARfddrvtGNISKFAPEARR 394
Cdd:PRK12474 221 AGRIQAKTGVRLYCDTFAPRIE------RGAGRVPIERIPyfheqitafLKDVEQLVLVGAK------PPVSFFAYPGKP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 395 AAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPvkersewfaqinkwkkeypyaymeETPGSKIkpq 474
Cdd:PRK12474 289 SWGAPPGCEIVYLAQPDEDLAQALQDLADAVDAPAEPAARTPLALP------------------------ALPKGAL--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 475 TVIKKLSKVANDTGRHVIV----TTGVGQHQMwaaqHWTWRNPHTFITSGGlGTMGYGLPAAIGAQVAKPESLVIDIDGD 550
Cdd:PRK12474 342 NSLGVAQLIAHRTPDQAIYadeaLTSGLFFDM----SYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGD 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 551 ASFNMTLTELSSAVQAGTPVKILILNNeeQGMVTQWQSLFY---------EHRYSHTHQLNPDFIKLAEAMGLKGLRVKK 621
Cdd:PRK12474 417 GGAAYTMQALWTMARENLDVTVVIFAN--RSYAILNGELQRvgaqgagrnALSMLDLHNPELNWMKIAEGLGVEASRATT 494
|
570 580
....*....|....*....|....
gi 151946264 622 QEELDAKLKEFVSTKGPVLLEVEV 645
Cdd:PRK12474 495 AEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
139-250 |
2.04e-15 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 74.07 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 139 EQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNV 218
Cdd:cd07037 44 ERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSV 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 151946264 219 MVKSVEELP------LRINEAFEIATSGRPGPVLVDLP 250
Cdd:cd07037 124 DLPPPEDDDdlwyllRLANRAVLEALSAPPGPVHLNLP 161
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
105-645 |
2.41e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 79.12 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 105 QNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM 184
Cdd:PRK07586 14 GGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLANLHNARRARTPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 185 VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPT 264
Cdd:PRK07586 94 VNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADVAWSEGGPPAPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 265 kttlpsnalnqLTSRAQDEFVMQSINKAADLINLAKKPVLYVG-----------AGILNHADGPRLLKELSD-RAQipvt 332
Cdd:PRK07586 174 -----------PPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGgralrerglaaAARIAAATGARLLAETFPaRME---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 333 ttlQGLGSFDQED-PKSLDMlgmhgcATANLAvqNADLIIAVGARfddrvtGNISKFAPEARRAAAEGRGGIIHfevspk 411
Cdd:PRK07586 239 ---RGAGRPAVERlPYFAEQ------ALAQLA--GVRHLVLVGAK------APVAFFAYPGKPSRLVPEGCEVH------ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 412 ninkvvqTQIAVEGDATTNLgkmmskifpvkersEWFAQINKWKKEYPYA---YMEETPGSKIKPQTvikklskVANDTG 488
Cdd:PRK07586 296 -------TLAGPGEDAAAAL--------------EALADALGAKPAAPPLaapARPPLPTGALTPEA-------IAQVIA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 489 RHV----IV-----TTGVGQHQMWAAQhwtwrNPHTFITSGGlGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTE 559
Cdd:PRK07586 348 ALLpenaIVvdesiTSGRGFFPATAGA-----APHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQA 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 560 LSSAVQAGTPVKILILNNeeqgmvtqwqslfyeHRYS-----------------HTHQL---NP--DFIKLAEAMGLKGL 617
Cdd:PRK07586 422 LWTQARENLDVTTVIFAN---------------RAYAilrgelarvgagnpgprALDMLdldDPdlDWVALAEGMGVPAR 486
|
570 580
....*....|....*....|....*...
gi 151946264 618 RVKKQEELDAKLKEFVSTKGPVLLEVEV 645
Cdd:PRK07586 487 RVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
491-647 |
3.53e-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: 51.16 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 491 VIVTTGVGQHQMWAAQH-WTWRNPHTFITSGGlgtMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELS-SAVQAGT 568
Cdd:cd03371 18 VVSTTGMTSRELFELRDrPGGGHAQDFLTVGS---MGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLAtIGGLAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 569 PVKILILNNEEQGMV-TQwqslfyehrysHTHQLNPDFIKLAEAMGL-KGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:cd03371 95 NLIHIVLNNGAHDSVgGQ-----------PTVSFDVSLPAIAKACGYrAVYEVPSLEELVAALAKALAADGPAFIEVKVR 163
|
.
gi 151946264 647 K 647
Cdd:cd03371 164 P 164
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
107-379 |
4.25e-07 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 53.17 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 107 VDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKpGVVLVTSGPGATNVVTPMADAFADGIPMVV 186
Cdd:PLN02573 31 VTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGV-GACVVTFTVGGLSVLNAIAGAYSENLPVIC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 187 FTGQvPTS-----------AIGTDAF-QEADVVgisRSCTKWNVMVKSVEELPLRINEAfeIATS-GRPGPVLV----DL 249
Cdd:PLN02573 110 IVGG-PNSndygtnrilhhTIGLPDFsQELRCF---QTVTCYQAVINNLEDAHELIDTA--ISTAlKESKPVYIsvscNL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 250 PKDVTAAILRNPIPtkTTLPSNALNQLTSRAqdefvmqSINKAADLINLAKKPVLyVGAGILNHADGPRLLKELSDRAQI 329
Cdd:PLN02573 184 AAIPHPTFSREPVP--FFLTPRLSNKMSLEA-------AVEAAAEFLNKAVKPVL-VGGPKLRVAKACKAFVELADASGY 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 151946264 330 PVTTTLQGLGSFDQEDPKsldMLGMHGCA--TANLA--VQNADLIIAVGARFDD 379
Cdd:PLN02573 254 PVAVMPSAKGLVPEHHPH---FIGTYWGAvsTPFCAeiVESADAYLFAGPIFND 304
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
491-651 |
6.91e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 50.21 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 491 VIVTTGVGQHQMWAAQHwtwrNPHTFITsggLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSS-AVQAGTP 569
Cdd:PRK06163 32 VIGGIGNTNFDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 570 VKILILNNeeqGM--VTQWQSLFYEHryshthqlNPDFIKLAEAMGL-KGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:PRK06163 105 LTIIVMDN---GVyqITGGQPTLTSQ--------TVDVVAIARGAGLeNSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
....*
gi 151946264 647 KKVPV 651
Cdd:PRK06163 174 DKPGV 178
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
521-638 |
1.17e-05 |
|
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: 46.50 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 521 GLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMT-LTELSSAVQAGTPVKILILNNEEQGMvTQWQSLFYEHRYSHTH 599
Cdd:cd02008 49 TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSgILGLINAVYNKANITVVILDNRTTAM-TGGQPHPGTGKTLTEP 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 151946264 600 QLNPDFIKLAEAMGLKGLRVKKQEELDA---KLKEFVSTKGP 638
Cdd:cd02008 128 TTVIDIEALVRAIGVKRVVVVDPYDLKAireELKEALAVPGV 169
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
476-654 |
1.79e-05 |
|
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: 45.74 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 476 VIKKLSKVANDtgrhVIVTTGVG--QHQMWAAQHwtwrNPHTFITsggLGTMGYGLPAAIGAQVAKPESlVIDIDGDASF 553
Cdd:cd03372 4 AIKTLIADLKD----ELVVSNIGfpSKELYAAGD----RPLNFYM---LGSMGLASSIGLGLALAQPRK-VIVIDGDGSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 554 NMTLTELSS-AVQAGTPVKILILNNE---EQGMVTqwqslfyehrySHTHqLNPDFIKLAEAMGLKGLRVKKQEELDAKL 629
Cdd:cd03372 72 LMNLGALATiAAEKPKNLIIVVLDNGaygSTGNQP-----------THAG-KKTDLEAVAKACGLDNVATVASEEAFEKA 139
|
170 180
....*....|....*....|....*...
gi 151946264 630 KEFVStKGPVLLEVEVD---KKVPVLPM 654
Cdd:cd03372 140 VEQAL-DGPSFIHVKIKpgnTDVPNIPR 166
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
532-646 |
1.01e-04 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 43.35 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 532 AIGAQVA--KPESLVIdidGDASFNMTLTELSSAVQAGTPVKILILNNeeQG-----MVTQWQSLFYEHRYSHTHQlNPD 604
Cdd:cd02009 60 ALGIALAtdKPTVLLT---GDLSFLHDLNGLLLGKQEPLNLTIVVINN--NGggifsLLPQASFEDEFERLFGTPQ-GLD 133
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 151946264 605 FIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVD 646
Cdd:cd02009 134 FEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
476-645 |
1.39e-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: 42.86 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 476 VIKKLSKVANDTGrhVIVTTGVGQHQMWAAQHwtwRNPHTFItsggLGTMGygLPAAIGAQVA-KPESLVIDIDGDASFN 554
Cdd:cd02001 4 AIAEIIEASGDTP--IVSTTGYASRELYDVQD---RDGHFYM----LGSMG--LAGSIGLGLAlGLSRKVIVVDGDGSLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 555 MTLTELSS-AVQAGTPVKILILNNEEQGMvTQWQSlfyehryshTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFV 633
Cdd:cd02001 73 MNPGVLLTaGEFTPLNLILVVLDNRAYGS-TGGQP---------TPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLL 142
|
170
....*....|..
gi 151946264 634 STKGPVLLEVEV 645
Cdd:cd02001 143 ATTGPTLLHAPI 154
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
139-250 |
2.39e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 41.38 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151946264 139 EQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTK--W 216
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRffF 427
|
90 100 110
....*....|....*....|....*....|....*....
gi 151946264 217 NVMVKSvEELPLR-----INEAFEIATSGRPGPVLVDLP 250
Cdd:PLN02980 428 NLPPPT-DLIPARmvlttLDSAVHWATSSPCGPVHINCP 465
|
|
| |
