|
Name |
Accession |
Description |
Interval |
E-value |
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
1-646 |
0e+00 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 1148.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 1 MGKLRLTTAQALVKFLDNQYLEVDGVELKFVKGIFAIFGHGNVLGLGQALEQDSGDMRVYQGRNEQGMAHAATGFARQAL 80
Cdd:COG3962 2 MKTIRLTVAQALVRFLANQYVERDGEEQPLFAGVFGIFGHGNVAGLGQALEQDPDELPTYQGRNEQGMAHAAIAYAKQKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 81 RRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQSYDLSISTNDAFRAVSKYWDRITRPE 160
Cdd:COG3962 82 RRRIMACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLEHFHDPTISVNDAFRPVSRYWDRITRPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 161 QLMSACINAMRVLTDPAETGAVTLCLPQDVQGEAWDYPESFFARRVHRLDRRPASAAQLADAVAAIKASRKPLIVCGGGV 240
Cdd:COG3962 162 QLMSALPRAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRIRRPPPDPAELARAVELIRAAKRPLIIAGGGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 241 KYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQHP 320
Cdd:COG3962 242 RYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLQDFTTGSKTLFANP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 321 EVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAGWGAQIESVQSRQLKETQRVYQAVWQeksfvpeidd 400
Cdd:COG3962 322 DVRFVNINVARFDAYKHDALPVVADAREGLEALTEALAGWRYPAAWTDEAAELKAEWDAEVDRLYAPTNG---------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 401 hldresvyrefrqitdSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGV 480
Cdd:COG3962 392 ----------------GLPTQAQVIGAVNEAAGPDDIVVCAAGSLPGDLHKLWRTRDPGTYHVEYGYSCMGYEIAGGLGV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 481 KLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEFRYRQPETGQLQGGLVP 560
Cdd:COG3962 456 KLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFGCINRLQMSTGSQSFGTELRDRDTETGRLDGGLLP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 561 VDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLPKTMVHKYGSWWNVGVAQTALSERIRKVAQMINEKR 640
Cdd:COG3962 536 VDFAANAASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKTDPKTMTPGGGSWWDVGVAEVSERESVRAARAEYEEAR 615
|
....*.
gi 1757862790 641 AQARDY 646
Cdd:COG3962 616 AKQRRY 621
|
|
| myo_inos_iolD |
TIGR04377 |
3,5/4-trihydroxycyclohexa-1,2-dione hydrolase; Members of this protein family, 3,5 ... |
5-644 |
0e+00 |
|
3,5/4-trihydroxycyclohexa-1,2-dione hydrolase; Members of this protein family, 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (iolD), represent one of eight enzymes in a pathway converting myo-inositol to acetyl-CoA. IolD hydrolyzes the cyclic molecule 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione to yield 5-deoxy-D-glucuronic acid. TPP is a cofactor. [Energy metabolism, Sugars]
Pssm-ID: 275170 [Multi-domain] Cd Length: 615 Bit Score: 1060.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKFLDNQYLEVDGVELKFVKGIFAIFGHGNVLGLGQALEQDSGDMRVYQGRNEQGMAHAATGFARQALRRQI 84
Cdd:TIGR04377 1 RLTMAQALVRFLAAQYVERDGEEVPFFAGVFAIFGHGNVAGLGEALEEDPDDLPTYRGRNEQGMAHAAIAYAKQKNRRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 IACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMS 164
Cdd:TIGR04377 81 MACTSSIGPGATNMVTAAALATVNRLPVLLLPGDTFATRQPDPVLQQLEDFSDLTVSVNDAFRPVSRYFDRITRPEQLMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 165 ACINAMRVLTDPAETGAVTLCLPQDVQGEAWDYPESFFARRVHRLDRRPASAAQLADAVAAIKASRKPLIVCGGGVKYSG 244
Cdd:TIGR04377 161 ALPNAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRIRRPEPDPAELERAVAAIRAAKKPLIVAGGGVHYSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 245 AGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQHPEVRF 324
Cdd:TIGR04377 241 AGEALAAFAEKHGIPVAETQAGKGALPWDHPLNLGAIGVTGTLAANALAAEADLVIAVGTRLQDFTTASKTLFQNPDVRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 325 LNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAGWGAQIESVQSRQLKETQRVYQAvwqeksfvpeiddhldr 404
Cdd:TIGR04377 321 VNINVARFDAYKHDALPLVADARAGLEALSEALGGYRADSAWAAEAAAAKAAWDAEVDRLYAA----------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 405 esvyrefRQITDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQ 484
Cdd:TIGR04377 384 -------EYTAGGLPTQAEVIGAVNRAAGPDDVVVCAAGSLPGDLHKLWRTRDPGGYHMEYGYSCMGYEIAGGLGVKLAE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 485 PQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEFRYrqPETGQLQGGLVPVDFA 564
Cdd:TIGR04377 457 PDREVYVMVGDGSYLMLNSELATSVQEGKKIIVVLLDNRGFGCINNLQMSTGGASFNTELRY--EDTGRLDGGLLPVDFA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 565 TIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLPKTMVHKYGSWWNVGVAQTALSERIRKVAQMINEKRAQAR 644
Cdd:TIGR04377 535 AHAAALGAKTYKVTTIAELEAALARAKAADRTTLIVIDTDPKTMTEGYGSWWDVGVAEVSERESVRKAREEYEEAKKAQR 614
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
421-624 |
3.36e-108 |
|
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: 325.03 E-value: 3.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 421 QSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMM 500
Cdd:cd02003 1 QTEVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 501 LHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEFRYRQPETGQLQGGLVPVDFATIAAGYGCKTWRVTTL 580
Cdd:cd02003 81 LHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDRDQESGQLDGALLPVDFAANARSLGARVEKVKTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1757862790 581 DELRHALDAARRETVSTLIDIKVLPKTMVHKYGSWWNVGVAQTA 624
Cdd:cd02003 161 EELKAALAKAKASDRTTVIVIKTDPKSMTPGYGSWWDVGVAEVS 204
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
5-605 |
5.84e-106 |
|
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: 331.35 E-value: 5.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKFLDNQylevdGVELkfvkgIFAIFGhGNVLGLGQALEQDSGdMRVYQGRNEQGMAHAATGFARqaLRRQI 84
Cdd:COG0028 2 KMTGADALVEALEAE-----GVET-----VFGVPG-GAILPLYDALRRQSG-IRHILVRHEQGAAFMADGYAR--ATGKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 IACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATrqpdpvlqQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMS 164
Cdd:COG0028 68 GVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTS--------LIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 165 ACINAMRVLTDPaETGAVTLCLPQDVQGEAWDY-PESFFARRVHRldRRPASAAQLADAVAAIKASRKPLIVCGGGVKYS 243
Cdd:COG0028 140 VLRRAFRIATSG-RPGPVVLDIPKDVQAAEAEEePAPPELRGYRP--RPAPDPEAIEEAAELLAAAKRPVILAGGGARRA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 244 GAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTaSKWIFQHPEVR 323
Cdd:COG0028 217 GAAEELRALAERLGAPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVT-GNWDEFAPDAK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 324 FLNINVsnfDAWKLD-----GIAMLADAREAMTALDAALADSGWQ-AGWGAQIESVQSRQLKETQRvyqavwqeksfvpe 397
Cdd:COG0028 296 IIHIDI---DPAEIGknypvDLPIVGDAKAVLAALLEALEPRADDrAAWLARIAAWRAEYLAAYAA-------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 398 iddhldresvyrefrqiTDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAA 477
Cdd:COG0028 359 -----------------DDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAA 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 478 LGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-MEHGMDSFGTEFRyrqpetgqlqg 556
Cdd:COG0028 422 IGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQeLFYGGRYSGTDLP----------- 490
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1757862790 557 glvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLP 605
Cdd:COG0028 491 ---NPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDP 536
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
5-603 |
1.84e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 181.13 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKfldnqYLEVDGVELkfvkgIFAIFGhGNVLGLGQALeQDSgDMRVYQGRNEQGMAHAATGFARQALRRQI 84
Cdd:PRK06048 7 KMTGARAIIK-----CLEKEGVEV-----IFGYPG-GAIIPVYDEL-YDS-DLRHILVRHEQAAAHAADGYARATGKVGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 iaCTSSIGPGAANMITAAGTASANRIPLLLLPGDVfatrqPDPVLqqieqsydlsisTNDAFRA--VSKYWDRITRPEQL 162
Cdd:PRK06048 74 --CVATSGPGATNLVTGIATAYMDSVPIVALTGQV-----PRSMI------------GNDAFQEadITGITMPITKHNYL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 163 MSACINAMRVLTDP---AETG---AVTLCLPQDVQGEA--WDYPESFFAR------RVHRLDRRPASAAqladavaaIKA 228
Cdd:PRK06048 135 VQDAKDLPRIIKEAfhiASTGrpgPVLIDLPKDVTTAEidFDYPDKVELRgykptyKGNPQQIKRAAEL--------IMK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 229 SRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSD 308
Cdd:PRK06048 207 AERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 309 FTTASKWIFQhPEVRFLNINVSNFDAWK---LDgIAMLADAREAMTALdaaladsgwqagwgaqIESVQSRQLKEtqrvy 385
Cdd:PRK06048 287 RVTGKLASFA-PNAKIIHIDIDPAEISKnvkVD-VPIVGDAKQVLKSL----------------IKYVQYCDRKE----- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 386 qavWQEKsfvpeIDDhLDREsvYREFRQITDSTLTQSSVLGVLNETLPaEAVIVAAAGSLPGDLQRVWRNRAENTYHVEY 465
Cdd:PRK06048 344 ---WLDK-----INQ-WKKE--YPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKYKYPRTFITSG 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 466 GYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehgmdSFGTEFR 545
Cdd:PRK06048 412 GLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQ------ELFYDKR 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1757862790 546 YRQPETGQlqgglvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK06048 486 YSHTCIKG------SVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIV 537
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
21-603 |
1.78e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 175.80 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 21 LEVDGVELKFVKGIFAIFGHGNvLGLGQALEQD--SGDMRVYQGRNEQGMAHAATGFARQALRRQIiaCTSSIGPGAANM 98
Cdd:PRK06456 7 ILVDSLKREGVKVIFGIPGLSN-MQIYDAFVEDlaNGELRHVLMRHEQAAAHAADGYARASGVPGV--CTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 99 ITAAGTASANRIPLLLLPGDVfatrqPDPVLQQIE-QSYDlsisTNDAFRAVSKYWDRITRPEQLMSACINAMRVLTDpA 177
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQV-----PRSVMGKMAfQEAD----AMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATT-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 178 ETGAVTLCLPQDVQGEAWD---YPESFFARRVHRLDRRPASAAQLADAVAAIKASRkPLIVCGGGVKYSGAGEALSRFAE 254
Cdd:PRK06456 154 RPGPVVIDIPRDIFYEKMEeikWPEKPLVKGYRDFPTRIDRLALKKAAEILINAER-PIILVGTGVVWSNATPEVLELAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 255 RYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQHPEVRFLNINVSNFD- 333
Cdd:PRK06456 233 LLHIPIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETRKKFIMVNIDPTDg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 334 --AWKLDgIAMLADAREAMTALDAALADSGWQAGWGAQIesvqsRQLKETQRVYQAVWqeksfvpeiddhldresvYREf 411
Cdd:PRK06456 313 ekAIKVD-VGIYGNAKIILRELIKAITELGQKRDRSAWL-----KRVKEYKEYYSQFY------------------YTE- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 412 rqiTDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYS 491
Cdd:PRK06456 368 ---ENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 492 LVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-MEHGMDSFGTEFryrqpetgqlqgGLVPvDFATIAAGY 570
Cdd:PRK06456 445 LDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQVQdLFFGKRIVGVDY------------GPSP-DFVKLAEAF 511
|
570 580 590
....*....|....*....|....*....|...
gi 1757862790 571 GCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK06456 512 GALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPV 544
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
6-603 |
5.40e-47 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 174.01 E-value: 5.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 6 LTTAQALVKFLDNQylevdGVELkfvkgIFAIFG-HGNVLGLGQAleqDSGdMRVYQGRNEQGMAHAATGFARQALRRQI 84
Cdd:PRK07524 2 TTCGEALVRLLEAY-----GVET-----VFGIPGvHTVELYRGLA---GSG-IRHVTPRHEQGAGFMADGYARVSGKPGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 iaCTSSIGPGAANMITAAGTASANRIPLLLLPGdVFATRQ-----------PDpvlQQieqsydlsistnDAFRAVSKYW 153
Cdd:PRK07524 68 --CFIITGPGMTNIATAMGQAYADSIPMLVISS-VNRRASlgkgrgklhelPD---QR------------AMVAGVAAFS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 154 DRITRPEQLMSACINAMRVLtDPAETGAVTLCLPQDVQGEAWDYPESffaRRVHRLDRRPASAAQLADAVAAIKASRKPL 233
Cdd:PRK07524 130 HTLMSAEDLPEVLARAFAVF-DSARPRPVHIEIPLDVLAAPADHLLP---APPTRPARPGPAPAALAQAAERLAAARRPL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 234 IVCGGGVKysGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGvgeTGCLAA-NLLAKEADLVIGVGTRF--SDFT 310
Cdd:PRK07524 206 ILAGGGAL--AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGA---SQSLPAvRALIAEADVVLAVGTELgeTDYD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 311 TASKWIFQHPEvRFLNINVsnfDAWKLDG-----IAMLADAREAMTALDAALADSGWQAGWGAqiesvqSRqlkeTQRVY 385
Cdd:PRK07524 281 VYFDGGFPLPG-ELIRIDI---DPDQLARnyppaLALVGDARAALEALLARLPGQAAAADWGA------AR----VAALR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 386 QAVWQEksfvpeiddhldresvyrefrqITDSTLTQSSVLGVLNETLPaEAVIV------AAAGSLPGDL--QRVWRNRA 457
Cdd:PRK07524 347 QALRAE----------------------WDPLTAAQVALLDTILAALP-DAIFVgdstqpVYAGNLYFDAdaPRRWFNAS 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 458 EntyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGM 537
Cdd:PRK07524 404 T-------GYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDI 476
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1757862790 538 DSFGTEFRyrqpetgqlqgglvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK07524 477 EPVGVDPY--------------TPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQ 528
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
6-610 |
1.91e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 173.40 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 6 LTTAQALVKfldnqYLEVDGVELkfvkgifaIFGH--GNVLGLGQALeQDSgDMRVYQGRNEQGMAHAATGFARQALRRQ 83
Cdd:PRK06276 1 MKGAEAIIK-----ALEAEGVKI--------IFGYpgGALLPFYDAL-YDS-DLIHILTRHEQAAAHAADGYARASGKVG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 84 IiaCTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQsydLSIstndaFRAVSKYWDRITRPEQLM 163
Cdd:PRK06276 66 V--CVATSGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDA---LGI-----FMPITKHNFQIKKPEEIP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 164 SACINAMRVltdpAETG---AVTLCLPQDVQGEAWDYPESFFARRVHRLDRRPASA---AQLADAVAAIKASRKPLIVCG 237
Cdd:PRK06276 136 EIFRAAFEI----AKTGrpgPVHIDLPKDVQEGELDLEKYPIPAKIDLPGYKPTTFghpLQIKKAAELIAEAERPVILAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 238 GGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIF 317
Cdd:PRK06276 212 GGVIISGASEELIELSELVKIPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 318 QhPEVRFLNINVSNFDAWK---LDgIAMLADAREAMTALDAALA------DSGWqagwgaqIESVQSRQlketqrvyqav 388
Cdd:PRK06276 292 A-PNAKIIHIDIDPAEIGKnvrVD-VPIVGDAKNVLRDLLAELMkkeiknKSEW-------LERVKKLK----------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 389 wqeKSFVPEI---DDHLDRESVYREFRQitdstltqssvlgVLNETLP-AEAVIVAAAGSLPGDLQRVWRNRAENTYHVE 464
Cdd:PRK06276 352 ---KESIPRMdfdDKPIKPQRVIKELME-------------VLREIDPsKNTIITTDVGQNQMWMAHFFKTSAPRSFISS 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 465 YGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHgmdsfgteF 544
Cdd:PRK06276 416 GGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVYQWQNLY--------Y 487
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1757862790 545 RYRQPETgqlQGGLVPvDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLPKTMVH 610
Cdd:PRK06276 488 GKRQSEV---HLGETP-DFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEALP 549
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
3-609 |
2.96e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 166.81 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 3 KLRLTTAQALVKFLDNQylevdGVelKFVKGIFAifghGNVLGLGQALEQdSGDMRVYQGRNEQGMAHAATGFARQALRR 82
Cdd:PRK08155 10 RKRFTGAELIVRLLERQ-----GI--RIVTGIPG----GAILPLYDALSQ-STQIRHILARHEQGAGFIAQGMARTTGKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 83 QIiaCTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEqSYDLSIStndafraVSKYWDRITRPEQL 162
Cdd:PRK08155 78 AV--CMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVD-TYGISIP-------ITKHNYLVRDIEEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 163 MSACINAMRVLTDpAETGAVTLCLPQDVQGEAWD---YPESFfarrvhRLDRRPA-SAAQLADAVAAIKASRKPLIVCGG 238
Cdd:PRK08155 148 PQVISDAFRIAQS-GRPGPVWIDIPKDVQTAVIEleaLPAPA------EKDAAPAfDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 239 GVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQ 318
Cdd:PRK08155 221 GVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 319 hPEVRFLNINVsnfDAWKLDGI-----AMLADAREAMTALDAALADSGwQAGWGAQIESVQsrqlketqrvyqavwQEKS 393
Cdd:PRK08155 301 -PNAKIIHVDI---DRAELGKIkqphvAIQADVDDVLAQLLPLVEAQP-RAEWHQLVADLQ---------------REFP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 394 F-VPEIDDHLdresvyrefrqitdstltqsSVLGVLNET---LPAEAVIVAAAG--------SLPGDLQRVWRNRAenty 461
Cdd:PRK08155 361 CpIPKADDPL--------------------SHYGLINAVaacVDDNAIITTDVGqhqmwtaqAYPLNRPRQWLTSG---- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 462 hveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-MEHGMDSF 540
Cdd:PRK08155 417 ----GLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQsLFYGQRVF 492
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 541 GTEFRYRqpetgqlqgglvpVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDI------KVLPktMV 609
Cdd:PRK08155 493 AATYPGK-------------INFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVridaeeKVYP--MV 552
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
5-603 |
4.31e-44 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 165.95 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKFLDNQylEVDGVelkfvkgiFAIFGhGNVLGLGQALEQDSGDMRVYQGRNEQGMAHAATGFARQALRrqI 84
Cdd:PRK08266 3 TMTGGEAIVAGLVAH--GVDTV--------FGLPG-AQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGR--P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 IACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFAtrqpdpvlQQIEQSYDLSISTND---AFRAVSKYWDRITRPEQ 161
Cdd:PRK08266 70 GVCSVVPGPGVLNAGAALLTAYGCNSPVLCLTGQIPS--------ALIGKGRGHLHEMPDqlaTLRSFTKWAERIEHPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 162 ---LMSACINAMRvltdPAETGAVTLCLPQDVQGEAWDYPESFFARRVHRLDRRPasaAQLADAVAAIKASRKPLIVCGG 238
Cdd:PRK08266 142 apaLVAEAFQQML----SGRPRPVALEMPWDVFGQRAPVAAAPPLRPAPPPAPDP---DAIAAAAALIAAAKNPMIFVGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 239 GVkySGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLnvggvGETgCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQ 318
Cdd:PRK08266 215 GA--AGAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPL-----GLN-FAAAYELWPQTDVVIGIGSRLELPTFRWPWRPD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 319 HPEVRFLNINVSNFDAWKLDgIAMLADAREAMTALDAALADSGwqagwgaqiesvqsrqlketqrvyqavwqeksfvpei 398
Cdd:PRK08266 287 GLKVIRIDIDPTEMRRLKPD-VAIVADAKAGTAALLDALSKAG------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 399 DDHLDRESVYREFRQITDSTLT----QSSVLGVLNETLPAEAVIV--------AAAGSLPgdlqrVWRNRaenTYhVEYG 466
Cdd:PRK08266 329 SKRPSRRAELRELKAAARQRIQavqpQASYLRAIREALPDDGIFVdelsqvgfASWFAFP-----VYAPR---TF-VTCG 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 467 YS-CMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEhgmdSFGTefR 545
Cdd:PRK08266 400 YQgTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKR----RFGG--R 473
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1757862790 546 YrqpetgqLQGGLVPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK08266 474 V-------VASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
6-603 |
4.75e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 165.77 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 6 LTTAQALVKFLDNQylevdGVELkfvkgIFAIFGHGNvLGLGQALeQDSgDMRVYQGRNEQGMAHAATGFARqaLRRQII 85
Cdd:PRK08322 1 MKAADLFVKCLENE-----GVEY-----IFGIPGEEN-LDLLEAL-RDS-SIKLILTRHEQGAAFMAATYGR--LTGKAG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 86 ACTSSIGPGAANMITAAGTASANRIPLLLLPGDVfatrqpdPVL---QQIEQSYDLSistnDAFRAVSKYWDRITRPEQL 162
Cdd:PRK08322 66 VCLSTLGPGATNLVTGVAYAQLGGMPMVAITGQK-------PIKrskQGSFQIVDVV----AMMAPLTKWTRQIVSPDNI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 163 MSACINAMRVltdpAET---GAVTLCLPQDVQGEawDYPESFFARRVHRldrRP-ASAAQLADAVAAIKASRKPLIVCGG 238
Cdd:PRK08322 135 PEVVREAFRL----AEEerpGAVHLELPEDIAAE--ETDGKPLPRSYSR---RPyASPKAIERAAEAIQAAKNPLILIGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 239 GVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGetgcLAA----NLLAKEADLVIGVG---TRFSDFtt 311
Cdd:PRK08322 206 GANRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPLSLGTAG----LSQgdyvHCAIEHADLIINVGhdvIEKPPF-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 312 asKWifqHPEVRFLNINVsNFDAWKLDG-----IAMLADAREAMTALDAALAD-SGWQAGWGAQIesvqsRQLKETQRVY 385
Cdd:PRK08322 280 --FM---NPNGDKKVIHI-NFLPAEVDPvyfpqVEVVGDIANSLWQLKERLADqPHWDFPRFLKI-----REAIEAHLEE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 386 QAvwQEKSF--VPEiddhldresvyrefRQITDstltqssvlgvLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHV 463
Cdd:PRK08322 349 GA--DDDRFpmKPQ--------------RIVAD-----------LRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 464 EYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTE 543
Cdd:PRK08322 402 DNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLD 481
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 544 FryRQPetgqlqgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK08322 482 F--GNP------------DFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
53-605 |
2.41e-43 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 163.89 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 53 DSGDMRVYQGRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANmiTAAG--TASANRIPLLLLPGDV---FATRQpdp 127
Cdd:PRK08199 43 DETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTR--GPGATN--ASIGvhTAFQDSTPMILFVGQVardFRERE--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 128 VLQQIEqsYDlsistnDAFRAVSKYWDRITRPEQLMSACINAMRVLTD--PaetGAVTLCLPQDVqgeAWDYPESFFARR 205
Cdd:PRK08199 116 AFQEID--YR------RMFGPMAKWVAEIDDAARIPELVSRAFHVATSgrP---GPVVLALPEDV---LSETAEVPDAPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 206 VHRLDRRPASAAQLADAVAaIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGetg 285
Cdd:PRK08199 182 YRRVAAAPGAADLARLAEL-LARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDLG--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 286 cLAAN--LLA--KEADLVIGVGTRFSDFTTASKWIFQ--HPEVRFLNINVsnfDAWKLdG------IAMLADAREAMTAL 353
Cdd:PRK08199 258 -LGINpaLAAriREADLVLAVGTRLGEVTTQGYTLLDipVPRQTLVHVHP---DAEEL-GrvyrpdLAIVADPAAFAAAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 354 DA--ALADSGWqAGWGAqiesvqsrqlkETQRVYQAvWQEKSFVPeiddhldresvyrefrqitdSTLTQSSVLGVLNET 431
Cdd:PRK08199 333 AAlePPASPAW-AEWTA-----------AAHADYLA-WSAPLPGP--------------------GAVQLGEVMAWLRER 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 432 LPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYScMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQE 511
Cdd:PRK08199 380 LPADAIITNGAGNYATWLHRFFRFRRYRTQLAPTSGS-MGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 512 RAKINVVLFDNmangcinnlqmehGMdsFGT-----EFRY--RQPETgqlqgGLVPVDFATIAAGYGCKTWRVTTLDELR 584
Cdd:PRK08199 459 GLPIIVIVVNN-------------GM--YGTirmhqEREYpgRVSGT-----DLTNPDFAALARAYGGHGETVERTEDFA 518
|
570 580
....*....|....*....|.
gi 1757862790 585 HALDAARRETVSTLIDIKVLP 605
Cdd:PRK08199 519 PAFERALASGKPALIEIRIDP 539
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
63-605 |
3.64e-43 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 163.78 E-value: 3.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfATRQPDP-VLQQIEQSydlsis 141
Cdd:PRK06112 56 RTENAGGAMADGYARVSGKVAVVTAQN--GPAATLLVAPLAEALKASVPIVALVQDV-NRDQTDRnAFQELDHI------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 142 tnDAFRAVSKYWDRITRPEQLMSACINAMRVLTDpAETGAVTLCLPQDVQGEAWDYPESFFARRVHR--LDRRPASAAQL 219
Cdd:PRK06112 127 --ALFQSCTKWVRRVTVAERIDDYVDQAFTAATS-GRPGPVVLLLPADLLTAAAAAPAAPRSNSLGHfpLDRTVPAPQRL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 220 ADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGEtgCLAANLLAK----- 294
Cdd:PRK06112 204 AEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGS--LMGPRSPGRhlrdl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 295 --EADLVIGVGTRFSDFTTASkWIFQHPEVRFLNINVS------NFDAWKLDGiamlaDAREAMTALDAAL------ADS 360
Cdd:PRK06112 282 vrEADVVLLVGTRTNQNGTDS-WSLYPEQAQYIHIDVDgeevgrNYEALRLVG-----DARLTLAALTDALrgrdlaARA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 361 GWQAGWGAQIESVQSRQLKETQRVYQAvwqekSFVP--------EIDDHLDRESVYrefrqITDSTLTQSSVLGVLNETl 432
Cdd:PRK06112 356 GRRAALEPAIAAGREAHREDSAPVALS-----DASPirperimaELQAVLTGDTIV-----VADASYSSIWVANFLTAR- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 433 paeavivaAAGslpgdlQRVWRNRaentyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQER 512
Cdd:PRK06112 425 --------RAG------MRFLTPR---------GLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 513 AKINVVLFDNMangcINNLQMEHGMDSFGTefryrqpETGQLQGGlvPVDFATIAAGYGCKTWRVTTLDELRHALDAARR 592
Cdd:PRK06112 482 VPVTIVVLNNG----ILGFQKHAETVKFGT-------HTDACHFA--AVDHAAIARACGCDGVRVEDPAELAQALAAAMA 548
|
570
....*....|...
gi 1757862790 593 ETVSTLIDIKVLP 605
Cdd:PRK06112 549 APGPTLIEVITDP 561
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
5-609 |
9.70e-43 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 163.23 E-value: 9.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKfldnqYLEVDGVELkfvkgIFAIFGhGNVLGLGQALeQDSGDMRVYQGRNEQGMAHAATGFArQALRRqI 84
Cdd:PRK07789 30 RMTGAQAVVR-----SLEELGVDV-----VFGIPG-GAILPVYDPL-FDSTKVRHVLVRHEQGAGHAAEGYA-QATGR-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 IACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATrqpdpvlqqieqsydlSISTnDAFR---------AVSKYWDR 155
Cdd:PRK07789 96 GVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRG----------------LIGT-DAFQeadivgitmPITKHNFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 156 ITRPEQLMSACINAMRVltdpAETG---AVTLCLPQDVQGEAWDY----------------PESFFARRVHRLdrrpasa 216
Cdd:PRK07789 159 VTDADDIPRVIAEAFHI----ASTGrpgPVLVDIPKDALQAQTTFswpprmdlpgyrpvtkPHGKQIREAAKL------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 217 aqladavaaIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEA 296
Cdd:PRK07789 228 ---------IAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 297 DLVIGVGTRFSDFTTASKWIFQhPEVRFLNINV------SNFDAwkldGIAMLADAREAMTALDAALADSGWQAG----- 365
Cdd:PRK07789 299 DLLIALGARFDDRVTGKLDSFA-PDAKVIHADIdpaeigKNRHA----DVPIVGDVKEVIAELIAALRAEHAAGGkpdlt 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 366 -WGAQIESVQSRqlketqrvYQAVWQEKSfvpeiddhldresvyrefrqitDSTLTQSSVLGVLNETLPAEAVIVA---- 440
Cdd:PRK07789 374 aWWAYLDGWRET--------YPLGYDEPS----------------------DGSLAPQYVIERLGEIAGPDAIYVAgvgq 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 441 ----AAGSLPGDLQRVWRNRAentyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKIN 516
Cdd:PRK07789 424 hqmwAAQFIDYEKPRTWLNSG--------GLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIK 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 517 VVLFDNMANGCINNLQmehgmdsfgTEF---RYRQPETGQlQGGLVPvDFATIAAGYGCKTWRVTTLDELRHALDAAR-- 591
Cdd:PRK07789 496 VALINNGNLGMVRQWQ---------TLFyeeRYSNTDLHT-HSHRIP-DFVKLAEAYGCVGLRCEREEDVDAVIEKARai 564
|
650 660
....*....|....*....|
gi 1757862790 592 --RETVstlIDIKVLPKTMV 609
Cdd:PRK07789 565 ndRPVV---IDFVVGKDAMV 581
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
63-617 |
1.67e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 161.81 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfatrqpdpvlqqieqsyDLSIST 142
Cdd:PRK08527 48 RHEQAAVHAADGYARASGKVGVAIVTS--GPGFTNAVTGLATAYMDSIPLVLISGQV-----------------PNSLIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 143 NDAFR---AVSkywdrITRP---EQLMSACINAM-RVLTDP---AET---GAVTLCLPQDVQGEA--WDYPES------- 200
Cdd:PRK08527 109 TDAFQeidAVG-----ISRPcvkHNYLVKSIEELpRILKEAfyiARSgrpGPVHIDIPKDVTATLgeFEYPKEislktyk 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 201 ----FFARRVHRLdrrpasaaqladaVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPL 276
Cdd:PRK08527 184 ptykGNSRQIKKA-------------AEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMARGVLRSDDPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 277 NVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIF-QHPEVRFLNINVSNfdawkldgIAMLADAREAMTA-LD 354
Cdd:PRK08527 251 LLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFaKHAKIIHVDIDPSS--------ISKIVNADYPIVGdLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 355 AALADsgwqagwgaQIESVQSRQLKETQRvyqavWQEksfvpeiddHLDResvYREFRQIT----DSTLTQSSVLGVLNE 430
Cdd:PRK08527 323 NVLKE---------MLEELKEENPTTYKE-----WRE---------ILKR---YNELHPLSyedsDEVLKPQWVIERVGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 431 TLPAEAVIVA--------AAGSLPGDLQRVWRNRAentyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLH 502
Cdd:PRK08527 377 LLGDDAIISTdvgqhqmwVAQFYPFNYPRQLATSG--------GLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 503 SELVTSLQERAK-INVVLFDNMangcinnLQMEHGMDSFGTEFRYRQPETgQLQgglvPvDFATIAAGYGCKTWRVTTLD 581
Cdd:PRK08527 449 QELMTAVEYKIPvINIILNNNF-------LGMVRQWQTFFYEERYSETDL-STQ----P-DFVKLAESFGGIGFRVTTKE 515
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1757862790 582 ELRHALDAARRETVSTLIDIK------VLPktMVHKYGSWWN 617
Cdd:PRK08527 516 EFDKALKEALESDKVALIDVKidrfenVLP--MVPAGGALYN 555
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
441-601 |
5.26e-42 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 148.89 E-value: 5.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 441 AAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLF 520
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 521 DNMANGCINNLQMEHGMDSFGTEFRYRQPetgqlqgglvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLID 600
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILP----------PVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALID 150
|
.
gi 1757862790 601 I 601
Cdd:pfam02775 151 V 151
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
33-582 |
1.79e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 158.83 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 33 GIFAIFGH--GNVLGLGQALEQDSGdMRVYQGRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRI 110
Cdd:PRK07282 24 GVDTIFGYpgGAVLPLYDAIYNFEG-IRHILARHEQGALHEAEGYAKSTGKLGVAVVTS--GPGATNAITGIADAMSDSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 111 PLLLLPGDVfATRqpdpvlqqieqsydlSIStNDAFR---------AVSKYWDRITRPEQLMSACINAMRVLTDpAETGA 181
Cdd:PRK07282 101 PLLVFTGQV-ARA---------------GIG-KDAFQeadivgitmPITKYNYQIRETADIPRIITEAVHIATT-GRPGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 182 VTLCLPQDVQGEAWDYpesFFARRVHRLDRRP---ASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGV 258
Cdd:PRK07282 163 VVIDLPKDVSALETDF---IYDPEVNLPSYQPtlePNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 259 PFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIF-QHPEVRFLNINVSNFDAWKL 337
Cdd:PRK07282 240 PVVTTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFaKNAKVAHIDIDPAEIGKIIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 338 DGIAMLADAREAMTALdaaladsgwqagwgAQIESVQSRQLKETQRVYqavwQEKSFVPEIDdhlDRESVYREfrqitds 417
Cdd:PRK07282 320 TDIPVVGDAKKALQML--------------LAEPTVHNNTEKWIEKVT----KDKNRVRSYD---KKERVVQP------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 418 tltqSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGS 497
Cdd:PRK07282 372 ----QAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 498 FMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehgmDSFGTEfryrqpETGQLQGGLVPvDFATIAAGYGCKTWRV 577
Cdd:PRK07282 448 FQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQ-----ESFYEG------RTSESVFDTLP-DFQLMAQAYGIKHYKF 515
|
....*...
gi 1757862790 578 T---TLDE 582
Cdd:PRK07282 516 DnpeTLAQ 523
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
19-587 |
4.13e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 157.82 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 19 QYLEVDGVE--LKFVK--GIFAIFGH--GNVLGLGQALeQDSGdMRVYQGRNEQGMAHAATGFARQALRRQIIACTSsiG 92
Cdd:PRK06725 11 QCEEVTGAGhvIQCLKklGVTTVFGYpgGAILPVYDAL-YESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATS--G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 93 PGAANMITAAGTASANRIPLLLLPGDVfAT--------RQPD------PVLQ---QIEQSYDLSISTNDAFravskYWDR 155
Cdd:PRK06725 87 PGATNLVTGLADAYMDSIPLVVITGQV-ATpligkdgfQEADvvgitvPVTKhnyQVRDVNQLSRIVQEAF-----YIAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 156 ITRPeqlmsacinamrvltdpaetGAVTLCLPQDVQGE--AWDYPESFFARRvHRLDRRPASAAQLADAVAaIKASRKPL 233
Cdd:PRK06725 161 SGRP--------------------GPVLIDIPKDVQNEkvTSFYNEVVEIPG-YKPEPRPDSMKLREVAKA-ISKAKRPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 234 IVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTAS 313
Cdd:PRK06725 219 LYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 314 KWIFQ-HPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALdaaLADSGWqagwgaqiesVQSRQLKETQRVYQAVWQek 392
Cdd:PRK06725 299 LELFSpHSKKVHIDIDPSEFHKNVAVEYPVVGDVKKALHML---LHMSIH----------TQTDEWLQKVKTWKEEYP-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 393 sfvpeiddhldresvyREFRQiTDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGY 472
Cdd:PRK06725 364 ----------------LSYKQ-KESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 473 EVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehgmdSFGTEFRYRQPETG 552
Cdd:PRK06725 427 GFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQ------EMFYENRLSESKIG 500
|
570 580 590
....*....|....*....|....*....|....*
gi 1757862790 553 QlqgglvPvDFATIAAGYGCKTWRVTTLDELRHAL 587
Cdd:PRK06725 501 S------P-DFVKVAEAYGVKGLRATNSTEAKQVM 528
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
5-593 |
8.61e-40 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 154.37 E-value: 8.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKFLdnqylEVDGVELKF-VKGIfAIfghgnvLGLGQALEQdSGDMRVYQGRNEQGMAHAATGFARqALRRQ 83
Cdd:PRK11269 3 KMRAVDAAVLVL-----EKEGVTTAFgVPGA-AI------NPFYSAMRK-HGGIRHILARHVEGASHMAEGYTR-ATAGN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 84 IIACTSSIGPGAANMITAAGTASANRIPLLLLPGdvfatRQPDPVLQQIE-QSYDL-SIStndafRAVSKYWDRITRPEQ 161
Cdd:PRK11269 69 IGVCIGTSGPAGTDMITGLYSASADSIPILCITG-----QAPRARLHKEDfQAVDIeSIA-----KPVTKWAVTVREPAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 162 LMSACINAMRVLTDpAETGAVTLCLPQDVQGEAWDY-PESFFARRVHRldrrP-ASAAQLADAVAAIKASRKPLIVCGGG 239
Cdd:PRK11269 139 VPRVFQQAFHLMRS-GRPGPVLIDLPFDVQVAEIEFdPDTYEPLPVYK----PaATRAQIEKALEMLNAAERPLIVAGGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 240 VKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVG-ETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQ 318
Cdd:PRK11269 214 VINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLMAGMVGlQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 319 HpEVRFLNINVSNFDAWKL---D-GIAmlADAREAMTALDAALADsgWQAG-----WGAQIESVQSRqlKET-QRvyqav 388
Cdd:PRK11269 294 K-GRKFVHVDIEPTQIGRVfgpDlGIV--SDAKAALELLVEVARE--WKAAgrlpdRSAWVADCQER--KRTlLR----- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 389 wqeksfvpeiDDHLDR-----ESVYREfrqitdstltqssvlgvLNETLPAEAVIVAAAGslpgdLQRVWRNRAENTYHV 463
Cdd:PRK11269 362 ----------KTHFDNvpikpQRVYEE-----------------MNKAFGRDTCYVSTIG-----LSQIAAAQFLHVYKP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 464 EYGYSC-----MGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMD 538
Cdd:PRK11269 410 RHWINCgqagpLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRAFDMD 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1757862790 539 sFGTEFRYRQPETGQLQG-GlvpVDFATIAAGYGCKTWRVTTLDELRHALDAARRE 593
Cdd:PRK11269 490 -YCVQLAFENINSPELNGyG---VDHVKVAEGLGCKAIRVFKPEDIAPALEQAKAL 541
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
32-590 |
1.08e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 150.74 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 32 KGIFAIFGH--GNVLGLGQALEQDSGDMRVYQgRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANR 109
Cdd:PRK08979 17 EGVKHIFGYpgGSVLDIYDALHEKSGIEHILV-RHEQAAVHMADGYARATGKVGVVLVTS--GPGATNTITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 110 IPLLLLPGDVfatrqPDpvlqqieqsydlSISTNDAF---------RAVSKYWDRITRPEQLMSACINAMRVLTDpAETG 180
Cdd:PRK08979 94 IPMVVLSGQV-----PS------------NLIGNDAFqecdmigisRPVVKHSFLVKDAEDIPEIIKKAFYIAST-GRPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 181 AVTLCLPQDVQGEA----WDYPESFFARRVHrldrrPASAAQLADAVAAIKA---SRKPLIVCGGGVKYSGAGEALSRFA 253
Cdd:PRK08979 156 PVVIDLPKDCLNPAilhpYEYPESIKMRSYN-----PTTSGHKGQIKRGLQAllaAKKPVLYVGGGAIISGADKQILQLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 254 ERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTT--ASKWIfqhPEVRFLNINV-- 329
Cdd:PRK08979 231 EKLNLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnLEKYC---PNATILHIDIdp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 330 -SNFDAWKLDgIAMLADAREAMTALDAALADSGWQ------AGWGAQIESVQSRqlketqrvyQAVWQEKSfvpeiDDHL 402
Cdd:PRK08979 308 sSISKTVRVD-IPIVGSADKVLDSMLALLDESGETndeaaiASWWNEIEVWRSR---------NCLAYDKS-----SERI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 403 DRESVYREFRQITDSTLTQSSVLGVLNetlpaeaviVAAAGSLPGDLQRVWRNRAentyhveyGYSCMGYEVNAALGVKL 482
Cdd:PRK08979 373 KPQQVIETLYKLTNGDAYVASDVGQHQ---------MFAALYYPFDKPRRWINSG--------GLGTMGFGLPAAMGVKF 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 483 AQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-----MEHG---MDSfgtefryrqpetgql 554
Cdd:PRK08979 436 AMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQWQdmiyqGRHShsyMDS--------------- 500
|
570 580 590
....*....|....*....|....*....|....*.
gi 1757862790 555 qgglVPvDFATIAAGYGCKTWRVTTLDELRHALDAA 590
Cdd:PRK08979 501 ----VP-DFAKIAEAYGHVGIRISDPDELESGLEKA 531
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
226-353 |
1.28e-38 |
|
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: 139.24 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 226 IKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTR 305
Cdd:pfam00205 8 LKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADLVLAVGAR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1757862790 306 FSDFTTASKWIFQHPEVRFLNINVsnfDAWKLD-----GIAMLADAREAMTAL 353
Cdd:pfam00205 88 FDDIRTTGKLPEFAPDAKIIHIDI---DPAEIGknypvDVPIVGDAKETLEAL 137
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
63-589 |
1.28e-38 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 150.03 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfatrqPDPVlqqieqsydlsIST 142
Cdd:PRK08978 45 RHEQGAAMAAIGYARATGKVGVCIATS--GPGATNLITGLADALLDSVPVVAITGQV-----SSPL-----------IGT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 143 nDAFR---------AVSKYWDRITRPEQLMSACINAMRVltdpAET---GAVTLCLPQDVQGEAWDYPESFFARrvhrLD 210
Cdd:PRK08978 107 -DAFQeidvlglslACTKHSFLVQSLEELPEIMAEAFEI----ASSgrpGPVLVDIPKDIQLAEGELEPHLTTV----EN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 211 RRPASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAAN 290
Cdd:PRK08978 178 EPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAAN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 291 LLAKEADLVIGVGTRFSDFTTASKWIF-QHPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAgwgaq 369
Cdd:PRK08978 258 LAVQECDLLIAVGARFDDRVTGKLNTFaPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPALQQPLNIDAWRQ----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 370 iesvQSRQLKETQRV-YqavwqeksfvpeidDHLDrESVYrefrqitdstltQSSVLGVLNETLPAEAVIV--------- 439
Cdd:PRK08978 333 ----HCAQLRAEHAWrY--------------DHPG-EAIY------------APALLKQLSDRKPADTVVTtdvgqhqmw 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 440 AAagslpgdlQRVWRNRAENtYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVL 519
Cdd:PRK08978 382 VA--------QHMRFTRPEN-FITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 520 FDNMANGCINNLQmehgmDSFgteFRYRQPETgQLQGGlvPvDFATIAAGYGCKTWRVTTLDELRHALDA 589
Cdd:PRK08978 453 LDNQRLGMVRQWQ-----QLF---FDERYSET-DLSDN--P-DFVMLASAFGIPGQTITRKDQVEAALDT 510
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
33-603 |
6.63e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 149.04 E-value: 6.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 33 GIFAIFGH--GNVLGLGQAL---EQDsGDMRVYQGRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASA 107
Cdd:PRK07418 33 GVKHIFGYpgGAILPIYDELykaEAE-GWLKHILVRHEQGAAHAADGYARATGKVGVCFGTS--GPGATNLVTGIATAQM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 108 NRIPLLLLPGDVfatrqPDPvlqqieqsydlSISTnDAFRAVSKYwdRITRPeqlmsaCINAMRVLTDPAET-------- 179
Cdd:PRK07418 110 DSVPMVVITGQV-----PRP-----------AIGT-DAFQETDIF--GITLP------IVKHSYVVRDPSDMarivaeaf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 180 --------GAVTLCLPQDVQGEAWDY---------PESFfaRRVHRLDRRPASAAQLAdavaaIKASRKPLIVCGGGVKY 242
Cdd:PRK07418 165 hiassgrpGPVLIDIPKDVGQEEFDYvpvepgsvkPPGY--RPTVKGNPRQINAALKL-----IEEAERPLLYVGGGAIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 243 SGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQhPEV 322
Cdd:PRK07418 238 AGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFA-SRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 323 RFLNINVSNFDAWK--LDGIAMLADAREAMTALDAAL---ADSGWQAGWGAQIESvqsrqlketqrvyqavWQEKS--FV 395
Cdd:PRK07418 317 KVIHIDIDPAEVGKnrRPDVPIVGDVRKVLVKLLERSlepTTPPRTQAWLERINR----------------WKQDYplVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 396 PEIDDHLDRESVYREFRQitdstltqssvlgvlnetLPAEAVIVA--------AAGSL---PgdlqRVWRNRAentyhve 464
Cdd:PRK07418 381 PPYEGEIYPQEVLLAVRD------------------LAPDAYYTTdvgqhqmwAAQFLrngP----RRWISSA------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 465 yGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehgmDSFGTEf 544
Cdd:PRK07418 432 -GLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQWQ-----ESFYGE- 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1757862790 545 RYRQpeTGQLQGglVPvDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK07418 505 RYSA--SNMEPG--MP-DFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHV 558
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
56-594 |
2.10e-37 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 146.88 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 56 DMRVYQGRNEQGMAHAATGFARQALRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVfatrqPDPvLQQIEQS 135
Cdd:PRK06154 54 GIRPVIARTERVAVHMADGYARATSGERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVAPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 136 YdlsiSTNDAFRAVSKYWDRITRPEQLMsaciNAMRVLTDPAETGA---VTLCLPQDVQGEawDYPESFFARRVHRLDRR 212
Cdd:PRK06154 128 F----ESLRNYRHITKWCEQVTLPDEVP----ELMRRAFTRLRNGRpgpVVLELPVDVLAE--ELDELPLDHRPSRRSRP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 213 PASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVG--GVGETGCLAAN 290
Cdd:PRK06154 198 GADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGsgGRARPATVAHF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 291 LlaKEADLVIGVGTRFsdftTASKWIFQHPEVRflNINVSNFDAWKLD-----GIAMLADAREAMTALDAALA-----DS 360
Cdd:PRK06154 278 L--READVLFGIGCSL----TRSYYGLPMPEGK--TIIHSTLDDADLNkdypiDHGLVGDAALVLKQMIEELRrrvgpDR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 361 GWQAGWGAQIESVQSRQLKEtqrvyqavWQEKsfvpeiddhLDRESVyrefrqitdsTLTQSSVLGVLNETL-PAEAVIV 439
Cdd:PRK06154 350 GRAQQVAAEIEAVRAAWLAK--------WMPK---------LTSDST----------PINPYRVVWELQHAVdIKTVIIT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 440 AAAGSLPGDLQRVWRNRAENTYhVEYGYSC-MGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVV 518
Cdd:PRK06154 403 HDAGSPRDQLSPFYVASRPGSY-LGWGKTTqLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTI 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1757862790 519 LFDNmangciNNLQMEHGMDSFGTEFRYRQPETGqlqgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAARRET 594
Cdd:PRK06154 482 LLNN------FSMGGYDKVMPVSTTKYRATDISG---------DYAAIARALGGYGERVEDPEMLVPALLRALRKV 542
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
63-605 |
3.22e-36 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 143.69 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATGFARQAlrRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGdvfatrqpdpvlqQIEQSYdlsIST 142
Cdd:CHL00099 58 RHEQGAAHAADGYARST--GKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITG-------------QVGRAF---IGT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 143 nDAFRAVSKYwdRITRP----------EQLMSACINAMRVLTDPAETGAVTLCLPQDVQGEAWDYPESFFARRVHRL-DR 211
Cdd:CHL00099 120 -DAFQEVDIF--GITLPivkhsyvvrdARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEKFDYYPPEPGNTIIKIlGC 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 212 RPASAAQL---ADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLA 288
Cdd:CHL00099 197 RPIYKPTIkriEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 289 ANLLAKEADLVIGVGTRFSDFTTASKWIFQ-HPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSgwqagwG 367
Cdd:CHL00099 277 ANFAVSECDLLIALGARFDDRVTGKLDEFAcNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVLQELLELLKNS------P 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 368 AQIESVQSRQLKEtqRVyqAVWQEKS--FVPEIDDHLDRESVYREFRQITDSTLTQSSVlGvLNETLPAEAVIVaaagsl 445
Cdd:CHL00099 351 NLLESEQTQAWRE--RI--NRWRKEYplLIPKPSTSLSPQEVINEISQLAPDAYFTTDV-G-QHQMWAAQFLKC------ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 446 pgdLQRVWRNRAentyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMAN 525
Cdd:CHL00099 419 ---KPRKWLSSA--------GLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQ 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 526 GCINNLQmehgmDSFGTEfRYRQP--ETGQlqgglvPvDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:CHL00099 488 GMVRQWQ-----QAFYGE-RYSHSnmEEGA------P-DFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQV 554
|
..
gi 1757862790 604 LP 605
Cdd:CHL00099 555 IE 556
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
5-590 |
7.62e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 142.36 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 5 RLTTAQALVKFLDNQylevdGVELkfvkgifaIFGH--GNVLGLGQALEQDSGDMRVYQgRNEQGMAHAATGFARQALRR 82
Cdd:PRK06882 3 KLSGAEMVVQSLRDE-----GVEY--------VFGYpgGSVLDIYDAIHTLGGIEHVLV-RHEQAAVHMADGYARSTGKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 83 QIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQsydLSIStndafRAVSKYWDRITRPEQL 162
Cdd:PRK06882 69 GCVLVTS--GPGATNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDM---LGIS-----RPVVKHSFIVKNAEDI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 163 MSACINAMRVLTDpAETGAVTLCLPQDVQGEA----WDYPESFFARRVHrldrrPASAAQLADAVAAIKA---SRKPLIV 235
Cdd:PRK06882 139 PSTIKKAFYIAST-GRPGPVVIDIPKDMVNPAnkftYEYPEEVSLRSYN-----PTVQGHKGQIKKALKAllvAKKPVLF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 236 CGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTT--AS 313
Cdd:PRK06882 213 VGGGVITAECSEQLTQFAQKLNLPVTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTnnLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 314 KWIfQHPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGwqagwgaqiesvqsrqLKETQRVYQAVWQeks 393
Cdd:PRK06882 293 KYC-PNAKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEN----------------LAKSQTDLTAWWQ--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 394 fvpEIDDHLDRESVyrEFRQiTDSTLTQSSVLGVLNETLPAEAVIVA--------AAGSLPGDLQRVWRNRAentyhvey 465
Cdd:PRK06882 353 ---QINEWKAKKCL--EFDR-TSDVIKPQQVVEAIYRLTNGDAYVASdvgqhqmfAALHYPFDKPRRWINSG-------- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 466 GYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehgmdSFGTEFR 545
Cdd:PRK06882 419 GAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQWQ------DLIYSGR 492
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1757862790 546 YRQPETGQLQgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAA 590
Cdd:PRK06882 493 HSQVYMNSLP------DFAKLAEAYGHVGIQIDTPDELEEKLTQA 531
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
49-605 |
6.45e-35 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 139.75 E-value: 6.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 49 ALEQDSGDMRVYQGRNEQGMAHAATGFARqaLRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATrqpdpv 128
Cdd:PRK08611 36 ALRKEQDKIKFIQVRHEEVAALAAAAYAK--LTGKIGVCLSIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSD------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 129 lqQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMSACINAMRvlTDPAETGAVTLCLPQDV--QGEAWDY--PESFFAR 204
Cdd:PRK08611 108 --LLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIR--TAYEKKGVAVLTIPDDLpaQKIKDTTnkTVDTFRP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 205 RVHRLDRRpasaaQLADAVAAIKASRKPLIVCGGGVKysGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGET 284
Cdd:PRK08611 184 TVPSPKPK-----DIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNLGKI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 285 GCLAANLLAKEADLVIGVGTRF--SDF---TTASKWIFQHPEV---RFlNINVsnfdawkldGIAmlADAREAMTALDAA 356
Cdd:PRK08611 257 GTKPAYEAMQEADLLIMVGTNYpyVDYlpkKAKAIQIDTDPANigkRY-PVNV---------GLV--GDAKKALHQLTEN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 357 ladsgwqagwgaqIESVQSRQ-LKETQRvYQAVWqeksfvpeiDDHLDREsvyrefRQITDSTLTQSSVLGVLNETLPAE 435
Cdd:PRK08611 325 -------------IKHVEDRRfLEACQE-NMAKW---------WKWMEED------ENNASTPIKPERVMAAIQKIADDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 436 AVIVAAAGSLPgdlqrVWRNR-----AENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQ 510
Cdd:PRK08611 376 AVLSVDVGTVT-----VWSARylnlgTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 511 ERAKINVVLFDNmangciNNLQMehgmdsfgteFRYRQPETGQLQGG--LVPVDFATIAAGYGCKTWRVTTLDELRHALD 588
Cdd:PRK08611 451 YKLPIVVVVLNN------QQLAF----------IKYEQQAAGELEYAidLSDMDYAKFAEACGGKGYRVEKAEELDPAFE 514
|
570
....*....|....*..
gi 1757862790 589 AARRETVSTLIDIKVLP 605
Cdd:PRK08611 515 EALAQDKPVIIDVYVDP 531
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
3-609 |
1.13e-34 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 139.12 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 3 KLRLTTAQALVKFLDNQYLEVdgvelkfvkgifaIFGH--GNVLGLGQALeQDSGDMRVYQgRNEQGMAHAATGFARQAL 80
Cdd:PRK07710 13 EKLMTGAQMLIEALEKEGVEV-------------IFGYpgGAVLPLYDAL-YDCGIPHILT-RHEQGAIHAAEGYARISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 81 RRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfATrqpdpvlqqieqsydlSISTNDAFR---------AVSK 151
Cdd:PRK07710 78 KPGVVIATS--GPGATNVVTGLADAMIDSLPLVVFTGQV-AT----------------SVIGSDAFQeadimgitmPVTK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 152 YWDRITRPEQLMSACINAMRVLTDpAETGAVTLCLPQDV---QGEaWDYPESffarrVHRLDRRPA---SAAQLADAVAA 225
Cdd:PRK07710 139 HNYQVRKASDLPRIIKEAFHIATT-GRPGPVLIDIPKDMvveEGE-FCYDVQ-----MDLPGYQPNyepNLLQIRKLVQA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 226 IKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTR 305
Cdd:PRK07710 212 VSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 306 FSDFTTAS-KWIFQHPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAGWGAqiesvqsrQLKETQRV 384
Cdd:PRK07710 292 FDDRVTGNlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQALQVLLQQEGKKENHHEWLS--------LLKNWKEK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 385 YQAVWQEKSfvpeiddhldresvyrefrqitdSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVE 464
Cdd:PRK07710 364 YPLSYKRNS-----------------------ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 465 YGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEF 544
Cdd:PRK07710 421 GGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEEFYNQRYSHSL 500
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 545 RYRQPetgqlqgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLPKTMV 609
Cdd:PRK07710 501 LSCQP------------DFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKV 553
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
424-603 |
3.68e-34 |
|
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: 127.76 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 424 VLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHS 503
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 504 ELVTSLQERAKINVVLFDNMANGCINNLQMEHgmdsfgteFRYRQPETgqlqgGLVPVDFATIAAGYGCKTWRVTTLDEL 583
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAF--------YGGRVSGT-----DLSNPDFAALAEAYGAKGVRVEDPEDL 148
|
170 180
....*....|....*....|
gi 1757862790 584 RHALDAARRETVSTLIDIKV 603
Cdd:cd00568 149 EAALAEALAAGGPALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
19-604 |
1.58e-31 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 129.34 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 19 QYLEVDGVELKFvkGIFAIfgHGnvLGLGQALEQdSGDMRVYQGRNEQGMAHAATGFARQalRRQIIACTSSIGPGAAN- 97
Cdd:PRK07064 11 AFLEQCGVKTAF--GVISI--HN--MPILDAIGR-RGKIRFVPARGEAGAVNMADAHARV--SGGLGVALTSTGTGAGNa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 98 ---MITA--AGTasanriPLLLLPGDVfATRQPDPVLQQIEQSYD-LSIstndaFRAVSKYWDRITRPEQLMSACINAMR 171
Cdd:PRK07064 82 agaLVEAltAGT------PLLHITGQI-ETPYLDQDLGYIHEAPDqLTM-----LRAVSKAAFRVRSAETALATIREAVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 172 V-LTDPaeTGAVTLCLPQDVQGEAWDYPESFFARRVhrlDRRPASAAQLADAVAAIKASRKPLIVCGGGVKysGAGEALS 250
Cdd:PRK07064 150 VaLTAP--TGPVSVEIPIDIQAAEIELPDDLAPVHV---AVPEPDAAAVAELAERLAAARRPLLWLGGGAR--HAGAEVK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 251 RFAERyGVPFAETQAGKGTVVSSHPLNVGGVGETGclAANLLAKEADLVIGVGTRFSDFTTAsKWIFQHPEVRF-LNINV 329
Cdd:PRK07064 223 RLVDL-GFGVVTSTQGRGVVPEDHPASLGAFNNSA--AVEALYKTCDLLLVVGSRLRGNETL-KYSLALPRPLIrVDADA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 330 SNFDAWKLDGIAMLADAREAMTALDAALADSGW-QAGWGAQIesVQSRQLKETQrVYQAVWQEKSFVPEIDDHLDRESVY 408
Cdd:PRK07064 299 AADGRGYPNDLFVHGDAARVLARLADRLEGRLSvDPAFAADL--RAAREAAVAD-LRKGLGPYAKLVDALRAALPRDGNW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 409 reFRQITDStltqSSVLGvlNETLPA---EAVIVAAAGSLPGDLQrvwrnraentyhveygyscMGyevnaaLGVKLAQP 485
Cdd:PRK07064 376 --VRDVTIS----NSTWG--NRLLPIfepRANVHALGGGIGQGLA-------------------MA------IGAALAGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 486 QSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHgmdsFGTEFRYRQpetgqlqggLVPVDFAT 565
Cdd:PRK07064 423 GRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQ----YGGRRYYVE---------LHTPDFAL 489
|
570 580 590
....*....|....*....|....*....|....*....
gi 1757862790 566 IAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVL 604
Cdd:PRK07064 490 LAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDML 528
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-601 |
2.46e-31 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 129.35 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 1 MGKLRLTTAQALVKfldnqYLEVDGVELKFvkGIfaifghgnvlgLGQALeQDSGDM------RVYQGRNEQGMAHAATG 74
Cdd:PRK07525 1 MGKMKMTPSEAFVE-----TLQAHGITHAF--GI-----------IGSAF-MDASDLfppagiRFIDVAHEQNAGHMADG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 75 FARQALRRQiiACTSSIGPGAANMITAAGTASANRIPLLLLpgdvfaTRQPDPV------LQQIEQSydlsistnDAFRA 148
Cdd:PRK07525 62 YTRVTGRMG--MVIGQNGPGITNFVTAVATAYWAHTPVVLV------TPQAGTKtigqggFQEAEQM--------PMFED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 149 VSKYWDRITRPEQlMSACINamRVLTDP-AETGAVTLCLPQDvqgeawdypesFFARRV-------HRLDRRPASAAQLA 220
Cdd:PRK07525 126 MTKYQEEVRDPSR-MAEVLN--RVFDKAkRESGPAQINIPRD-----------YFYGVIdveipqpVRLERGAGGEQSLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 221 DAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVI 300
Cdd:PRK07525 192 EAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 301 GVGTRFSDFTTASK-----W-----IFQhpevrfLNINVSNFDAWKLDGIAMLADAREAMTALDAALA-----DSGwQAG 365
Cdd:PRK07525 272 ALGTRLNPFGTLPQygidyWpkdakIIQ------VDINPDRIGLTKKVSVGICGDAKAVARELLARLAerlagDAG-REE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 366 WGAQIESVQSRQLKEtqrvyqavwqeksfVPEIDDHLDRESVYREFRQITDST--LTQSSVLGVLNETLPAEAVIVAAAG 443
Cdd:PRK07525 345 RKALIAAEKSAWEQE--------------LSSWDHEDDDPGTDWNEEARARKPdyMHPRQALREIQKALPEDAIVSTDIG 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 444 SLpgdlqrvwrNRAENTY--------HVEYGY--SCmGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERA 513
Cdd:PRK07525 411 NN---------CSIANSYlrfekgrkYLAPGSfgNC-GYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNW 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 514 KINVVLFDNMANGCINNLQMEHGMDSF-GTEFRyrqpetgqlqgglVPVDFATIAAGYGCKTWRVTTLDELRHALDAA-- 590
Cdd:PRK07525 481 PVTAVVFRNYQWGAEKKNQVDFYNNRFvGTELD-------------NNVSYAGIAEAMGAEGVVVDTQEELGPALKRAid 547
|
650
....*....|..
gi 1757862790 591 -RRETVSTLIDI 601
Cdd:PRK07525 548 aQNEGKTTVIEI 559
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
32-590 |
4.03e-31 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 128.43 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 32 KGIFAIFGH--GNVLGLGQALEQDSGDMRVYQgRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANR 109
Cdd:PRK07979 17 QGVKQVFGYpgGAVLDIYDALHTVGGIDHVLV-RHEQAAVHMADGLARATGEVGVVLVTS--GPGATNAITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 110 IPLLLLPGDVfATrqpdpvlqqieqsydlSISTNDAF---------RAVSKYWDRITRPEQLMSACINAMrVLTDPAETG 180
Cdd:PRK07979 94 IPLVVLSGQV-AT----------------SLIGYDAFqecdmvgisRPVVKHSFLVKQTEDIPQVLKKAF-WLAASGRPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 181 AVTLCLPQDVQGEA----WDYPESFFARRV------HRLDRRPAsaaqladaVAAIKASRKPLIVCGGGVKYSGAGEALS 250
Cdd:PRK07979 156 PVVVDLPKDILNPAnklpYVWPESVSMRSYnpttqgHKGQIKRA--------LQTLVAAKKPVVYVGGGAINAACHQQLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 251 RFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTT--ASKWIfqhPEVRFLNIN 328
Cdd:PRK07979 228 ELVEKLNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTnnLAKYC---PNATVLHID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 329 VSNFDAWKL--DGIAMLADAREAMTALDAALADSGWQA------GWGAQIESVQSRQLKETQRVyqavwqeksfvpeiDD 400
Cdd:PRK07979 305 IDPTSISKTvtADIPIVGDARQVLEQMLELLSQESAHQpldeirDWWQQIEQWRARQCLKYDTH--------------SE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 401 HLDRESVYREFRQITDSTLTQSSVLGVLNetlpaeaviVAAAGSLPGDLQRVWRNRAentyhveyGYSCMGYEVNAALGV 480
Cdd:PRK07979 371 KIKPQAVIETLWRLTKGDAYVTSDVGQHQ---------MFAALYYPFDKPRRWINSG--------GLGTMGFGLPAALGV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 481 KLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQmehGMDSFGtefRYRQPETGQLQgglvp 560
Cdd:PRK07979 434 KMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQ---DMIYSG---RHSQSYMQSLP----- 502
|
570 580 590
....*....|....*....|....*....|
gi 1757862790 561 vDFATIAAGYGCKTWRVTTLDELRHALDAA 590
Cdd:PRK07979 503 -DFVRLAEAYGHVGIQISHPDELESKLSEA 531
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
10-188 |
5.06e-29 |
|
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: 113.01 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 10 QALVKFLDNQylevdGVELkfvkgIFAIFGHGNvLGLGQALEQDsgDMRVYQGRNEQGMAHAATGFARQALRRQiiACTS 89
Cdd:cd07035 1 DALVEALKAE-----GVDH-----VFGVPGGAI-LPLLDALARS--GIRYILVRHEQGAVGMADGYARATGKPG--VVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 90 SIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQsydlsistNDAFRAVSKYWDRITRPEQLMSACINA 169
Cdd:cd07035 66 TSGPGLTNAVTGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQ--------VALFRPITKWAYRVTSPEEIPEALRRA 137
|
170
....*....|....*....
gi 1757862790 170 MRVLTDPAeTGAVTLCLPQ 188
Cdd:cd07035 138 FRIALSGR-PGPVALDLPK 155
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-590 |
1.21e-28 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 121.00 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 6 LTTAQALVKFLDNQylevdGVELkfvkgifaIFGH--GNVLGLGQAL-EQDsgDMRVYQGRNEQGMAHAATGFARQALRR 82
Cdd:PRK06466 4 LSGAEMLVRALRDE-----GVEY--------IYGYpgGAVLHIYDALfKQD--KVEHILVRHEQAATHMADGYARATGKT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 83 QIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQsydLSIStndafRAVSKYWDRITRPEQL 162
Cdd:PRK06466 69 GVVLVTS--GPGATNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDM---VGIS-----RPIVKHSFMVKHASEI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 163 mSACINAMRVLTDPAETGAVTLCLPQDV----QGEAWDYPESFFAR------RVHRLDRRPAsaaqladaVAAIKASRKP 232
Cdd:PRK06466 139 -PEIIKKAFYIAQSGRPGPVVVDIPKDMtnpaEKFEYEYPKKVKLRsyspavRGHSGQIRKA--------VEMLLAAKRP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 233 LIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTT- 311
Cdd:PRK06466 210 VIYSGGGVVLGNASALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 312 -ASKWIfqhPEVRFLNINVSNFDAWK--LDGIAMLADAREAMTALDAALADSGwqagwgaqiesvqsrqlKETQRVYQAV 388
Cdd:PRK06466 290 gPAKFC---PNAKIIHIDIDPASISKtiKADIPIVGPVESVLTEMLAILKEIG-----------------EKPDKEALAA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 389 WQEksfvpEIDDHLDRESVYReFRQITDSTLTQSSVLGVLNETLPAEAVIVA--------AAGSLPGDLQRVWRNRAent 460
Cdd:PRK06466 350 WWK-----QIDEWRGRHGLFP-YDKGDGGIIKPQQVVETLYEVTNGDAYVTSdvgqhqmfAAQYYKFNKPNRWINSG--- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 461 yhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-MEHgmds 539
Cdd:PRK06466 421 -----GLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMVRQWQdMQY---- 491
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1757862790 540 fgtEFRYRQPETGQLQgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAA 590
Cdd:PRK06466 492 ---EGRHSHSYMESLP------DFVKLAEAYGHVGIRITDLKDLKPKLEEA 533
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
63-592 |
7.85e-28 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 118.37 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfatrqPDPVLQQieqsydlsist 142
Cdd:PRK06965 66 RHEQAAVHAADGYARATGKVGVALVTS--GPGVTNAVTGIATAYMDSIPMVVISGQV-----PTAAIGQ----------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 143 nDAFRAVSKYwdRITRPEQLMSACINAMRVLTDP-------AET---GAVTLCLPQDVQGE--AWDYPESFFARRVHRLd 210
Cdd:PRK06965 128 -DAFQECDTV--GITRPIVKHNFLVKDVRDLAETvkkafyiARTgrpGPVVVDIPKDVSKTpcEYEYPKSVEMRSYNPV- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 211 rRPASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAAN 290
Cdd:PRK06965 204 -TKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGMLGMHGTYEAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 291 LLAKEADLVIGVGTRFSDFTTASKWIFQHPEVRFLNINV---SNFDAWKLDgIAMLADAREAMTALDAAL------ADSG 361
Cdd:PRK06965 283 MAMQHCDVLIAIGARFDDRVIGNPAHFASRPRKIIHIDIdpsSISKRVKVD-IPIVGDVKEVLKELIEQLqtaehgPDAD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 362 WQAGWGAQIESVQSRQLKETQRVyqavwqeksfvpeiDDHLDRESVYREFRQITDSTLTQSSVLGVLNetlpaeaviVAA 441
Cdd:PRK06965 362 ALAQWWKQIEGWRSRDCLKYDRE--------------SEIIKPQYVVEKLWELTDGDAFVCSDVGQHQ---------MWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 442 AGSLPGDLQRVWRNRAentyhveyGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFD 521
Cdd:PRK06965 419 AQFYRFNEPRRWINSG--------GLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLN 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757862790 522 NMANGCINNLQ-MEHGMdsfgtefRYRQPETGQLQgglvpvDFATIAAGYGCKTWRVTTLDELRHALDAARR 592
Cdd:PRK06965 491 NRYLGMVRQWQeIEYSK-------RYSHSYMDALP------DFVKLAEAYGHVGMRIEKTSDVEPALREALR 549
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
56-605 |
1.86e-27 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 116.85 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 56 DMRVYQGRNEQGMAHAATGFARqaLRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVfatrQPDPVLQQIEQS 135
Cdd:PRK06457 39 KVKYVQVRHEEGAALAASVEAK--ITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIALTGQV----ESDMIGHDYFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 136 YDLSistnDAFRAVSKYWDRITRPEQ----LMSACINAMrvltdpAETGAVTLCLPQDVQGEAWDYPESFfarrvHRLDR 211
Cdd:PRK06457 113 VNLT----KLFDDVAVFNQILINPENaeyiIRRAIREAI------SKRGVAHINLPVDILRKSSEYKGSK-----NTEVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 212 RPASAAQLADAVAAIKASRKPLIVCGGGVKysGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANL 291
Cdd:PRK06457 178 KVKYSIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPKVMGGIGLLGTKPSIE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 292 LAKEADLVIGVGTRFsdfttaskwifqhPEVRFLNINVSNfdawkldgIAMLADAREAMTALDAALAdsgwqagwgAQIE 371
Cdd:PRK06457 256 AMDKADLLIMLGTSF-------------PYVNFLNKSAKV--------IQVDIDNSNIGKRLDVDLS---------YPIP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 372 SVQSRQLKETQRVYQAVWQEKSfvpEIDDHLDRESvYREFRqiTDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQR 451
Cdd:PRK06457 306 VAEFLNIDIEEKSDKFYEELKG---KKEDWLDSIS-KQENS--LDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTAR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 452 VWRNRAENTYHVEYGYSCMGYEVNAALGVKLA-QPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINN 530
Cdd:PRK06457 380 HFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKF 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 531 LQMEHGMDSFGTEfryrqpetgqlqggLVPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLP 605
Cdd:PRK06457 460 EQEVMGYPEWGVD--------------LYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDP 520
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
226-606 |
3.09e-27 |
|
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: 116.41 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 226 IKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGG-VGETGCLAANLLAKEADLVIGVGT 304
Cdd:COG3961 206 LAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 305 RFSDFTTAskwIFQH---PEvRFLNIN---VSNFDAWkLDGIAMladaREAMTALDAALADSGWQagwgaqiesvqsrql 378
Cdd:COG3961 286 VFTDTNTG---GFTAqldPE-RTIDIQpdsVRVGGHI-YPGVSL----ADFLEALAELLKKRSAP--------------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 379 ketqrvyqavWQEKSFVPEiddhldresvyrEFRQITDSTLTQSSVLGVLNETLPAEAVIVAAAGS---------LPGDl 449
Cdd:COG3961 342 ----------LPAPAPPPP------------PPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTslfgaadlrLPEG- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 450 qrvwrnraeNTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLqeRAKINVVLFdnmangCIN 529
Cdd:COG3961 399 ---------ATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTML--RYGLKPIIF------VLN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 530 N-----LQMEHGMDSfgtefRYRQpetgqlqggLVPVDFATIAAGYGCK---TWRVTTLDELRHALDAARRETVS-TLID 600
Cdd:COG3961 462 NdgytiERAIHGPDG-----PYND---------IANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEANTDRlTLIE 527
|
....*.
gi 1757862790 601 IkVLPK 606
Cdd:COG3961 528 V-VLDK 532
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
23-587 |
5.59e-27 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 115.99 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 23 VDGVELKFVKGIFAIFGhGNVLGLGQALEQdSGDMRVYQGRNEQGMAHAATGFARQALRRQIiaCTSSIGPGAANMITAA 102
Cdd:PLN02470 20 VEALEREGVDTVFAYPG-GASMEIHQALTR-SNCIRNVLCRHEQGEVFAAEGYAKASGKVGV--CIATSGPGATNLVTGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 103 GTASANRIPLLLLPG---------DVFatrQPDP---VLQQIEQSYDLSISTNDAFRAVSK--YWDRITRPeqlmsacin 168
Cdd:PLN02470 96 ADALLDSVPLVAITGqvprrmigtDAF---QETPiveVTRSITKHNYLVMDVEDIPRVIREafFLASSGRP--------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 169 amrvltdpaetGAVTLCLPQDVQGEA----WDYPESFFARrVHRLDRRPASAAQLADAVAaIKASRKPLIVCGGGVkySG 244
Cdd:PLN02470 164 -----------GPVLVDIPKDIQQQLavpnWNQPMKLPGY-LSRLPKPPEKSQLEQIVRL-ISESKRPVVYVGGGC--LN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 245 AGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTT------ASKWIFQ 318
Cdd:PLN02470 229 SSEELREFVELTGIPVASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTgkleafASRASIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 319 HpevrfLNINVSNFDAWKLDGIAMLADAREAMTALDAALadsgwqagwgaqiesvQSRQLKETQRvyqAVWQEksfvpEI 398
Cdd:PLN02470 309 H-----IDIDPAEIGKNKQPHVSVCADVKLALQGLNKLL----------------EERKAKRPDF---SAWRA-----EL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 399 DDHldRESVYREFRQITDSTLTQSSVlGVLNETLPAEAVIVA--------AAGSLPGDLQRVWRNRAentyhveyGYSCM 470
Cdd:PLN02470 360 DEQ--KEKFPLSYPTFGDAIPPQYAI-QVLDELTDGNAIISTgvgqhqmwAAQWYKYKEPRRWLTSG--------GLGAM 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 471 GYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCInnLQMEhgmDSFGTEFRYR--- 547
Cdd:PLN02470 429 GFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMV--VQWE---DRFYKANRAHtyl 503
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1757862790 548 -QPETgqlQGGLVPvDFATIAAGYGCKTWRVTTLDELRHAL 587
Cdd:PLN02470 504 gDPDA---EAEIFP-DFLKFAEGCKIPAARVTRKSDLREAI 540
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
6-597 |
1.34e-26 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 114.80 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 6 LTTAQALVKFLDNQylevdGVElkfvkgifAIFGH--GNVLGLGQALEQDSgDMRVYQGRNEQGMAHAATGFARQALRRQ 83
Cdd:PRK09107 11 MTGAEMVVQALKDQ-----GVE--------HIFGYpgGAVLPIYDEIFQQD-DIQHILVRHEQGAGHAAEGYARSTGKPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 84 IIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVfatrqPDPVLqqieqsydlsisTNDAFRAVSKYwdRITRP---- 159
Cdd:PRK09107 77 VVLVTS--GPGATNAVTPLQDALMDSIPLVCITGQV-----PTHLI------------GSDAFQECDTV--GITRPctkh 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 160 -------EQLMSACINAMRVLTDpAETGAVTLCLPQDVQGEAWDY-PESFFARRVHRLDRRPASAAQLADAVAAIKASRK 231
Cdd:PRK09107 136 nwlvkdvNDLARVIHEAFHVATS-GRPGPVVVDIPKDVQFATGTYtPPQKAPVHVSYQPKVKGDAEAITEAVELLANAKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 232 PLIVCGGGVKYSG--AGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSD- 308
Cdd:PRK09107 215 PVIYSGGGVINSGpeASRLLRELVELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDr 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 309 -------FTTASKWIFQHPEVRFLNINVsnfdawKLDgIAMLADAREAMTALDAAladsgWQAgwgaqiesvqsRQLKET 381
Cdd:PRK09107 295 itgrldaFSPNSKKIHIDIDPSSINKNV------RVD-VPIIGDVGHVLEDMLRL-----WKA-----------RGKKPD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 382 QRVYQAVWQeksfvpEIDDHLDRESVYreFRQITDSTLTQSSVLGVLNETLPAEAVIVAAAGSlpgdlQRVWrnrAENTY 461
Cdd:PRK09107 352 KEALADWWG------QIARWRARNSLA--YTPSDDVIMPQYAIQRLYELTKGRDTYITTEVGQ-----HQMW---AAQFF 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 462 HVEY--------GYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ- 532
Cdd:PRK09107 416 GFEEpnrwmtsgGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGMVRQWQq 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 533 MEHGMdsfgtefRYRQPETGQLqgglvPvDFATIAAGYGCKTWRVTTLDElrhaLDAARRETVST 597
Cdd:PRK09107 496 LLHGN-------RLSHSYTEAM-----P-DFVKLAEAYGAVGIRCEKPGD----LDDAIQEMIDV 543
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
424-605 |
2.61e-23 |
|
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: 97.22 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 424 VLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHS 503
Cdd:cd02014 7 VAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 504 ELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEfryrqpetgqlqggLVPVDFATIAAGYGCKTWRVTTLDEL 583
Cdd:cd02014 87 DLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVD--------------LPNPDFAKIAEAMGIKGIRVEDPDEL 152
|
170 180
....*....|....*....|..
gi 1757862790 584 RHALDAARRETVSTLIDIKVLP 605
Cdd:cd02014 153 EAALDEALAADGPVVIDVVTDP 174
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
9-193 |
2.70e-23 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 96.92 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 9 AQALVKFLDNQYlevdgvelkfVKGIFAIFGhGNVLGLGQALEqDSGDMRVYQGRNEQGMAHAATGFARQALRRQIIACT 88
Cdd:pfam02776 2 AEALADVLKALG----------VDTVFGVPG-GHILPLLDALA-KSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 89 SsiGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIeqsydlsISTNDAFRAVSKYWDRITRPEQLMSACIN 168
Cdd:pfam02776 70 S--GPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQE-------LDQLALFRPVTKWAVRVTSADEIPEVLRR 140
|
170 180
....*....|....*....|....*
gi 1757862790 169 AMRVLTDPaETGAVTLCLPQDVQGE 193
Cdd:pfam02776 141 AFRAALSG-RPGPVYLEIPLDVLLE 164
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
424-609 |
2.22e-22 |
|
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: 94.87 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 424 VLGVLNETLPAEAVIVA--------AAgslpgdlqRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGD 495
Cdd:cd02015 6 VIKELSELTPGDAIVTTdvgqhqmwAA--------QYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 496 GSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQ-MEHGMDSFGTEFRYrQPetgqlqgglvpvDFATIAAGYGCKT 574
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQeLFYEGRYSHTTLDS-NP------------DFVKLAEAYGIKG 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1757862790 575 WRVTTLDELRHALDAARRETVSTLIDIKVLPKTMV 609
Cdd:cd02015 145 LRVEKPEELEAALKEALASDGPVLLDVLVDPEENV 179
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
93-603 |
1.75e-20 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 95.45 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 93 PGAANMITAAGTASANRIPLLllpgdVFATRQPdpVLQQIEQ-SYDLSIS-TNDAF------RAVSKYWDRITRPEQLMS 164
Cdd:PRK08327 85 VGTANALGGVHNAARSRIPVL-----VFAGRSP--YTEEGELgSRNTRIHwTQEMRdqgglvREYVKWDYEIRRGDQIGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 165 ACINAMRVL-TDPAetGAVTLCLPQDVQGEAWDYPESFFARRVHRldRRPA-SAAQLADAVAAIKASRKPLIVCGGGVKY 242
Cdd:PRK08327 158 VVARAIQIAmSEPK--GPVYLTLPREVLAEEVPEVKADAGRQMAP--APPApDPEDIARAAEMLAAAERPVIITWRAGRT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 243 SGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETgclaanLLAkEADLVIGVGT------RFSDFTTASKWI 316
Cdd:PRK08327 234 AEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRA------DLA-EADLVLVVDSdvpwipKKIRPDADARVI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 317 FQHPEVRFLNINVSNFDAwkldGIAMLADAREAMTALDAALADSgwqagWGAQIESVQSRQLKETQRVYQAVWQEKsfvP 396
Cdd:PRK08327 307 QIDVDPLKSRIPLWGFPC----DLCIQADTSTALDQLEERLKSL-----ASAERRRARRRRAAVRELRIRQEAAKR---A 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 397 EIDDHLDRESVYREFrqitdstltqssVLGVLNETLPAEAVIVAAAGSLPGDLQRvwrnRAENTYHVEYGYSCMGYEVNA 476
Cdd:PRK08327 375 EIERLKDRGPITPAY------------LSYCLGEVADEYDAIVTEYPFVPRQARL----NKPGSYFGDGSAGGLGWALGA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 477 ALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAK--INVVLFDnmaNGCINNLQmehgmdsFGTEFRYrqPE---- 550
Cdd:PRK08327 439 ALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVAERYGlpVLVVVFN---NGGWLAVK-------EAVLEVY--PEgyaa 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 551 -TGQLQGGLV--PVDFATIAAGYGCKTWRVTTLDE----LRHALDAARRETVSTLIDIKV 603
Cdd:PRK08327 507 rKGTFPGTDFdpRPDFAKIAEAFGGYGERVEDPEElkgaLRRALAAVRKGRRSAVLDVIV 566
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
419-603 |
5.94e-20 |
|
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: 87.65 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 419 LTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYhveygYSC----MGYEVNAALGVKLAQPQSEVYSLVG 494
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSY-----FTLrgggLGWGLPAAVGAALANPDRKVVAIIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 495 DGSFMMLHSELVTSLQERAKINVVLFDnmaNGCINNLQMEhgMDSFGTEfryRQPETGQLQGGLV--PVDFATIAAGYGC 572
Cdd:cd02002 76 DGSFMYTIQALWTAARYGLPVTVVILN---NRGYGALRSF--LKRVGPE---GPGENAPDGLDLLdpGIDFAAIAKAFGV 147
|
170 180 190
....*....|....*....|....*....|.
gi 1757862790 573 KTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:cd02002 148 EAERVETPEELDEALREALAEGGPALIEVVV 178
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
63-601 |
1.83e-19 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 92.36 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 63 RNEQGMAHAATgfARQALRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLpgdvfATRQPDpvlQQIEQSYDLSIST 142
Cdd:PRK06546 48 RHEEAAAFAAA--AEAQLTGKLAVCAGSCGPGNLHLINGLYDAHRSGAPVLAI-----ASHIPS---AQIGSGFFQETHP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 143 NDAFRAVSKYWDRITRPEQ----LMSACINAMrvltdpAETGAVTLCLPQDVQGEawDYPESFFARRVhrLDRRPA---S 215
Cdd:PRK06546 118 DRLFVECSGYCEMVSSAEQaprvLHSAIQHAV------AGGGVSVVTLPGDIADE--PAPEGFAPSVI--SPRRPTvvpD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 216 AAQLADAVAAIKASRKPLIVCGGGVKysGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKE 295
Cdd:PRK06546 188 PAEVRALADAINEAKKVTLFAGAGVR--GAHAEVLALAEKIKAPVGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 296 ADLVIGVGTRF--SDFTtaskwifqhPEVRFLNINVsnfDAWKLD-----GIAMLADAREAMTAL--------DAALADs 360
Cdd:PRK06546 266 ADLLILLGTDFpyDQFL---------PDVRTAQVDI---DPEHLGrrtrvDLAVHGDVAETIRALlplvkektDRRFLD- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 361 gwqagwgaqiesvqsRQLKETQRVYQAVwqEKSFVPEIDDHldrESVYREFrqitdstltqssVLGVLNETLPAEAVIVA 440
Cdd:PRK06546 333 ---------------RMLKKHARKLEKV--VGAYTRKVEKH---TPIHPEY------------VASILDELAADDAVFTV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 441 AAGslpgdLQRVWRNR--AENTYHVEYGYSCMGYEVNA---ALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKI 515
Cdd:PRK06546 381 DTG-----MCNVWAARyiTPNGRRRVIGSFRHGSMANAlphAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 516 NVVLFDNMANGCINNLQMEHGMDSFGTEFRyrqpetgqlqgglvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETV 595
Cdd:PRK06546 456 KVVVFNNSTLGMVKLEMLVDGLPDFGTDHP--------------PVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPG 521
|
....*.
gi 1757862790 596 STLIDI 601
Cdd:PRK06546 522 PALVDV 527
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
428-603 |
3.23e-19 |
|
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: 85.42 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 428 LNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVT 507
Cdd:cd02010 8 LRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 508 SLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEFRyrqpetgqlqgglvPVDFATIAAGYGCKTWRVTTLDELRHAL 587
Cdd:cd02010 88 AVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFG--------------NPDFVKYAESFGAKGYRIESADDLLPVL 153
|
170
....*....|....*.
gi 1757862790 588 DAARRETVSTLIDIKV 603
Cdd:cd02010 154 ERALAADGVHVIDCPV 169
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
67-604 |
6.80e-19 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 90.40 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 67 GMAhaaTGFArQALRRqiiactssigPGAANMITAAG---------TASANRIPLLLLPGD-VFATRQPDPVLqqieqsy 136
Cdd:PRK07092 62 GMA---DGYA-QATGN----------AAFVNLHSAAGvgnamgnlfTAFKNHTPLVITAGQqARSILPFEPFL------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 137 dlsiSTNDAF---RAVSKYWDRITRPEQLMSACINAMRVLTDPAeTGAVTLCLPQDvqgeAWDYP-ESFFARRVHRlDRR 212
Cdd:PRK07092 121 ----AAVQAAelpKPYVKWSIEPARAEDVPAAIARAYHIAMQPP-RGPVFVSIPYD----DWDQPaEPLPARTVSS-AVR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 213 PaSAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVP-FAETQAGKGTVVSSHPLnVGGVGETGCLAANL 291
Cdd:PRK07092 191 P-DPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPvWVAPMSGRCSFPEDHPL-FAGFLPASREKISA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 292 LAKEADLVIGVGT---RFSDFTTASkwIFQHPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAGwga 368
Cdd:PRK07092 269 LLDGHDLVLVIGApvfTYHVEGPGP--HLPEGAELVQLTDDPGEAAWAPMGDAIVGDIRLALRDLLALLPPSARPAP--- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 369 qiesvQSRQLKETqrvyqavwqeksfVPEIDDHLDRESVyrefrqitdstltqssvLGVLNETLPAEAVIVAAAGSLPGD 448
Cdd:PRK07092 344 -----PARPMPPP-------------APAPGEPLSVAFV-----------------LQTLAALRPADAIVVEEAPSTRPA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 449 LQRVWRNRAENTYhveygYSC----MGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMA 524
Cdd:PRK07092 389 MQEHLPMRRQGSF-----YTMasggLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 525 NGcinnlqmehGMDSFGTEFRYRQpetgqLQGGLVP-VDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:PRK07092 464 YG---------ALRWFAPVFGVRD-----VPGLDLPgLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEV 529
|
.
gi 1757862790 604 L 604
Cdd:PRK07092 530 A 530
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
9-603 |
9.76e-18 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 86.83 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 9 AQALVKFLDNQylevdGVELkfvkgIFAIFGhGNVLGLGQALEQDSGDMRVyqGRNEQGMAHAATGFARQALRRQIIACT 88
Cdd:PRK08617 8 ADLVVDSLINQ-----GVKY-----VFGIPG-AKIDRVFDALEDSGPELIV--TRHEQNAAFMAAAIGRLTGKPGVVLVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 89 SsiGPGAANMITAAGTASANRIPLLLLPGDVfatRQPDpVLQQIEQSYDlsisTNDAFRAVSKYWDRITRPEQLMSACIN 168
Cdd:PRK08617 75 S--GPGVSNLATGLVTATAEGDPVVAIGGQV---KRAD-RLKRTHQSMD----NVALFRPITKYSAEVQDPDNLSEVLAN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 169 AMRVltdpAET---GAVTLCLPQDVQGEawdyPESFFARRVHRLDRR-PASAAQLADAVAAIKASRKPLIVCGGGVKYSG 244
Cdd:PRK08617 145 AFRA----AESgrpGAAFVSLPQDVVDA----PVTSKAIAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGMRASSPE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 245 AGEALSRFAERYGVPFAETQAGKGTVvsSHPLN---VGGVGetgcLAAN----LLAKEADLVIGVGtrFS----DfttAS 313
Cdd:PRK08617 217 VTAAIRRLLERTNLPVVETFQAAGVI--SRELEdhfFGRVG----LFRNqpgdELLKKADLVITIG--YDpieyE---PR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 314 KWIFQ-------------------HPEVRFL-NINVS-NFDAWKLDGIAMLADAREAMTALDAALADsgwQAGWGAQIES 372
Cdd:PRK08617 286 NWNSEgdatiihidvlpaeidnyyQPERELIgDIAATlDLLAEKLDGLSLSPQSLEILEELRAQLEE---LAERPARLEE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 373 VQSRQLketqrvyqavwqekSFVPEIDDHLDresvyrefrqiTDSTLTqssvlgvlnetlpaeaVIVaaaGSLpgdlqRV 452
Cdd:PRK08617 363 GAVHPL--------------RIIRALQDIVT-----------DDTTVT----------------VDV---GSH-----YI 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 453 WRNRAENTY---HVEY--GYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLqeRAKINVVLF---DNMA 524
Cdd:PRK08617 394 WMARYFRSYeprHLLFsnGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAV--RLKLNIVHIiwnDGHY 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 525 NgcinnlqmehgMDSFGTEFRYRQP---ETGqlqgglvPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDI 601
Cdd:PRK08617 472 N-----------MVEFQEEMKYGRSsgvDFG-------PVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDI 533
|
..
gi 1757862790 602 KV 603
Cdd:PRK08617 534 PV 535
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
56-601 |
4.62e-17 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 84.77 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 56 DMRVYQGRNEQGMAHAATGFARQALRRQIIACTSsiGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQS 135
Cdd:PRK05858 42 GIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTA--GPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 136 ydlsistnDAFRAVSKYWDRITRPEQLMSACINAMRVLTDPaETGAVTLCLPQDV---QGEAWDYPESFFARRVHRldrr 212
Cdd:PRK05858 120 --------PFVAPVTKFAATAQSAENAGRLVDQALQAAVTP-HRGPVFVDFPMDHafsMADDDGRPGALTELPAGP---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 213 PASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGvgetgclAANLL 292
Cdd:PRK05858 187 TPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSR-------ARGKA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 293 AKEADLVIGVGTRFsDFTTASKWIFQHPEVrflninVSNFDA-WKLDGIAMLA-----DAREAMTALDAALADSGWQAGW 366
Cdd:PRK05858 260 LGEADVVLVVGVPM-DFRLGFGVFGGTAQL------VHVDDApPQRAHHRPVAaglygDLSAILSALAGAGGDRTDHQGW 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 367 GAQIESVQSrqlketqrvyQAVWQEKSFVPEIDDHLDRESVYREfrqitdstltqssvlgvLNETLPAEAVIVAAAGSLP 446
Cdd:PRK05858 333 IEELRTAET----------AARARDAAELADDRDPIHPMRVYGE-----------------LAPLLDRDAIVIGDGGDFV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 447 GDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSF---MMLHSELVtslqeRAKINVVLFdnM 523
Cdd:PRK05858 386 SYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFgfsLMDVDTLV-----RHNLPVVSV--I 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757862790 524 ANGCINNLQmEHGMdsfgtEFRYRQPETGQLQGGLvPVDFATIAAGYGCKTwrVTTLDELRHALDAARRETVSTLIDI 601
Cdd:PRK05858 459 GNNGIWGLE-KHPM-----EALYGYDVAADLRPGT-RYDEVVRALGGHGEL--VTVPAELGPALERAFASGVPYLVNV 527
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
423-603 |
4.95e-17 |
|
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: 79.11 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 423 SVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSF---M 499
Cdd:cd02004 3 RVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFgfsG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 500 MlhsELVTSLQERAKINVVLfdnMANGCINnlqmeHGMDSFGTEFRYRQPeTGQLqggLVPVDFATIAAGYGCKTWRVTT 579
Cdd:cd02004 83 M---ELETAVRYNLPIVVVV---GNNGGWY-----QGLDGQQLSYGLGLP-VTTL---LPDTRYDLVAEAFGGKGELVTT 147
|
170 180
....*....|....*....|....
gi 1757862790 580 LDELRHALDAARRETVSTLIDIKV 603
Cdd:cd02004 148 PEELKPALKRALASGKPALINVII 171
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
45-590 |
2.01e-16 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 82.73 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 45 GLGQALEQDsGDMRVYQGRNEQGMAHAATGFArqALRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLpgdvfATRQ 124
Cdd:PRK09124 31 GLSDSLRRM-GTIEWMHTRHEEVAAFAAGAEA--QLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAI-----AAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 125 PDPvlqQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMSACINAMRvlTDPAETGAVTLCLPQDVQ-GEAWDYPESFFA 203
Cdd:PRK09124 103 PSS---EIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMR--KAILNRGVAVVVLPGDVAlKPAPERATPHWY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 204 RRVHRLDRRPASAAQLADAVaaIKASRKPLIVCGGGVkySGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGE 283
Cdd:PRK09124 178 HAPQPVVTPAEEELRKLAAL--LNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEYDNPYDVGMTGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 284 TGCLAANLLAKEADLVIGVGTRF--SDFTTASKWIFQhpevrfLNINVSNFDA-WKLDgIAMLADAREAMTALdaalads 360
Cdd:PRK09124 254 IGFSSGYHAMMNCDTLLMLGTDFpyRQFYPTDAKIIQ------IDINPGSLGRrSPVD-LGLVGDVKATLAAL------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 361 gwqagwgaqiesvQSRQLKETQRvyqavwqeksfvpeidDHLDReSV--YREFRQITDSTLTQSS---------VLGVLN 429
Cdd:PRK09124 320 -------------LPLLEEKTDR----------------KFLDK-ALehYRKARKGLDDLAVPSDggkpihpqyLARQIS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 430 ETLPAEAVIVAAAGSlPgdlqRVWRNR-----AENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSE 504
Cdd:PRK09124 370 EFAADDAIFTCDVGT-P----TVWAARylkmnGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 505 LVTSLQERAKINVVLFDnmaNGCINNLQMEH---GMDSFGTEfryrqpetgqlqggLVPVDFATIAAGYGCKTWRVTTLD 581
Cdd:PRK09124 445 FLSLVQLKLPVKIVVFN---NSVLGFVAMEMkagGYLTDGTD--------------LHNPDFAAIAEACGITGIRVEKAS 507
|
....*....
gi 1757862790 582 ELRHALDAA 590
Cdd:PRK09124 508 ELDGALQRA 516
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
7-370 |
6.20e-16 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 81.19 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 7 TTAQALVKFLDNQYLEVDGVELKFVKGIFAIFGHgNVLGLGQaLEQDSGdMRVYQGRNEQ--GMAHAATGFARQalrRQI 84
Cdd:PRK09259 1 TAMSDQLQLTDGFHLVIDALKLNGIDTIYGVVGI-PITDLAR-LAQAEG-IRYIGFRHEQsaGNAAAAAGFLTQ---KPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 85 IACTSSiGPGAANMITAAGTASANRIPLLLLPGDvfATRQ-PDpvLQQ--IEQSYDLSIStndafRAVSKYWDRITRPEQ 161
Cdd:PRK09259 75 VCLTVS-APGFLNGLTALANATTNCFPMIMISGS--SEREiVD--LQQgdYEELDQLNAA-----KPFCKAAFRVNRAED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 162 LMSACINAMRVLTDpAETGAVTLCLPQDVQGEAWDYPESffARRVHRL-DRRPA---SAAQLADAVAAIKASRKPLIVCG 237
Cdd:PRK09259 145 IGIGVARAIRTAVS-GRPGGVYLDLPAKVLAQTMDADEA--LTSLVKVvDPAPAqlpAPEAVDRALDLLKKAKRPLIILG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 238 GGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGgvgetgclAANLLA-KEADLVIGVGTRFSdfttaskWI 316
Cdd:PRK09259 222 KGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAA--------AARSLAlANADVVLLVGARLN-------WL 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1757862790 317 FQH-------PEVRFLNINVsnfDAWKLDG---IA--MLADAREAMTALDAALADSGWQAG--WGAQI 370
Cdd:PRK09259 287 LSHgkgktwgADKKFIQIDI---EPQEIDSnrpIAapVVGDIGSVMQALLAGLKQNTFKAPaeWLDAL 351
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
430-605 |
8.81e-13 |
|
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: 67.34 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 430 ETLPAEAVIVAAAGSLPGDLQRVwRNRAENTYHVE-YGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTS 508
Cdd:cd03371 10 SRAPATAAVVSTTGMTSRELFEL-RDRPGGGHAQDfLTVGSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 509 LQERAK--INVVLfdnmANGCinnlqmeHgmDSFGTefryrQPETGQlqgglvPVDFATIAAGYG-CKTWRVTTLDELRH 585
Cdd:cd03371 89 GGLAPAnlIHIVL----NNGA-------H--DSVGG-----QPTVSF------DVSLPAIAKACGyRAVYEVPSLEELVA 144
|
170 180
....*....|....*....|
gi 1757862790 586 ALDAARRETVSTLIDIKVLP 605
Cdd:cd03371 145 ALAKALAADGPAFIEVKVRP 164
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
418-606 |
6.08e-12 |
|
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: 64.48 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 418 TLTQSSVLGVLNETLPAEAVIVAAAGS---------LPGDLQrvwrnraentYHVEYGYSCMGYEVNAALGVKLAQPQSE 488
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTswfgaldlkLPKGTR----------FISQPLWGSIGYSVPAALGAALAAPDRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 489 VYSLVGDGSFMMLHSELVTSLqeRAKINVVLFdnmangCINN-----LQMEHGMDSfgtefRYRQpetgqlqggLVPVDF 563
Cdd:cd02005 71 VILLVGDGSFQMTVQELSTMI--RYGLNPIIF------LINNdgytiERAIHGPEA-----SYND---------IANWNY 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1757862790 564 ATIA----AGYGCKTWRVTTLDELRHALDAARRET-VSTLIDIkVLPK 606
Cdd:cd02005 129 TKLPevfgGGGGGLSFRVKTEGELDEALKDALFNRdKLSLIEV-ILPK 175
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
31-191 |
6.18e-12 |
|
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: 64.11 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 31 VKGIFAIFGHGNvLGLGQALeQDSGDMRVYQGRNEQGMAHAATGFARqaLRRQIIACTSSIGPGAANMITAAGTASANRI 110
Cdd:cd07039 15 VKRVYGIPGDSI-NGLMDAL-RREGKIEFIQVRHEEAAAFAASAEAK--LTGKLGVCLGSSGPGAIHLLNGLYDAKRDRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 111 PLLLLPGDVfatrqpdpVLQQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMSACINAMRvlTDPAETGAVTLCLPQDV 190
Cdd:cd07039 91 PVLAIAGQV--------PTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIR--TAIAKRGVAVLILPGDV 160
|
.
gi 1757862790 191 Q 191
Cdd:cd07039 161 Q 161
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
424-605 |
2.37e-11 |
|
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: 63.30 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 424 VLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHS 503
Cdd:cd02013 9 VLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 504 ELVTSLQERAKINVVLFDNMANGCINNLQmehgMDSFGTEFryrqpetgqLQGGLVPVDFATIAAGYGCKTWRVTTLDEL 583
Cdd:cd02013 89 EIMTAVRHKLPVTAVVFRNRQWGAEKKNQ----VDFYNNRF---------VGTELESESFAKIAEACGAKGITVDKPEDV 155
|
170 180
....*....|....*....|....*
gi 1757862790 584 RHALD---AARRETVSTLIDIKVLP 605
Cdd:cd02013 156 GPALQkaiAMMAEGKTTVIEIVCDQ 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
470-592 |
1.66e-10 |
|
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: 61.14 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 470 MGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDsFGTEFRYRQP 549
Cdd:cd02006 59 LGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMD-YQVNLAFENI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1757862790 550 ETGQLQGglVPVDFATIAAGYGCKTWRVTTLDELRHALDAARR 592
Cdd:cd02006 138 NSSELGG--YGVDHVKVAEGLGCKAIRVTKPEELAAAFEQAKK 178
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
477-603 |
4.13e-09 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 56.06 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 477 ALGVKLAQPQsEVYSLVGDGSFmmLH---SELVTSlQERAKINVVLFDNmaNGcinnlqmehgmdsfGTEFR-----YRQ 548
Cdd:cd02009 60 ALGIALATDK-PTVLLTGDLSF--LHdlnGLLLGK-QEPLNLTIVVINN--NG--------------GGIFSllpqaSFE 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 549 PETGQLQGGLVPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKV 603
Cdd:cd02009 120 DEFERLFGTPQGLDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
31-507 |
3.39e-08 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 56.46 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 31 VKGIFAIFGHGnVLGLGQALEQDSGDMRVYQGRNEQGMAHAATGFARqaLRRQIIACTSSIGPGAANMITAAGTASANRI 110
Cdd:PRK08273 18 VRRVFGYPGDG-INGLLGALGRADDKPEFVQARHEEMAAFMAVAHAK--FTGEVGVCLATSGPGAIHLLNGLYDAKLDHV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 111 PLLLLPGdvfatrqpdpvlQQ----IEQSYDLSISTNDAFRAV-SKYWDRITRPEQLMSACINAMRVLTdpAETGAVTLC 185
Cdd:PRK08273 95 PVVAIVG------------QQaraaLGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTAL--AERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 186 LPQDVQGEAWDYPESFF-----------ARRVHRLD--RRPAsaaqladavAAIKASRKPLIVCGGGVKysGAGEALSRF 252
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHgtvhsgvgytrPRVVPYDEdlRRAA---------EVLNAGRKVAILVGAGAL--GATDEVIAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 253 AERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEAD--LVIGVGTRFSDFTtaskwifqhPE---VRFLNI 327
Cdd:PRK08273 230 AERLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDtlLMVGSSFPYSEFL---------PKegqARGVQI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 328 NvsnfdawkLDG----------IAMLADAREAMTALDAALA---DSGWQAgwgaQIEsvqsRQLKETQRVYQAVWQEKSf 394
Cdd:PRK08273 301 D--------IDGrmlglrypmeVNLVGDAAETLRALLPLLErkkDRSWRE----RIE----KWVARWWETLEARAMVPA- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 395 vpeidDHLDRESVYREfrqitdstltqssvlgvLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEV 474
Cdd:PRK08273 364 -----DPVNPQRVFWE-----------------LSPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAV 421
|
490 500 510
....*....|....*....|....*....|....
gi 1757862790 475 NAALGVKLAQPQSEVYSLVGDGSFMMLH-SELVT 507
Cdd:PRK08273 422 PYAIAAKFAHPDRPVIALVGDGAMQMNGmAELIT 455
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
419-600 |
1.57e-07 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 54.47 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 419 LTQSSVLGVLNETLPAEAVIV------------AAAGSLPGD-LQrvwrnraeNTyhveyGYScMGYEVNAALGVKLAQP 485
Cdd:PRK07586 337 LTPEAIAQVIAALLPENAIVVdesitsgrgffpATAGAAPHDwLT--------LT-----GGA-IGQGLPLATGAAVACP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 486 QSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFdnmANGCINNLQMEhgMDSFGTEfryrqpETGQLQGGLV-----P 560
Cdd:PRK07586 403 DRKVLALQGDGSAMYTIQALWTQARENLDVTTVIF---ANRAYAILRGE--LARVGAG------NPGPRALDMLdlddpD 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1757862790 561 VDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLID 600
Cdd:PRK07586 472 LDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIE 511
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
49-590 |
2.82e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 53.34 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 49 ALEQDSGdMRVYQGRNEQGMAHAATGFARQALRRQiiACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPdpv 128
Cdd:PRK12474 37 ALDRVPR-MRPVLCLFEGVVTGAADGYGRIAGKPA--VTLLHLGPGLANGLANLHNARRAASPIVNIVGDHAVEHLQ--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 129 lqqieqsYDLSISTN-DAF-RAVSKYWDRITRPEQLMSACINAMRVlTDPAETGAVTLCLPQDVqgeAWDyPESFFARRV 206
Cdd:PRK12474 111 -------YDAPLTSDiDGFaRPVSRWVHRSASAGAVDSDVARAVQA-AQSAPGGIATLIMPADV---AWN-EAAYAAQPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 207 HRLDRRPASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALSRFAERYGVP-FAETQAGKG------TVVSSHPLNVG 279
Cdd:PRK12474 179 RGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRlYCDTFAPRIergagrVPIERIPYFHE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 280 GVGEtgclaanlLAKEADLVIGVGTRfsdfttaskwifqhPEVRFLninvsnfdawkldgiamladareamtaldaalAD 359
Cdd:PRK12474 259 QITA--------FLKDVEQLVLVGAK--------------PPVSFF--------------------------------AY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 360 SGwQAGWGAQIESVQSRQLKETQRVYQAVwqeksfvPEIDDHLD--RESVYREFRQITD---STLTQSSVLGVLNETLPA 434
Cdd:PRK12474 285 PG-KPSWGAPPGCEIVYLAQPDEDLAQAL-------QDLADAVDapAEPAARTPLALPAlpkGALNSLGVAQLIAHRTPD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 435 EAVIV--AAAGSLPGDLQRvwrNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQER 512
Cdd:PRK12474 357 QAIYAdeALTSGLFFDMSY---DRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMAREN 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 513 AKINVVLFDNMANGCINNLQMEHGMDSFGTE----FRYRQPEtgqlqgglvpVDFATIAAGYGCKTWRVTTLDELRHALD 588
Cdd:PRK12474 434 LDVTVVIFANRSYAILNGELQRVGAQGAGRNalsmLDLHNPE----------LNWMKIAEGLGVEASRATTAEEFSAQYA 503
|
..
gi 1757862790 589 AA 590
Cdd:PRK12474 504 AA 505
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
44-188 |
4.86e-07 |
|
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: 49.65 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 44 LGLGQALEQDSgDMRVYQGRNEQGMAHAATGFARQALRrqiIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATR 123
Cdd:cd06586 24 SSLLDALREGD-KRIIDTVIHELGAAGAAAGYARAGGP---PVVIVTSGTGLLNAINGLADAAAEHLPVVFLIGARGISA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757862790 124 QpdpVLQQIEQSYDLSIstndaFRAVSKYWDRITRPEQLMSACINAMRvlTDPAETGAVTLCLPQ 188
Cdd:cd06586 100 Q---AKQTFQSMFDLGM-----YRSIPEANISSPSPAELPAGIDHAIR--TAYASQGPVVVRLPR 154
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
469-599 |
1.65e-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: 45.73 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 469 CMGYEVNAALGVKLAQPQSEVYSLVGDGSFmmLHS---ELVTSLQERAKINVVLFDNMANGcinnlqMEHGMDSFGTEFR 545
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTF--FHSgilGLINAVYNKANITVVILDNRTTA------MTGGQPHPGTGKT 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1757862790 546 YRQPETgqlqgglvPVDFATIAAGYGCKTWRVTT---LDELRHAL-DAARRETVSTLI 599
Cdd:cd02008 124 LTEPTT--------VIDIEALVRAIGVKRVVVVDpydLKAIREELkEALAVPGVSVII 173
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
432-522 |
4.79e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.82 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 432 LPAEAVIVAAAGSLPGDLqrvWR--NRAENTYHVeygySCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSL 509
Cdd:PRK06163 26 LKDEEAVIGGIGNTNFDL---WAagQRPQNFYML----GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIA 98
|
90
....*....|....
gi 1757862790 510 QERAK-INVVLFDN 522
Cdd:PRK06163 99 ALAPKnLTIIVMDN 112
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
435-606 |
5.04e-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: 44.20 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 435 EAVIVAAAGSLPGDLQRVwRNRAENTYHV-EYGYSCMgyevnAALGVKLAQPQsEVYSLVGDGSFMMLHSELVTSLQERA 513
Cdd:cd03372 14 DELVVSNIGFPSKELYAA-GDRPLNFYMLgSMGLASS-----IGLGLALAQPR-KVIVIDGDGSLLMNLGALATIAAEKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 514 K-INVVLFDNMANGcinnlqmehgmdsfgtefryrqpETG-QLQGGLVPVDFATIAAGYGCK-TWRVTTLDELRHALDAA 590
Cdd:cd03372 87 KnLIIVVLDNGAYG-----------------------STGnQPTHAGKKTDLEAVAKACGLDnVATVASEEAFEKAVEQA 143
|
170
....*....|....*.
gi 1757862790 591 RRETVstLIDIKVLPK 606
Cdd:cd03372 144 LDGPS--FIHVKIKPG 157
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
231-522 |
4.47e-04 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 43.15 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 231 KPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVG---GVGETGCLAAnlLAKEADLVIGVGTRFS 307
Cdd:PLN02573 226 KPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGtywGAVSTPFCAE--IVESADAYLFAGPIFN 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 308 DFTTA--------SKWIFQHPEvrflNINVSNFDAWkldGIAMLADAREAMtaldaaladsgwqagwgaqiesvqSRQLK 379
Cdd:PLN02573 304 DYSSVgyslllkkEKAIIVQPD----RVTIGNGPAF---GCVLMKDFLEAL------------------------AKRVK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 380 ETQRVYQAVwqEKSFVPEiddhldresvYREFRQITDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVwRNRAEN 459
Cdd:PLN02573 353 KNTTAYENY--KRIFVPE----------GEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFNCQKL-KLPEGC 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1757862790 460 TYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDN 522
Cdd:PLN02573 420 GYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
424-605 |
2.57e-03 |
|
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: 39.01 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 424 VLGVLNETLpAEAVIVAAAGSLPGDLQRVwRNRAENTYHVeygySCMGYEVNAALGVKLAQPQsEVYSLVGDGSFMMLHS 503
Cdd:cd02001 4 AIAEIIEAS-GDTPIVSTTGYASRELYDV-QDRDGHFYML----GSMGLAGSIGLGLALGLSR-KVIVVDGDGSLLMNPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757862790 504 ELVTSLQERAK--INVVLfDNMANGcinnlqmehgmdsfgtefryrqpETGQLQGGLVPVDFATIAAGYGCKTWRVTTLD 581
Cdd:cd02001 77 VLLTAGEFTPLnlILVVL-DNRAYG-----------------------STGGQPTPSSNVNLEAWAAACGYLVLSAPLLG 132
|
170 180
....*....|....*....|....
gi 1757862790 582 ELRHALDAARRETVSTLIDIKVLP 605
Cdd:cd02001 133 GLGSEFAGLLATTGPTLLHAPIAP 156
|
|
| |
