|
Name |
Accession |
Description |
Interval |
E-value |
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
2-556 |
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: 691.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 2 SVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGT 81
Cdd:COG1165 1 SDKNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 82 AVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPA-RWLVSTIDHALGTL- 159
Cdd:COG1165 81 AAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDAlRYLRRTINRALAAAl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 160 --HAGGVHINCPFAEPLYGEMDDTglswqqrlgDWWQDDKPWLR-----EAPRLESEKQRDWFFWRQKRGVVVAGRMSAE 232
Cdd:COG1165 161 gpPPGPVHINVPFREPLYPDPDEE---------DPLAAGGPWIRvtppePAPSPEALAQLADELERAKRGLIVAGPLPPP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 233 E--GKKVALWAQTLGWPLIGDVLSQT--GQPLPCADLWLGNAKATSELqQAQIVVQLGSSLTGKRLLQWQASCEPEEYWI 308
Cdd:COG1165 232 EelAEALAALAEALGWPVLADPLSNLrhPNVISTYDLLLRNPEFAELL-QPDLVIRFGGPPVSKRLKQFLRRHPPAEHWV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 309 VDDIEGRLDPAHHRGRRLIANIADWLELHPAE---KRQPWCvEIPRLAEQAMQAVIARR---DAFGEAQLAHRICDYLPE 382
Cdd:COG1165 311 VDPSGEWRDPFHSLTRVIEADPEAFLEALAERlppADSAWL-ARWLAAEQKARAAIDEYlaeDPLSEGAVARRLLEALPE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 383 QGQLFVGNSLVVRLIDALSQ-LPAGYPVYSNKGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAP 461
Cdd:COG1165 390 GSTLFVGNSMPVRDLDLFARpLPKGVRVYANRGASGIDGTVSTALGAALASGKPTVLLTGDLSFLHDLNGLLLLYELPPN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 462 LVLIVVNNNGGQIFSLLPTPQSE--RERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVND 539
Cdd:COG1165 470 LTIVVVNNDGGGIFSMLPGAKFEpeFERFFGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDR 549
|
570
....*....|....*..
5Z2P_B 540 TDGAQTLQQLLAQVSHL 556
Cdd:COG1165 550 EENAELLKALFAAVAAA 566
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
10-431 |
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: 521.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 10 WAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPA 89
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 90 LIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTL---HAGGVHI 166
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEPLAYLRSTVDRALAQAqgaPPGPVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 167 NCPFAEPLYGEmddtglSWQQRLGDWWQDDKPWL-REAPRLESEK-QRDWFFWRQ-KRGVVVAGRMS-AEEGKKVALWAQ 242
Cdd:TIGR00173 161 NVPFREPLYPD------PLLQPLQPWLRSGVPTIsTGPPVLDPESlQELWDRLRQaKRGLIIAGPLAgAEDAEALAALAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 243 TLGWPLIGDVLSQTGQP-----LPCADLWLGNAKATSELqQAQIVVQLGSSLTGKRLLQWQAScEPEEYWIVDDIEGRLD 317
Cdd:TIGR00173 235 ALGWPLLADPLSGLRGGphplvIDHYDLLLANAELREEL-QPDLVIRFGGPPVSKRLRQWLAR-APAEYWVVDPRPGWLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 318 PAHHRGRRLIANIADWLELHPAEKRQPW------CVEIPRLAEQAMQAVIARRDAFgEAQLAHRICDYLPEQGQLFVGNS 391
Cdd:TIGR00173 313 PFHHATTRLEASPAAFAEALAGLLKNPAaawldrWLEAEAKARAALREVLAEEPLS-ELSLARALSQLLPDGSALFVGNS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
5Z2P_B 392 LVVRLIDALSQLPAG-YPVYSNKGASGIDGLLSTAAGVQRA 431
Cdd:TIGR00173 392 MPIRDLDTFSSPPDKpIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| TPP_enzyme_M_2 |
pfam16582 |
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine ... |
184-388 |
3.04e-114 |
|
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine pyrophosphate in sequences not captured by pfam00205. This enzyme is necessary for the first step of the biosynthesis of menaquinone, or vitamin K2, an important cofactor in electron transport in bacteria.
Pssm-ID: 435442 Cd Length: 207 Bit Score: 337.75 E-value: 3.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 184 SWQQRLGDWWQDDKPWLRE-APRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPC 262
Cdd:pfam16582 1 SWLAPLGDWLQQNKPWLRYqAQQLEVPTHDDWDFWRQKKGVIVAGRLSAEEGMQLAAWAQKLGWPLLTDVQSQTGQPLPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 263 ADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKR 342
Cdd:pfam16582 81 ADLWLANPTAREELAQADIVIQFGGRLTSKRLLQFLAACKPHEYWLVDPLPGRLDPAHHRGRRFVASVGEWLRAHPPLRQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
5Z2P_B 343 QPWCVEIPRLAEQAMQAVIAR-RDAFGEAQLAHRICDYLPEQGQLFV 388
Cdd:pfam16582 161 APWALELLALSEFLASFIEQQvGGEFGEAQLAHRIAALLPDQGQLFI 207
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
2-535 |
6.58e-94 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 314.49 E-value: 6.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 2 SVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGT 81
Cdd:PLN02980 295 DYANINAVWASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 82 AVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHAL--GTL 159
Cdd:PLN02980 375 AVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMVLTTLDSAVhwATS 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 160 HA-GGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREApRLESEKQRD----------WFFWRQKRGVVVAGR 228
Cdd:PLN02980 455 SPcGPVHINCPFREPLDGSPTNWMSSCLKGLDMWMSNAEPFTKYI-QMQSSKADGdttgqitevlEVIQEAKRGLLLIGA 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 229 MSAEEGK-KVALWAQTLGWPLIGDVLS-----QTGQPLPCAD---LWLGN------AKATSELQQAQIVVQLGSSLTGKR 293
Cdd:PLN02980 534 IHTEDDIwAALLLAKHLMWPVVADILSglrlrKLFKSFPEFElniLFVDHldhallSDSVRNWIQFDVVIQIGSRITSKR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 294 LLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLE-LHPAE---KRQPWCVEIP---RLAEQAMQAVIARRDA 366
Cdd:PLN02980 614 VSQMLEKCFPFSYILVDKHPCRHDPSHLVTHRVQSNIVQFADcLLKAQfprRRSKWHGHLQaldGMVAQEISFQIHAESS 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 367 FGEAQLAHRICDYLPEQGQLFVGNSLVVRLID----------------ALSQLP--AGYPVYSNKGASGIDGLLSTAAGV 428
Cdd:PLN02980 694 LTEPYVAHVISEALTSDSALFIGNSMAIRDADmygcssenyssrivdmMLSAELpcQWIQVAGNRGASGIDGLLSTAIGF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 429 QRASGKPTLAIVGDLSALYDLNALALLRQVSA--PLVLIVVNNNGGQIFSLLP----TPQSERERFYLMPQNVHFEHAAA 502
Cdd:PLN02980 774 AVGCNKRVLCVVGDISFLHDTNGLSILSQRIArkPMTILVINNHGGAIFSLLPiakrTEPRVLNQYFYTSHDISIENLCL 853
|
570 580 590
....*....|....*....|....*....|...
5Z2P_B 503 MFELKYHRPQNWQELETAFADAWRTPTTTVIEM 535
Cdd:PLN02980 854 AHGVRHLHVGTKSELEDALFTSQVEQMDCVVEV 886
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
12-170 |
2.68e-76 |
|
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: 238.17 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 12 AVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALI 91
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 92 EAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTL---HAGGVHINC 168
Cdd:cd07037 81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEAlsaPPGPVHLNL 160
|
..
5Z2P_B 169 PF 170
Cdd:cd07037 161 PF 162
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
2-556 |
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: 691.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 2 SVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGT 81
Cdd:COG1165 1 SDKNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 82 AVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPA-RWLVSTIDHALGTL- 159
Cdd:COG1165 81 AAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDAlRYLRRTINRALAAAl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 160 --HAGGVHINCPFAEPLYGEMDDTglswqqrlgDWWQDDKPWLR-----EAPRLESEKQRDWFFWRQKRGVVVAGRMSAE 232
Cdd:COG1165 161 gpPPGPVHINVPFREPLYPDPDEE---------DPLAAGGPWIRvtppePAPSPEALAQLADELERAKRGLIVAGPLPPP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 233 E--GKKVALWAQTLGWPLIGDVLSQT--GQPLPCADLWLGNAKATSELqQAQIVVQLGSSLTGKRLLQWQASCEPEEYWI 308
Cdd:COG1165 232 EelAEALAALAEALGWPVLADPLSNLrhPNVISTYDLLLRNPEFAELL-QPDLVIRFGGPPVSKRLKQFLRRHPPAEHWV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 309 VDDIEGRLDPAHHRGRRLIANIADWLELHPAE---KRQPWCvEIPRLAEQAMQAVIARR---DAFGEAQLAHRICDYLPE 382
Cdd:COG1165 311 VDPSGEWRDPFHSLTRVIEADPEAFLEALAERlppADSAWL-ARWLAAEQKARAAIDEYlaeDPLSEGAVARRLLEALPE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 383 QGQLFVGNSLVVRLIDALSQ-LPAGYPVYSNKGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAP 461
Cdd:COG1165 390 GSTLFVGNSMPVRDLDLFARpLPKGVRVYANRGASGIDGTVSTALGAALASGKPTVLLTGDLSFLHDLNGLLLLYELPPN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 462 LVLIVVNNNGGQIFSLLPTPQSE--RERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVND 539
Cdd:COG1165 470 LTIVVVNNDGGGIFSMLPGAKFEpeFERFFGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDR 549
|
570
....*....|....*..
5Z2P_B 540 TDGAQTLQQLLAQVSHL 556
Cdd:COG1165 550 EENAELLKALFAAVAAA 566
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
10-431 |
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: 521.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 10 WAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPA 89
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 90 LIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTL---HAGGVHI 166
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEPLAYLRSTVDRALAQAqgaPPGPVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 167 NCPFAEPLYGEmddtglSWQQRLGDWWQDDKPWL-REAPRLESEK-QRDWFFWRQ-KRGVVVAGRMS-AEEGKKVALWAQ 242
Cdd:TIGR00173 161 NVPFREPLYPD------PLLQPLQPWLRSGVPTIsTGPPVLDPESlQELWDRLRQaKRGLIIAGPLAgAEDAEALAALAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 243 TLGWPLIGDVLSQTGQP-----LPCADLWLGNAKATSELqQAQIVVQLGSSLTGKRLLQWQAScEPEEYWIVDDIEGRLD 317
Cdd:TIGR00173 235 ALGWPLLADPLSGLRGGphplvIDHYDLLLANAELREEL-QPDLVIRFGGPPVSKRLRQWLAR-APAEYWVVDPRPGWLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 318 PAHHRGRRLIANIADWLELHPAEKRQPW------CVEIPRLAEQAMQAVIARRDAFgEAQLAHRICDYLPEQGQLFVGNS 391
Cdd:TIGR00173 313 PFHHATTRLEASPAAFAEALAGLLKNPAaawldrWLEAEAKARAALREVLAEEPLS-ELSLARALSQLLPDGSALFVGNS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
5Z2P_B 392 LVVRLIDALSQLPAG-YPVYSNKGASGIDGLLSTAAGVQRA 431
Cdd:TIGR00173 392 MPIRDLDTFSSPPDKpIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| TPP_enzyme_M_2 |
pfam16582 |
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine ... |
184-388 |
3.04e-114 |
|
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine pyrophosphate in sequences not captured by pfam00205. This enzyme is necessary for the first step of the biosynthesis of menaquinone, or vitamin K2, an important cofactor in electron transport in bacteria.
Pssm-ID: 435442 Cd Length: 207 Bit Score: 337.75 E-value: 3.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 184 SWQQRLGDWWQDDKPWLRE-APRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPC 262
Cdd:pfam16582 1 SWLAPLGDWLQQNKPWLRYqAQQLEVPTHDDWDFWRQKKGVIVAGRLSAEEGMQLAAWAQKLGWPLLTDVQSQTGQPLPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 263 ADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKR 342
Cdd:pfam16582 81 ADLWLANPTAREELAQADIVIQFGGRLTSKRLLQFLAACKPHEYWLVDPLPGRLDPAHHRGRRFVASVGEWLRAHPPLRQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
5Z2P_B 343 QPWCVEIPRLAEQAMQAVIAR-RDAFGEAQLAHRICDYLPEQGQLFV 388
Cdd:pfam16582 161 APWALELLALSEFLASFIEQQvGGEFGEAQLAHRIAALLPDQGQLFI 207
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
2-535 |
6.58e-94 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 314.49 E-value: 6.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 2 SVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGT 81
Cdd:PLN02980 295 DYANINAVWASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 82 AVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHAL--GTL 159
Cdd:PLN02980 375 AVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMVLTTLDSAVhwATS 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 160 HA-GGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREApRLESEKQRD----------WFFWRQKRGVVVAGR 228
Cdd:PLN02980 455 SPcGPVHINCPFREPLDGSPTNWMSSCLKGLDMWMSNAEPFTKYI-QMQSSKADGdttgqitevlEVIQEAKRGLLLIGA 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 229 MSAEEGK-KVALWAQTLGWPLIGDVLS-----QTGQPLPCAD---LWLGN------AKATSELQQAQIVVQLGSSLTGKR 293
Cdd:PLN02980 534 IHTEDDIwAALLLAKHLMWPVVADILSglrlrKLFKSFPEFElniLFVDHldhallSDSVRNWIQFDVVIQIGSRITSKR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 294 LLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLE-LHPAE---KRQPWCVEIP---RLAEQAMQAVIARRDA 366
Cdd:PLN02980 614 VSQMLEKCFPFSYILVDKHPCRHDPSHLVTHRVQSNIVQFADcLLKAQfprRRSKWHGHLQaldGMVAQEISFQIHAESS 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 367 FGEAQLAHRICDYLPEQGQLFVGNSLVVRLID----------------ALSQLP--AGYPVYSNKGASGIDGLLSTAAGV 428
Cdd:PLN02980 694 LTEPYVAHVISEALTSDSALFIGNSMAIRDADmygcssenyssrivdmMLSAELpcQWIQVAGNRGASGIDGLLSTAIGF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 429 QRASGKPTLAIVGDLSALYDLNALALLRQVSA--PLVLIVVNNNGGQIFSLLP----TPQSERERFYLMPQNVHFEHAAA 502
Cdd:PLN02980 774 AVGCNKRVLCVVGDISFLHDTNGLSILSQRIArkPMTILVINNHGGAIFSLLPiakrTEPRVLNQYFYTSHDISIENLCL 853
|
570 580 590
....*....|....*....|....*....|...
5Z2P_B 503 MFELKYHRPQNWQELETAFADAWRTPTTTVIEM 535
Cdd:PLN02980 854 AHGVRHLHVGTKSELEDALFTSQVEQMDCVVEV 886
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
12-170 |
2.68e-76 |
|
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: 238.17 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 12 AVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALI 91
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 92 EAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTL---HAGGVHINC 168
Cdd:cd07037 81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEAlsaPPGPVHLNL 160
|
..
5Z2P_B 169 PF 170
Cdd:cd07037 161 PF 162
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
367-538 |
7.95e-76 |
|
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: 237.49 E-value: 7.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 367 FGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQ-LPAGYPVYSNKGASGIDGLLSTAAGVQRASGKPTLAIVGDLSA 445
Cdd:cd02009 1 LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFALpSDKTVRVFANRGASGIDGTLSTALGIALATDKPTVLLTGDLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 446 LYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLP--TPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFAD 523
Cdd:cd02009 81 LHDLNGLLLGKQEPLNLTIVVINNNGGGIFSLLPqaSFEDEFERLFGTPQGLDFEHLAKAYGLEYRRVSSLDELEQALES 160
|
170
....*....|....*
5Z2P_B 524 AWRTPTTTVIEMVVN 538
Cdd:cd02009 161 ALAQDGPHVIEVKTD 175
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
12-170 |
1.87e-44 |
|
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: 154.43 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 12 AVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVaVIVTSGTAVANLYPALI 91
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPV-VIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 92 EAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPtqdipaRWLVSTIDHALGTLHA--GGVHINCP 169
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSP------AELPAGIDHAIRTAYAsqGPVVVRLP 153
|
.
5Z2P_B 170 F 170
Cdd:cd06586 154 R 154
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
11-543 |
1.02e-20 |
|
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: 95.61 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 11 AAVILEALTRHGVRHI-CIaPGSRSTPLTLAAAENSAfIHHTHF-DERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYP 88
Cdd:COG0028 6 ADALVEALEAEGVETVfGV-PGGAILPLYDALRRQSG-IRHILVrHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 89 ALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPtQDIPArwlvsTIDHALGTLHA---GGVH 165
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDP-EDLPE-----VLRRAFRIATSgrpGPVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 166 INCPfAEPLYGEMDDTglSWQQRLGDWWQDDKP----------WLREAprlesekqrdwffwrqKRGVVVAGR--MSAEE 233
Cdd:COG0028 158 LDIP-KDVQAAEAEEE--PAPPELRGYRPRPAPdpeaieeaaeLLAAA----------------KRPVILAGGgaRRAGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 234 GKKVALWAQTLGWPLigdVLSQTGQ-PLPCAD-LWLGNA-----KATSE-LQQAQIVVQLGSSLtGKRLLQWQASCEPEE 305
Cdd:COG0028 219 AEELRALAERLGAPV---VTTLMGKgAFPEDHpLYLGMLgmhgtPAANEaLAEADLVLAVGARF-DDRVTGNWDEFAPDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 306 YWI-VDDIEGRLDPAHHRGRRLIANIADWLE-LHPA-----EKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRICD 378
Cdd:COG0028 295 KIIhIDIDPAEIGKNYPVDLPIVGDAKAVLAaLLEAlepraDDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALRE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 379 YLPEQGQLF--VGNSLVVrlidALSQLPAGYP--VYSNKGASGIdGL-LSTAAGVQRA-SGKPTLAIVGDLSALYDLNAL 452
Cdd:COG0028 375 ALPDDAIVVtdVGQHQMW----AARYLRFRRPrrFLTSGGLGTM-GYgLPAAIGAKLArPDRPVVAITGDGGFQMNLQEL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 453 ALLRQVSAPLVLIVVNNNG-GQIfsllptpQSERERFYLMP------QNVHFEHAAAMFELKYHRPQNWQELETAFADAW 525
Cdd:COG0028 450 ATAVRYGLPVKVVVLNNGGlGMV-------RQWQELFYGGRysgtdlPNPDFAKLAEAFGAKGERVETPEELEAALEEAL 522
|
570
....*....|....*...
5Z2P_B 526 RTPTTTVIEMVVNDTDGA 543
Cdd:COG0028 523 ASDGPALIDVRVDPEENP 540
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
13-169 |
9.11e-20 |
|
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: 86.05 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 13 VILEALTRHGVRHICIAPGSRSTPLtLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIE 92
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPL-LDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 93 AGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPtQDIPArwlvsTIDHALGTLHA---GGVHINCP 169
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSP-EEIPE-----ALRRAFRIALSgrpGPVALDLP 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
11-169 |
6.19e-19 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 84.21 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 11 AAVILEALTRHGVRHICIAPGSRSTPLtLAAAENSAFIHHTHF-DERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPA 89
Cdd:pfam02776 2 AEALADVLKALGVDTVFGVPGGHILPL-LDALAKSPGIRYVLTrHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 90 LIEAGLTGEKLILLTADRPPELIDCGANQAIR-QPGMFASHPTHSISLPRPTQDIPArwLVSTIDHALgTLHAGGVHINC 168
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQELdQLALFRPVTKWAVRVTSADEIPEV--LRRAFRAAL-SGRPGPVYLEI 157
|
.
5Z2P_B 169 P 169
Cdd:pfam02776 158 P 158
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
371-537 |
9.04e-10 |
|
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: 57.65 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 371 QLAHRICDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNKGASGIDGLLSTAAGVQRAS-GKPTLAIVGDLSALYDL 449
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAApDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 450 NALALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFehaAAMFE---LKYHRPQNWQELETAFADAWR 526
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDF---AALAEaygAKGVRVEDPEDLEAALAEALA 157
|
170
....*....|.
5Z2P_B 527 TPTTTVIEMVV 537
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
414-537 |
5.65e-06 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 49.18 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 414 GASGidGL---LSTAAGVQRAS-GKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNG-------GQIFSLLPTPQ 482
Cdd:PRK07092 404 MASG--GLgygLPAAVGVALAQpGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRygalrwfAPVFGVRDVPG 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
5Z2P_B 483 SErerfylMPqNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVV 537
Cdd:PRK07092 482 LD------LP-GLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEV 529
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
370-537 |
2.93e-05 |
|
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: 44.89 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 370 AQLAHRICDYLPEQGQLF---VGNSLVVRLidalsQLPAGYP-VYSNKGASGIDGLLSTAAGVQRA-SGKPTLAIVGDLS 444
Cdd:cd02002 4 EYLAAALAAALPEDAIIVdeaVTNGLPLRD-----QLPLTRPgSYFTLRGGGLGWGLPAAVGAALAnPDRKVVAIIGDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 445 ALYDLNALALLRQVSAPLVLIVVNNNGGQI---FSLLPTPQSERERFYLMPQ----NVHFEHAAAMFELKYHRPQNWQEL 517
Cdd:cd02002 79 FMYTIQALWTAARYGLPVTVVILNNRGYGAlrsFLKRVGPEGPGENAPDGLDlldpGIDFAAIAKAFGVEAERVETPEEL 158
|
170 180
....*....|....*....|
5Z2P_B 518 ETAFADAWRTPTTTVIEMVV 537
Cdd:cd02002 159 DEALREALAEGGPALIEVVV 178
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
11-144 |
1.02e-04 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 45.20 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 11 AAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPAL 90
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
5Z2P_B 91 IEAGLTGEKLILLTADRPPELIdcgANQAIRQPGMFA-SHPT--HSISLPRPtQDIP 144
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLI---GNDAFQECDMIGiSRPVvkHSFLVKDA-EDIP 139
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
8-118 |
1.04e-04 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 45.11 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 8 RRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLY 87
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110
....*....|....*....|....*....|.
5Z2P_B 88 PALIEAGLTGEKLILLTADRPPELIDCGANQ 118
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDAFQ 123
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
422-534 |
1.04e-04 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 42.57 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 422 LSTAAGVQRAS-GKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNG-GQI--FSLLPTPQSERERFYLMPQNVHF 497
Cdd:pfam02775 34 LPAAIGAKLARpDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGyGMTrgQQTPFGGGRYSGPSGKILPPVDF 113
|
90 100 110
....*....|....*....|....*....|....*..
5Z2P_B 498 EHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIE 534
Cdd:pfam02775 114 AKLAEAYGAKGARVESPEELEEALKEALEHDGPALID 150
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
335-543 |
1.12e-04 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 44.97 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 335 ELHPAEKRQPWCVEiprLAEQAMQAVIARRDAF--GEAQLAHRICDYLPeqGQLFVGNSlvvrlidalSQlpagyPVYSN 412
Cdd:PRK07524 327 RLPGQAAAADWGAA---RVAALRQALRAEWDPLtaAQVALLDTILAALP--DAIFVGDS---------TQ-----PVYAG 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 413 K-------------GASGIDGL---LSTAAGVQRAS-GKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNG-GQI 474
Cdd:PRK07524 388 NlyfdadaprrwfnASTGYGTLgygLPAAIGAALGApERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGyGEI 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5Z2P_B 475 FSLLptPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGA 543
Cdd:PRK07524 468 RRYM--VARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQACWFAA 534
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
55-534 |
2.49e-04 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 43.83 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 55 ERGLGHLALGLAKVSkQPVAVIVTS-GTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGA---NQAIRQPGMFashp 130
Cdd:PRK07064 50 EAGAVNMADAHARVS-GGLGVALTStGTGAGNAAGALVEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTML---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 131 tHSISlprptqdiPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDdtgLSWQQRLGDWWQDDKPwlREAPRLESEK 210
Cdd:PRK07064 125 -RAVS--------KAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP---IDIQAAEIELPDDLAP--VHVAVPEPDA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 211 QRDWFFWRQ----KRGVVVAGRMSAEEGKKVALWAQtLGWPLigdVLSQTGQP-LPCAD-LWLG---NAKATSEL-QQAQ 280
Cdd:PRK07064 191 AAVAELAERlaaaRRPLLWLGGGARHAGAEVKRLVD-LGFGV---VTSTQGRGvVPEDHpASLGafnNSAAVEALyKTCD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 281 IVVQLGSSLTGKRLLQW-----------------QASCEPEEYWIVDDIEGRLDpahhrgrRLIANIADWLELHPAekrq 343
Cdd:PRK07064 267 LLLVVGSRLRGNETLKYslalprplirvdadaaaDGRGYPNDLFVHGDAARVLA-------RLADRLEGRLSVDPA---- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 344 pWcveIPRLAEQAMQAVIARRDAFGE-AQLAHRICDYLPEQGqLFV----------GNslvvRLIDALSQLPAGYPVysn 412
Cdd:PRK07064 336 -F---AADLRAAREAAVADLRKGLGPyAKLVDALRAALPRDG-NWVrdvtisnstwGN----RLLPIFEPRANVHAL--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 413 kgASGIDGLLSTAAGVQRA-SGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNG-GQIFSLLPTPQSERERFyl 490
Cdd:PRK07064 404 --GGGIGQGLAMAIGAALAgPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGyGVIRNIQDAQYGGRRYY-- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
5Z2P_B 491 mpQNVH---FEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIE 534
Cdd:PRK07064 480 --VELHtpdFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVE 524
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
422-537 |
4.10e-04 |
|
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: 41.71 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 422 LSTAAGVQRAS-GKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNG-G------QIFsllptpQSERERFYLMPQ 493
Cdd:cd02015 56 LPAAIGAKVARpDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGSlGmvrqwqELF------YEGRYSHTTLDS 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
5Z2P_B 494 NVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVV 537
Cdd:cd02015 130 NPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDGPVLLDVLV 173
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
425-527 |
3.15e-03 |
|
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: 38.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 425 AAGVQRASGKPTLAIV----GDLSAlydLNALALLRQVSAPLVLIVvnnngGQIfsllPTPQSERERFYLMPQNVHFEHA 500
Cdd:cd07035 50 ADGYARATGKPGVVLVtsgpGLTNA---VTGLANAYLDSIPLLVIT-----GQR----PTAGEGRGAFQEIDQVALFRPI 117
|
90 100
....*....|....*....|....*...
5Z2P_B 501 AamfelKY-HRPQNWQELETAFADAWRT 527
Cdd:cd07035 118 T-----KWaYRVTSPEEIPEALRRAFRI 140
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
11-151 |
9.37e-03 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 38.68 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5Z2P_B 11 AAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPAL 90
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5Z2P_B 91 IEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSIsLPRPTQDIP-----ARWLVST 151
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSF-LVKQTEDIPqvlkkAFWLAAS 151
|
|
| |
