|
Name |
Accession |
Description |
Interval |
E-value |
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
1-574 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 788.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 1 MTVNPITHYIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGT 80
Cdd:COG1165 1 SDKNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 81 AAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQMLRYIRTLASRAAGEAQ 160
Cdd:COG1165 81 AAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDALRYLRRTINRALAAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 161 KRPMGPVHVNVPLREPLMPDLSDEPFGRmRTGRHVSVKTGTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDA-DKENII 239
Cdd:COG1165 161 GPPPGPVHINVPFREPLYPDPDEEDPLA-AGGPWIRVTPPEPAPSPEALAQLADELERAKRGLIVAGPLPPPEeLAEALA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 240 ALSKALQYPILADPLSNLRNGvhdksTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDDPAIQQIVIDED 319
Cdd:COG1165 240 ALAEALGWPVLADPLSNLRHP-----NVISTYDLLLRNPEFAELLQPDLVIRFGGPPVSKRLKQFLRRHPPAEHWVVDPS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 320 GGWRDPTQASAHMIHCNASVFAEEIMGGLTAAarSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSS 399
Cdd:COG1165 315 GEWRDPFHSLTRVIEADPEAFLEALAERLPPA--DSAWLARWLAAEQKARAAIDEYLAEDPLSEGAVARRLLEALPEGST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 400 LFVGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTV 479
Cdd:COG1165 393 LFVGNSMPVRDLDLFARPLPKGVRVYANRGASGIDGTVSTALGAALASGKPTVLLTGDLSFLHDLNGLLLLYELPPNLTI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 480 ILVNNDGGGIFSFLPQASEKTHFEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAPQADKPGLHLIEIKTDRQSR 559
Cdd:COG1165 473 VVVNNDGGGIFSMLPGAKFEPEFERFFGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREEN 552
|
570
....*....|....*
gi 2036878232 560 VQLHRDMLNEAVREV 574
Cdd:COG1165 553 AELLKALFAAVAAAL 567
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
9-446 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695). 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 272941 [Multi-domain] Cd Length: 432 Bit Score: 621.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 9 YIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPA 88
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 89 VVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQmLRYIRTLASRAAGEAQKRPMGPVH 168
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEP-LAYLRSTVDRALAQAQGAPPGPVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 169 VNVPLREPLMPDLSDEPFGRMRTGRHVSVKTGTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKENIIALSKALQYP 248
Cdd:TIGR00173 160 INVPFREPLYPDPLLQPLQPWLRSGVPTISTGPPVLDPESLQELWDRLRQAKRGLIIAGPLAGAEDAEALAALAEALGWP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 249 ILADPLSNLRNGVHDksTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDDPaIQQIVIDEDGGWRDPTQA 328
Cdd:TIGR00173 240 LLADPLSGLRGGPHP--LVIDHYDLLLANAELREELQPDLVIRFGGPPVSKRLRQWLARAP-AEYWVVDPRPGWLDPFHH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 329 SAHMIHCNASVFAEEIMGGLtaAARSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSSLFVGNSMPI 408
Cdd:TIGR00173 317 ATTRLEASPAAFAEALAGLL--KNPAAAWLDRWLEAEAKARAALREVLAEEPLSELSLARALSQLLPDGSALFVGNSMPI 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 2036878232 409 RDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEG 446
Cdd:TIGR00173 395 RDLDTFSSPPDKPIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
14-496 |
3.24e-92 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 310.64 E-value: 3.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 14 IDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAH 93
Cdd:PLN02980 308 IEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEAS 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 94 YSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDsaLPEESPQM-LRYIRTLASRAAGEAQKRPMGPVHVNVP 172
Cdd:PLN02980 388 QDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFN--LPPPTDLIpARMVLTTLDSAVHWATSSPCGPVHINCP 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 173 LREPL--MPD--------------LSDEPFGRMRTGRHVSvktgTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKE 236
Cdd:PLN02980 466 FREPLdgSPTnwmssclkgldmwmSNAEPFTKYIQMQSSK----ADGDTTGQITEVLEVIQEAKRGLLLIGAIHTEDDIW 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 237 NIIALSKALQYPILADPLSNLR--------NGVHDKSTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDD 308
Cdd:PLN02980 542 AALLLAKHLMWPVVADILSGLRlrklfksfPEFELNILFVDHLDHALLSDSVRNWIQFDVVIQIGSRITSKRVSQMLEKC 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 309 PAIQQIVIDEDGGWRDPTQASAHMIHCNASVFAEEIMGGlTAAARSSEWLEKWQFVNGRF-REHLQTISSEDVSFEGNLY 387
Cdd:PLN02980 622 FPFSYILVDKHPCRHDPSHLVTHRVQSNIVQFADCLLKA-QFPRRRSKWHGHLQALDGMVaQEISFQIHAESSLTEPYVA 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 388 RILQHLVPENSSLFVGNSMPIRDVDTF-----------------FEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAP 450
Cdd:PLN02980 701 HVISEALTSDSALFIGNSMAIRDADMYgcssenyssrivdmmlsAELPCQWIQVAGNRGASGIDGLLSTAIGFAVGCNKR 780
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2036878232 451 VTLVIGDLSFYHDLNGL--LAAKKLGIPLTVILVNNDGGGIFSFLPQA 496
Cdd:PLN02980 781 VLCVVGDISFLHDTNGLsiLSQRIARKPMTILVINNHGGAIFSLLPIA 828
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
381-555 |
1.15e-89 |
|
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: 274.09 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 381 SFEGNLYRILQHLVPENSSLFVGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPVTLVIGDLSF 460
Cdd:cd02009 1 LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFALPSDKTVRVFANRGASGIDGTLSTALGIALATDKPTVLLTGDLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 461 YHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQASEKTHFEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAP 540
Cdd:cd02009 81 LHDLNGLLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEDEFERLFGTPQGLDFEHLAKAYGLEYRRVSSLDELEQALES 160
|
170
....*....|....*
gi 2036878232 541 QADKPGLHLIEIKTD 555
Cdd:cd02009 161 ALAQDGPHVIEVKTD 175
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
21-179 |
2.82e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 119.26 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 21 GITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPII 100
Cdd:pfam02776 13 GVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 101 VLTADRPHELREVGAPQA-INQHFLFGNFVKFFTDSALPEESPQMLRyirtlasRAAGEAQKRPMGPVHVNVPLREPLMP 179
Cdd:pfam02776 93 VISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLR-------RAFRAALSGRPGPVYLEIPLDVLLEE 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
1-574 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 788.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 1 MTVNPITHYIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGT 80
Cdd:COG1165 1 SDKNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 81 AAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQMLRYIRTLASRAAGEAQ 160
Cdd:COG1165 81 AAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDALRYLRRTINRALAAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 161 KRPMGPVHVNVPLREPLMPDLSDEPFGRmRTGRHVSVKTGTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDA-DKENII 239
Cdd:COG1165 161 GPPPGPVHINVPFREPLYPDPDEEDPLA-AGGPWIRVTPPEPAPSPEALAQLADELERAKRGLIVAGPLPPPEeLAEALA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 240 ALSKALQYPILADPLSNLRNGvhdksTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDDPAIQQIVIDED 319
Cdd:COG1165 240 ALAEALGWPVLADPLSNLRHP-----NVISTYDLLLRNPEFAELLQPDLVIRFGGPPVSKRLKQFLRRHPPAEHWVVDPS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 320 GGWRDPTQASAHMIHCNASVFAEEIMGGLTAAarSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSS 399
Cdd:COG1165 315 GEWRDPFHSLTRVIEADPEAFLEALAERLPPA--DSAWLARWLAAEQKARAAIDEYLAEDPLSEGAVARRLLEALPEGST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 400 LFVGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTV 479
Cdd:COG1165 393 LFVGNSMPVRDLDLFARPLPKGVRVYANRGASGIDGTVSTALGAALASGKPTVLLTGDLSFLHDLNGLLLLYELPPNLTI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 480 ILVNNDGGGIFSFLPQASEKTHFEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAPQADKPGLHLIEIKTDRQSR 559
Cdd:COG1165 473 VVVNNDGGGIFSMLPGAKFEPEFERFFGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREEN 552
|
570
....*....|....*
gi 2036878232 560 VQLHRDMLNEAVREV 574
Cdd:COG1165 553 AELLKALFAAVAAAL 567
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
9-446 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695). 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 272941 [Multi-domain] Cd Length: 432 Bit Score: 621.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 9 YIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPA 88
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 89 VVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQmLRYIRTLASRAAGEAQKRPMGPVH 168
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEP-LAYLRSTVDRALAQAQGAPPGPVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 169 VNVPLREPLMPDLSDEPFGRMRTGRHVSVKTGTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKENIIALSKALQYP 248
Cdd:TIGR00173 160 INVPFREPLYPDPLLQPLQPWLRSGVPTISTGPPVLDPESLQELWDRLRQAKRGLIIAGPLAGAEDAEALAALAEALGWP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 249 ILADPLSNLRNGVHDksTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDDPaIQQIVIDEDGGWRDPTQA 328
Cdd:TIGR00173 240 LLADPLSGLRGGPHP--LVIDHYDLLLANAELREELQPDLVIRFGGPPVSKRLRQWLARAP-AEYWVVDPRPGWLDPFHH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 329 SAHMIHCNASVFAEEIMGGLtaAARSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSSLFVGNSMPI 408
Cdd:TIGR00173 317 ATTRLEASPAAFAEALAGLL--KNPAAAWLDRWLEAEAKARAALREVLAEEPLSELSLARALSQLLPDGSALFVGNSMPI 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 2036878232 409 RDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEG 446
Cdd:TIGR00173 395 RDLDTFSSPPDKPIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
14-496 |
3.24e-92 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 310.64 E-value: 3.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 14 IDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAH 93
Cdd:PLN02980 308 IEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEAS 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 94 YSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDsaLPEESPQM-LRYIRTLASRAAGEAQKRPMGPVHVNVP 172
Cdd:PLN02980 388 QDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFN--LPPPTDLIpARMVLTTLDSAVHWATSSPCGPVHINCP 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 173 LREPL--MPD--------------LSDEPFGRMRTGRHVSvktgTQSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKE 236
Cdd:PLN02980 466 FREPLdgSPTnwmssclkgldmwmSNAEPFTKYIQMQSSK----ADGDTTGQITEVLEVIQEAKRGLLLIGAIHTEDDIW 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 237 NIIALSKALQYPILADPLSNLR--------NGVHDKSTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPVFLWLKDD 308
Cdd:PLN02980 542 AALLLAKHLMWPVVADILSGLRlrklfksfPEFELNILFVDHLDHALLSDSVRNWIQFDVVIQIGSRITSKRVSQMLEKC 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 309 PAIQQIVIDEDGGWRDPTQASAHMIHCNASVFAEEIMGGlTAAARSSEWLEKWQFVNGRF-REHLQTISSEDVSFEGNLY 387
Cdd:PLN02980 622 FPFSYILVDKHPCRHDPSHLVTHRVQSNIVQFADCLLKA-QFPRRRSKWHGHLQALDGMVaQEISFQIHAESSLTEPYVA 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 388 RILQHLVPENSSLFVGNSMPIRDVDTF-----------------FEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAP 450
Cdd:PLN02980 701 HVISEALTSDSALFIGNSMAIRDADMYgcssenyssrivdmmlsAELPCQWIQVAGNRGASGIDGLLSTAIGFAVGCNKR 780
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2036878232 451 VTLVIGDLSFYHDLNGL--LAAKKLGIPLTVILVNNDGGGIFSFLPQA 496
Cdd:PLN02980 781 VLCVVGDISFLHDTNGLsiLSQRIARKPMTILVINNHGGAIFSLLPIA 828
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
381-555 |
1.15e-89 |
|
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: 274.09 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 381 SFEGNLYRILQHLVPENSSLFVGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPVTLVIGDLSF 460
Cdd:cd02009 1 LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFALPSDKTVRVFANRGASGIDGTLSTALGIALATDKPTVLLTGDLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 461 YHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQASEKTHFEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAP 540
Cdd:cd02009 81 LHDLNGLLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEDEFERLFGTPQGLDFEHLAKAYGLEYRRVSSLDELEQALES 160
|
170
....*....|....*
gi 2036878232 541 QADKPGLHLIEIKTD 555
Cdd:cd02009 161 ALAQDGPHVIEVKTD 175
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
13-173 |
2.65e-88 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 270.14 E-value: 2.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 13 FIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEA 92
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 93 HYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPqMLRYIRTLASRAAGEAQKRPMGPVHVNVP 172
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDD-DLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
.
gi 2036878232 173 L 173
Cdd:cd07037 162 F 162
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
21-179 |
2.82e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 119.26 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 21 GITDAVVCPGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPII 100
Cdd:pfam02776 13 GVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 101 VLTADRPHELREVGAPQA-INQHFLFGNFVKFFTDSALPEESPQMLRyirtlasRAAGEAQKRPMGPVHVNVPLREPLMP 179
Cdd:pfam02776 93 VISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLR-------RAFRAALSGRPGPVYLEIPLDVLLEE 165
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
54-557 |
2.36e-30 |
|
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: 125.27 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFft 133
Cdd:COG0028 50 EQGAAFMADGYARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKW-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 134 dSALPEESPQMLRYIRtlasRAAGEAQKRPMGPVHVNVPLreplmpDLSDEPFGRMRTGRHVSVKTGTQSVDRESLSDVA 213
Cdd:COG0028 128 -SYLVTDPEDLPEVLR----RAFRIATSGRPGPVVLDIPK------DVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 214 EMLAEAEKGMIVCGE--LHSDADKEnIIALSKALQYPILA-----------DPLSNLRNGVHDKSTVIDAYDsflkddel 280
Cdd:COG0028 197 ELLAAAKRPVILAGGgaRRAGAAEE-LRALAERLGAPVVTtlmgkgafpedHPLYLGMLGMHGTPAANEALA-------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 281 krklRPDVVI----RFGPMPVSKPVfLWLKDDPAIQqivIDEDGGWRDPTQASAHMIHCNASVFAEEIMGGLTAAARS-S 355
Cdd:COG0028 268 ----EADLVLavgaRFDDRVTGNWD-EFAPDAKIIH---IDIDPAEIGKNYPVDLPIVGDAKAVLAALLEALEPRADDrA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 356 EWLEKWQFVNGRFREHLQTiSSEDVSFEgNLYRILQHLVPENSSLFVGNSMPIRDVDTFFeKQDRPFRIYSNRGANGIdG 435
Cdd:COG0028 340 AWLARIAAWRAEYLAAYAA-DDGPIKPQ-RVIAALREALPDDAIVVTDVGQHQMWAARYL-RFRRPRRFLTSGGLGTM-G 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 436 V-VSSAMGVCEG-TKAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNdggGIFSFLPQASEKTHFEDLFGT-PTGL 512
Cdd:COG0028 416 YgLPAAIGAKLArPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNN---GGLGMVRQWQELFYGGRYSGTdLPNP 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2036878232 513 DFKHAAALYGGTYSCPASWDEFKTAYApQA-DKPGLHLIEIKTDRQ 557
Cdd:COG0028 493 DFAKLAEAFGAKGERVETPEELEAALE-EAlASDGPALIDVRVDPE 537
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
13-172 |
1.06e-18 |
|
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: 83.35 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 13 FIDEFALSGITDAVVCPGSRSTPLAVLCAaHPDISVHVQIDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEA 92
Cdd:cd07035 3 LVEALKAEGVDHVFGVPGGAILPLLDALA-RSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLANA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 93 HYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQMLRyirtlasRAAGEAQKRPMGPVHVNVP 172
Cdd:cd07035 82 YLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALR-------RAFRIALSGRPGPVALDLP 154
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
29-172 |
1.17e-14 |
|
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: 71.61 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 29 PGSRSTPLAVLCAAHPDISVHVQIDERSAGFFALGLAKAKQRPVLLIcTSGTAAANFYPAVVEAHYSRVPIIVLTADRPH 108
Cdd:cd06586 19 PGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIV-TSGTGLLNAINGLADAAAEHLPVVFLIGARGI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2036878232 109 ELREVGAPQAINQHFLFGNFVKFFTDSALPEESP-QMLRYIRTLasraageaqKRPMGPVHVNVP 172
Cdd:cd06586 98 SAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPaGIDHAIRTA---------YASQGPVVVRLP 153
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
386-554 |
7.18e-14 |
|
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: 69.59 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 386 LYRILQHLVPENSSLFVGNSMPIRDVDTFFEKQdRPFRIYSNRGANGIDGVVSSAMGVCEGTK-APVTLVIGDLSFYHDL 464
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLR-RGRRFLTSTGFGAMGYGLPAAIGAALAAPdRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 465 NGLLAAKKLGIPLTVILVNNDGGGIfsfLPQASEKTHFEDLFGT-PTGLDFKHAAALYGGTYSCPASWDEFKTAYAPQAD 543
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGT---IRMHQEAFYGGRVSGTdLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALA 157
|
170
....*....|.
gi 2036878232 544 KPGLHLIEIKT 554
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
54-556 |
4.82e-08 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 55.75 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRP-VLLICTsGTAAANFYPAVVEAHYSRVPIIVLTA-----------DRPHELRevgapqaiNQ 121
Cdd:PRK07524 48 EQGAGFMADGYARVSGKPgVCFIIT-GPGMTNIATAMGQAYADSIPMLVISSvnrraslgkgrGKLHELP--------DQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 122 HFLFGNfVKFFTDSAL-PEESPQMLRyiRTLASRAAGeaqkRPmGPVHVNVPLreplmpDLSDEPFGRMRTGRHVSVKTG 200
Cdd:PRK07524 119 RAMVAG-VAAFSHTLMsAEDLPEVLA--RAFAVFDSA----RP-RPVHIEIPL------DVLAAPADHLLPAPPTRPARP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 201 TQsvDRESLSDVAEMLAEAEKGMIVCGELHSDADKEnIIALSKALQYPILadpLSNLRNGV--HDKSTVIDAYDSFLKDD 278
Cdd:PRK07524 185 GP--APAALAQAAERLAAARRPLILAGGGALAAAAA-LRALAERLDAPVA---LTINAKGLlpAGHPLLLGASQSLPAVR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 279 ELKRKlrPDVVIRFG--------------PMPVSKpvflwlkddpAIQQIVIDEDGGWRDPTQASAhmIHCNASVFAEEI 344
Cdd:PRK07524 259 ALIAE--ADVVLAVGtelgetdydvyfdgGFPLPG----------ELIRIDIDPDQLARNYPPALA--LVGDARAALEAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 345 MGGLTAAARSSEW-LEKWQFVNGRFREhlqTISSEDVSFEGNLYRILQHLvPENssLFVGNS-MPIRDVDTFFEkQDRPF 422
Cdd:PRK07524 325 LARLPGQAAAADWgAARVAALRQALRA---EWDPLTAAQVALLDTILAAL-PDA--IFVGDStQPVYAGNLYFD-ADAPR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 423 RIYSNRGANGIDGV-VSSAMGVCEGT-KAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDG-GGIfsflpqaseK 499
Cdd:PRK07524 398 RWFNASTGYGTLGYgLPAAIGAALGApERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGyGEI---------R 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2036878232 500 THFEDLFGTPTGL-----DFKHAAALYGGTYSCPASWDEFKTAYAPQADKPGLHLIEIKTDR 556
Cdd:PRK07524 469 RYMVARDIEPVGVdpytpDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
54-249 |
6.21e-08 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 55.53 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFT 133
Cdd:PRK06276 47 EQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 134 DSALPEESPQMLRYIRTLASRAageaqkRPmGPVHVNVP-------LREPLMPDLSDEPFgrmrTGRHVSVKTGTQSVDR 206
Cdd:PRK06276 127 QIKKPEEIPEIFRAAFEIAKTG------RP-GPVHIDLPkdvqegeLDLEKYPIPAKIDL----PGYKPTTFGHPLQIKK 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2036878232 207 eslsdVAEMLAEAEKGMIVCGE--LHSDADKEnIIALSKALQYPI 249
Cdd:PRK06276 196 -----AAELIAEAERPVILAGGgvIISGASEE-LIELSELVKIPV 234
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
32-555 |
1.66e-07 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 54.00 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 32 RSTPLAVLCAAhPDISVHvQI---DERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPH 108
Cdd:PRK06112 35 QSLPSALFLAA-EAIGIR-QIayrTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 109 ELREVGAPQAINQHFLFGNFVKFFTDSALPEespQMLRYIrTLASRAAgeAQKRPmGPVHVNVPLreplmpDLSDEPfgR 188
Cdd:PRK06112 113 DQTDRNAFQELDHIALFQSCTKWVRRVTVAE---RIDDYV-DQAFTAA--TSGRP-GPVVLLLPA------DLLTAA--A 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 189 MRTGRHVSVKTGTQSVDR-----ESLSDVAEMLAEAEKGMIVCGE-LHSDADKENIIALSKALQYPILAdplSNLRNGVH 262
Cdd:PRK06112 178 AAPAAPRSNSLGHFPLDRtvpapQRLAEAASLLAQAQRPVVVAGGgVHISGASAALAALQSLAGLPVAT---TNMGKGAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 263 DKSTVIDA--YDSFLKDDELKRKLR-----PDVVIRFGPMPVSKPVFLWLKDDPAIQQIVIDEDGGWRDPTQASAHMIHC 335
Cdd:PRK06112 255 DETHPLSLgvVGSLMGPRSPGRHLRdlvreADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYEALRLVGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 336 NASVFAE--EIMG--GLTAAARSSEWLEKwQFVNGR--FREHLQTISSEDVSfEGNLYRI---LQHLVPEN--------- 397
Cdd:PRK06112 335 ARLTLAAltDALRgrDLAARAGRRAALEP-AIAAGReaHREDSAPVALSDAS-PIRPERImaeLQAVLTGDtivvadasy 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 398 SSLFVGNSMPIRDVDTffekqdrpfRIYSNRGANGIDGVVSSAMGV-CEGTKAPVTLVIGDLSFYHDLNGLLAAKKLGIP 476
Cdd:PRK06112 413 SSIWVANFLTARRAGM---------RFLTPRGLAGLGWGVPMAIGAkVARPGAPVICLVGDGGFAHVWAELETARRMGVP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 477 LTVILVNNdggGIFSFLPQASEKthfedLFGTPTGL-DFK---HAA-ALYGGtysCPA----SWDEFKTAYAPQADKPGL 547
Cdd:PRK06112 484 VTIVVLNN---GILGFQKHAETV-----KFGTHTDAcHFAavdHAAiARACG---CDGvrveDPAELAQALAAAMAAPGP 552
|
....*...
gi 2036878232 548 HLIEIKTD 555
Cdd:PRK06112 553 TLIEVITD 560
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
54-249 |
1.21e-06 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 51.54 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFft 133
Cdd:PRK07525 52 EQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKY-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 134 dsalPEESPQ---MLRYIRTLASRAageaqKRPMGPVHVNVPlREPLMPDLSDEPFGRMRTGRhvsvktgtQSVDRESLS 210
Cdd:PRK07525 130 ----QEEVRDpsrMAEVLNRVFDKA-----KRESGPAQINIP-RDYFYGVIDVEIPQPVRLER--------GAGGEQSLA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2036878232 211 DVAEMLAEAEKGMIVCGELHSDAD-KENIIALSKALQYPI 249
Cdd:PRK07525 192 EAAELLSEAKFPVILSGAGVVLSDaIEECKALAERLDAPV 231
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
61-226 |
1.53e-06 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 51.15 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 61 ALGLAKAKQRP--VLLICTSGTAaaNFYPAVVEAHYSRVPIIVLTADRPH-ELREVGA-------PQ-AINQHFLFGNFV 129
Cdd:PRK08327 66 AHGYALVTGKPqaVMVHVDVGTA--NALGGVHNAARSRIPVLVFAGRSPYtEEGELGSrntrihwTQeMRDQGGLVREYV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 130 KFFTDSALPEESPQMLRyirtlasRAAGEAQKRPMGPVHVNVPlREPLMpdlsdEPFGR--MRTGRHVSVKTGtqSVDRE 207
Cdd:PRK08327 144 KWDYEIRRGDQIGEVVA-------RAIQIAMSEPKGPVYLTLP-REVLA-----EEVPEvkADAGRQMAPAPP--APDPE 208
|
170
....*....|....*....
gi 2036878232 208 SLSDVAEMLAEAEKGMIVC 226
Cdd:PRK08327 209 DIARAAEMLAAAERPVIIT 227
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
54-233 |
1.64e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 50.86 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHEL------REV---GAPQAINQH-F 123
Cdd:PRK08155 60 EQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMigtdafQEVdtyGISIPITKHnY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 124 LFGNfvkfftdsalPEESPQMLRYirtlASRAAgeAQKRPmGPVHVNVP------------LREPLMPDLSDEPfgrmrt 191
Cdd:PRK08155 140 LVRD----------IEELPQVISD----AFRIA--QSGRP-GPVWIDIPkdvqtavieleaLPAPAEKDAAPAF------ 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2036878232 192 grhvsvktgtqsvDRESLSDVAEMLAEAEKGMIVCGE--LHSDA 233
Cdd:PRK08155 197 -------------DEESIRDAAAMINAAKRPVLYLGGgvINSGA 227
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
54-172 |
7.13e-06 |
|
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: 46.39 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHELREVGAPQAINQHFLFGNFVKFFT 133
Cdd:cd07039 47 EEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNE 126
|
90 100 110
....*....|....*....|....*....|....*....
gi 2036878232 134 DSALPEESPQMLryirTLASRAAgeAQKRpmGPVHVNVP 172
Cdd:cd07039 127 TVTSPEQLPELL----DRAIRTA--IAKR--GVAVLILP 157
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
437-552 |
1.45e-05 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 45.27 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 437 VSSAMGVC-EGTKAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQAS-EKTHFEDLFGTPTGLDF 514
Cdd:pfam02775 34 LPAAIGAKlARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGYGMTRGQQTPFgGGRYSGPSGKILPPVDF 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 2036878232 515 -KHAAAlYGGTYSCPASWDEFKTAYAPQADKPGLHLIEI 552
Cdd:pfam02775 114 aKLAEA-YGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-555 |
8.34e-05 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 45.33 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 78 SGTAAANFYpavvEAHYSRVPIIVlTADRphELREVGAPQAinqhFLFGN--------FVKFFTDSALPEESPQMLryir 149
Cdd:PRK07092 85 VGNAMGNLF----TAFKNHTPLVI-TAGQ--QARSILPFEP----FLAAVqaaelpkpYVKWSIEPARAEDVPAAI---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 150 tlaSRAAGEAQKRPMGPVHVNVPLreplmpDLSDEPFGRMRTgRHVSVKTGtqsVDRESLSDVAEMLAEAEKGMIVCG-E 228
Cdd:PRK07092 150 ---ARAYHIAMQPPRGPVFVSIPY------DDWDQPAEPLPA-RTVSSAVR---PDPAALARLGDALDAARRPALVVGpA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 229 LHSDADKENIIALSKALQYPILADPLSnlrngvhdkstvidAYDSFLKDDELKRKLRP-------------DVVIRFGpm 295
Cdd:PRK07092 217 VDRAGAWDDAVRLAERHRAPVWVAPMS--------------GRCSFPEDHPLFAGFLPasrekisalldghDLVLVIG-- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 296 pvsKPVFLWLKDDPA--------IQQIVIDEDGGWRDPTQASahmIHCNASVFAEEIMGGLTAAARSSEwlekwqfvNGR 367
Cdd:PRK07092 281 ---APVFTYHVEGPGphlpegaeLVQLTDDPGEAAWAPMGDA---IVGDIRLALRDLLALLPPSARPAP--------PAR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 368 FREHLQTISSEDVSFEgNLYRILQHLVPENsSLFVGNS----------MPIRDVDTFFekqdrpfriysNRGANGIDGVV 437
Cdd:PRK07092 347 PMPPPAPAPGEPLSVA-FVLQTLAALRPAD-AIVVEEApstrpamqehLPMRRQGSFY-----------TMASGGLGYGL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 438 SSAMGVCEGT-KAPVTLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDG-GGIFSFlpqaSEKTHFEDLFGT--PtGLD 513
Cdd:PRK07092 414 PAAVGVALAQpGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRyGALRWF----APVFGVRDVPGLdlP-GLD 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2036878232 514 FKHAAALYGgtysCPA----SWDEFKTAY--APQADKPglHLIEIKTD 555
Cdd:PRK07092 489 FVALARGYG----CEAvrvsDAAELADALarALAADGP--VLVEVEVA 530
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
450-561 |
1.84e-03 |
|
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: 39.98 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 450 PVTLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQASEKTHFEDLF-------GTPTG----LDF-KHA 517
Cdd:cd02003 68 EVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFrdrdqesGQLDGallpVDFaANA 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2036878232 518 AALYGGTYSCpASWDEFKTAYAPQADKPGLHLIEIKTDRQSRVQ 561
Cdd:cd02003 148 RSLGARVEKV-KTIEELKAALAKAKASDRTTVIVIKTDPKSMTP 190
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
54-227 |
5.85e-03 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 39.48 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 54 ERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIVLTADRPHEL------REV---GAPQAINQHfl 124
Cdd:PRK08978 47 EQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLigtdafQEIdvlGLSLACTKH-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036878232 125 fgnfvKFFTDSalPEESPQMLRYIRTLAsrAAGeaqkRPmGPVHVNVPlREPLMPDLSDEPfgrmrtgrHVSVKTGTQSV 204
Cdd:PRK08978 125 -----SFLVQS--LEELPEIMAEAFEIA--SSG----RP-GPVLVDIP-KDIQLAEGELEP--------HLTTVENEPAF 181
|
170 180
....*....|....*....|...
gi 2036878232 205 DRESLSDVAEMLAEAEKGMIVCG 227
Cdd:PRK08978 182 PAAELEQARALLAQAKKPVLYVG 204
|
|
| |
