|
Name |
Accession |
Description |
Interval |
E-value |
| SE |
pfam08491 |
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ... |
276-547 |
7.45e-148 |
|
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.
Pssm-ID: 400679 Cd Length: 276 Bit Score: 426.75 E-value: 7.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 276 HAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLVDIRGE-MPR- 353
Cdd:pfam08491 1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 354 ---NLREYMAEKIYPQLPDHLKEPFLEAIQNSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTGGGMTVVFKDLKLW 430
Cdd:pfam08491 81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 431 RKLLKSIPDLYDDAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAKDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 510
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 545520806 511 LSPNPLILIGHFFAVALYATYFCFKSEPWITKPRAIF 547
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
122-567 |
8.20e-126 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 381.12 E-value: 8.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVvDGYIIHDQD 200
Cdd:PTZ00367 33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 201 SKsEVQIPYpvsenSQVRSGRAFHHGRFIMGLRKAAMA--EPNTKFIEGIVLQLLEED----DAVMGVQYRDKETGDV-- 272
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDVpe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 273 ------------------KELHAPLTVVADGLFSKFRKNLISNKVSVS--SHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PTZ00367 186 npfredppsanpsattvrKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 333 IYQISSNETRVLVDIRGEMPRNLRE---YMAEKIYPQLPDHLKEPFLEAIQN-SRLRSMPASFLPSSPVNKRGVLLLGDA 408
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASKDtKRIRSMPNARYPPAFPSIKGYVGIGDH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 409 YNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYD---------DAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAK 479
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 480 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVALYA--------------------TYFCFKSEPW 539
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGvlnlimetgaysifgkqlssFEKLTNVASF 499
|
490 500
....*....|....*....|....*...
gi 545520806 540 ITKPRAIFSSGAVLYKACSVIFPLIYSE 567
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSE 527
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
120-489 |
3.14e-21 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 95.00 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIdAQVVDGYIIHDQ 199
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 DSKSEV-QIPYPVsenSQVRSGRAFHHGRFIMGLRKAAmAEPNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeLHAP 278
Cdd:COG0654 80 SDGRVLaRFDAAE---TGLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 279 LTVVADGLFSKFRKnlisnkvsvsSHFVGFLMKNAPQfkanhaeliltnpspvliyqissneTRVLVDIRGEMprnlrey 358
Cdd:COG0654 151 LVVGADGARSAVRR----------LLGIGFTGRDYPQ-------------------------RALWAGVRTEL------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 359 maEKIYPQLPDHLKEpFLEAIQNSRLrsmPASFLPSSPVNKRGVLLLGDA-YNMrHPLTGGGMTVVFKD-LKLWRKLLKS 436
Cdd:COG0654 189 --RARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDaAALAWKLAAA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 545520806 437 IPDLyDDAAVFQAkksfYW-ERKTSHSFVVNiLAQALYELFSAKDDSLHQLRKA 489
Cdd:COG0654 262 LRGR-DDEAALAR----YErERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
134-421 |
2.25e-16 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 79.63 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 134 GSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEdidaQVVDGYIIHDQDSKSeVQIPYPVSE 213
Cdd:COG0644 5 GSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSPGGKS-VELPPGRGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 214 NSQVRsgRAfhhgRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMgVqyrdkETGDVKELHAPLTVVADGLFSKFRK 292
Cdd:COG0644 80 GYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARSLLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 293 NLISNKVSVSSHFVGFLMK------NAPQFKANHAELILTNPSPV-LIYQISSNETRVLVDIrgemprnlreymaekiyp 365
Cdd:COG0644 147 KLGLKRRSDEPQDYALAIKehwelpPLEGVDPGAVEFFFGEGAPGgYGWVFPLGDGRVSVGI------------------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 545520806 366 qlpdhlkepfleaiqnsrlrsmPASFLPSSPVnKRGVLLLGDAYNMRHPLTGGGMT 421
Cdd:COG0644 209 ----------------------PLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIH 241
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
121-426 |
9.13e-16 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 79.18 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVVDGY-IIHDQ 199
Cdd:PRK07045 4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 DSKSevqipypvSENSQVRSGRAFhhgrFIM----GLRKAAMA----EPNTKFIEGIVLQLLE--EDDAVMGVQYRDKET 269
Cdd:PRK07045 84 ELIA--------SLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 270 gdvkelHAPLTVV-ADGLFSKFRKNLI---SNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLV 345
Cdd:PRK07045 152 ------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 346 DIRGEmprNLREYMA----EKIYPQLPDHLKEPFLEAIQ----NSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTG 417
Cdd:PRK07045 226 SFPAD---EMQGYLAdttrTKLLARLNEFVGDESADAMAaigaGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITG 302
|
....*....
gi 545520806 418 GGMTVVFKD 426
Cdd:PRK07045 303 QGMNLAIED 311
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
124-369 |
4.43e-06 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 48.93 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 163
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 164 EFLQPGGYRVLEDLGLKDAVEDIDAQVVDGYIIHDQDSKSEVQIpYPVSENSQ----VRSGRAFHHGRFIMGLRKAAMAE 239
Cdd:pfam01266 81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAELLDAEELREL-EPLLPGLRgglfYPDGGHVDPARLLRALARAAEAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 240 pNTKFIEGIVLQLLEEDDAVMGVQyrdkETGDVKELhapltVVADGLFSKF-RKNLISNKVSVSSHFVGFLMKnaPQFKA 318
Cdd:pfam01266 160 -GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADLlALPGLRLPVRPVRGQVLVLEP--LPEAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545520806 319 NHAELILTNPSPVLIYQISSNETRVLV--------DIRGEMPRNLREYM---AEKIYPQLPD 369
Cdd:pfam01266 228 LILPVPITVDPGRGVYLRPRADGRLLLggtdeedgFDDPTPDPEEIEELleaARRLFPALAD 289
|
|
| mannonate_red_SDR_c |
cd08935 |
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ... |
121-189 |
1.77e-04 |
|
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187640 [Multi-domain] Cd Length: 271 Bit Score: 43.60 E-value: 1.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545520806 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG------YRVLEDLGLKDAVEDIDAQ 189
Cdd:cd08935 5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGraialaADVLDRASLERAREEIVAQ 79
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SE |
pfam08491 |
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ... |
276-547 |
7.45e-148 |
|
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.
Pssm-ID: 400679 Cd Length: 276 Bit Score: 426.75 E-value: 7.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 276 HAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLVDIRGE-MPR- 353
Cdd:pfam08491 1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 354 ---NLREYMAEKIYPQLPDHLKEPFLEAIQNSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTGGGMTVVFKDLKLW 430
Cdd:pfam08491 81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 431 RKLLKSIPDLYDDAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAKDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 510
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 545520806 511 LSPNPLILIGHFFAVALYATYFCFKSEPWITKPRAIF 547
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
122-567 |
8.20e-126 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 381.12 E-value: 8.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVvDGYIIHDQD 200
Cdd:PTZ00367 33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 201 SKsEVQIPYpvsenSQVRSGRAFHHGRFIMGLRKAAMA--EPNTKFIEGIVLQLLEED----DAVMGVQYRDKETGDV-- 272
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDVpe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 273 ------------------KELHAPLTVVADGLFSKFRKNLISNKVSVS--SHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PTZ00367 186 npfredppsanpsattvrKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 333 IYQISSNETRVLVDIRGEMPRNLRE---YMAEKIYPQLPDHLKEPFLEAIQN-SRLRSMPASFLPSSPVNKRGVLLLGDA 408
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASKDtKRIRSMPNARYPPAFPSIKGYVGIGDH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 409 YNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYD---------DAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAK 479
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 480 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVALYA--------------------TYFCFKSEPW 539
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGvlnlimetgaysifgkqlssFEKLTNVASF 499
|
490 500
....*....|....*....|....*...
gi 545520806 540 ITKPRAIFSSGAVLYKACSVIFPLIYSE 567
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSE 527
|
|
| PLN02985 |
PLN02985 |
squalene monooxygenase |
95-527 |
3.67e-101 |
|
squalene monooxygenase
Pssm-ID: 178566 [Multi-domain] Cd Length: 514 Bit Score: 315.69 E-value: 3.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 95 SRRHKKGTSISEttligaAASSIPSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVL 174
Cdd:PLN02985 22 TNRKKKATELAD------AVAEERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERMMGEFMQPGGRFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 175 EDLGLKDAVEDIDAQVVDGYIIHdQDSKsEVQIPYPVSEN--SQVRSGRAFHHGRFIMGLRKAAMAEPNTKFIEGIVLQL 252
Cdd:PLN02985 96 SKLGLEDCLEGIDAQKATGMAVY-KDGK-EAVAPFPVDNNnfPYEPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 253 LEEDDAVMGVQYRDKETGDVKELhAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PLN02985 174 IEEKGVIKGVTYKNSAGEETTAL-APLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 333 IYQISSNETRVLVDI---------RGEMPRNLREYMAekiyPQLPDHLKEPFLEAI-QNSRLRSMPASFLPSSPVNKRGV 402
Cdd:PLN02985 253 LYQISSTDVRCVFEVlpdnipsiaNGEMSTFVKNTIA----PQVPPKLRKIFLKGIdEGAHIKVVPTKRMSATLSDKKGV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 403 LLLGDAYNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYDDAAVFQAKKSFYWERKtSHSFVVNILAQALYE-LFSAKDD 481
Cdd:PLN02985 329 IVLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRK-PMSATVNTLGNAFSQvLVASTDE 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 545520806 482 SLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVAL 527
Cdd:PLN02985 408 AKEAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITL 453
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
120-489 |
3.14e-21 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 95.00 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIdAQVVDGYIIHDQ 199
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 DSKSEV-QIPYPVsenSQVRSGRAFHHGRFIMGLRKAAmAEPNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeLHAP 278
Cdd:COG0654 80 SDGRVLaRFDAAE---TGLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 279 LTVVADGLFSKFRKnlisnkvsvsSHFVGFLMKNAPQfkanhaeliltnpspvliyqissneTRVLVDIRGEMprnlrey 358
Cdd:COG0654 151 LVVGADGARSAVRR----------LLGIGFTGRDYPQ-------------------------RALWAGVRTEL------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 359 maEKIYPQLPDHLKEpFLEAIQNSRLrsmPASFLPSSPVNKRGVLLLGDA-YNMrHPLTGGGMTVVFKD-LKLWRKLLKS 436
Cdd:COG0654 189 --RARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDaAALAWKLAAA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 545520806 437 IPDLyDDAAVFQAkksfYW-ERKTSHSFVVNiLAQALYELFSAKDDSLHQLRKA 489
Cdd:COG0654 262 LRGR-DDEAALAR----YErERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
134-421 |
2.25e-16 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 79.63 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 134 GSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEdidaQVVDGYIIHDQDSKSeVQIPYPVSE 213
Cdd:COG0644 5 GSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSPGGKS-VELPPGRGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 214 NSQVRsgRAfhhgRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMgVqyrdkETGDVKELHAPLTVVADGLFSKFRK 292
Cdd:COG0644 80 GYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARSLLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 293 NLISNKVSVSSHFVGFLMK------NAPQFKANHAELILTNPSPV-LIYQISSNETRVLVDIrgemprnlreymaekiyp 365
Cdd:COG0644 147 KLGLKRRSDEPQDYALAIKehwelpPLEGVDPGAVEFFFGEGAPGgYGWVFPLGDGRVSVGI------------------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 545520806 366 qlpdhlkepfleaiqnsrlrsmPASFLPSSPVnKRGVLLLGDAYNMRHPLTGGGMT 421
Cdd:COG0644 209 ----------------------PLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIH 241
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
121-426 |
9.13e-16 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 79.18 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVVDGY-IIHDQ 199
Cdd:PRK07045 4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 DSKSevqipypvSENSQVRSGRAFhhgrFIM----GLRKAAMA----EPNTKFIEGIVLQLLE--EDDAVMGVQYRDKET 269
Cdd:PRK07045 84 ELIA--------SLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 270 gdvkelHAPLTVV-ADGLFSKFRKNLI---SNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLV 345
Cdd:PRK07045 152 ------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 346 DIRGEmprNLREYMA----EKIYPQLPDHLKEPFLEAIQ----NSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTG 417
Cdd:PRK07045 226 SFPAD---EMQGYLAdttrTKLLARLNEFVGDESADAMAaigaGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITG 302
|
....*....
gi 545520806 418 GGMTVVFKD 426
Cdd:PRK07045 303 QGMNLAIED 311
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
124-292 |
3.53e-14 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 74.51 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIE------RDLKepdrivGEFLQPGGYRVLEDLGLKDAVEDIDaqvvdgyiiH 197
Cdd:PRK06185 8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDFR------GDTVHPSTLELMDELGLLERFLELP---------H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 198 DQDSKSEVQIPypvseNSQVRS---GRAFHHGRFIM---------GLRKAAMAEPNTKFIEG-IVLQLLEEDDAVMGVQY 264
Cdd:PRK06185 73 QKVRTLRFEIG-----GRTVTLadfSRLPTPYPYIAmmpqwdfldFLAEEASAYPNFTLRMGaEVTGLIEEGGRVTGVRA 147
|
170 180
....*....|....*....|....*...
gi 545520806 265 RDKEtGDVkELHAPLTVVADGLFSKFRK 292
Cdd:PRK06185 148 RTPD-GPG-EIRADLVVGADGRHSRVRA 173
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
119-306 |
1.53e-11 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 66.21 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 119 SQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIErdlkEPDRIvGEF-----LQPGGYRVLEDLGLKDAVEDIdAQVVDG 193
Cdd:PRK08163 1 MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLE----QAAEI-GEIgagiqLGPNAFSALDALGVGEAARQR-AVFTDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 194 YIIHD-QDSKSEVQIpyPVSENSQVRSG-------RAFHHGRFImglrKAAMAEPNTKFIEGIVLQLLEEDDAvmGVQYR 265
Cdd:PRK08163 75 LTMMDaVDAEEVVRI--PTGQAFRARFGnpyavihRADIHLSLL----EAVLDHPLVEFRTSTHVVGIEQDGD--GVTVF 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545520806 266 DKETgdvKELHAPLTVVADGLFSKFRKNLISNKVSVSSHFV 306
Cdd:PRK08163 147 DQQG---NRWTGDALIGCDGVKSVVRQSLVGDAPRVTGHVV 184
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
122-420 |
1.05e-10 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 63.50 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIV---GEFLQPGGYRVLEDLGLKDAVEDIDA---------Q 189
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERH---ATTSVlprAHGLNQRTMELLRQAGLEDRILAEGVphegmglafY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 190 VVDGYIIHDQDSKSEVQIPYPVSENSQVrsgrafhhgrfimgLRKAAMAEPnTKFIEGIVLQLLEEDDAVMGVQYRDKET 269
Cdd:pfam01494 78 NTRRRADLDFLTSPPRVTVYPQTELEPI--------------LVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRDRRD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 270 GDVKELHAPLTVVADGLFSKFRKNL---ISNKVSVSSHFVG--FLMKNAPQFKANHA--ELILTNPSPVLIYQISSNETR 342
Cdd:pfam01494 143 GEEYTVRAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDvlFDAPDLSDPVERAFvhYLIYAPHSRGFMVGPWRSAGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 343 VLVDIRGEmprnLREYMAEKIYPQLPDHLKEPFLEAIQNSRLrsmPASFLPSS--PVNKR--------GVLLLGDAYNmR 412
Cdd:pfam01494 223 ERYYVQVP----WDEEVEERPEEFTDEELKQRLRSIVGIDLA---LVEILWKSiwGVASRvatryrkgRVFLAGDAAH-I 294
|
....*....
gi 545520806 413 HPLTGG-GM 420
Cdd:pfam01494 295 HPPTGGqGL 303
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
125-292 |
4.55e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 55.26 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDiDAQVVDGYIIHDQDSKSE 204
Cdd:PRK06847 7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECLE-AGFGFDGVDLFDPDGTLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 205 VQIPYPVSENSQVRSG-----RAFHHgrfImgLRKAAMAEpNTKFIEGIVLQLLEEDDAVMGVQYRDKETGdvkelHAPL 279
Cdd:PRK06847 86 AELPTPRLAGDDLPGGggimrPALAR---I--LADAARAA-GADVRLGTTVTAIEQDDDGVTVTFSDGTTG-----RYDL 154
|
170
....*....|...
gi 545520806 280 TVVADGLFSKFRK 292
Cdd:PRK06847 155 VVGADGLYSKVRS 167
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
125-294 |
1.49e-07 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 53.79 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD----LKEPD---RIVGefLQPGGYRVLEDLGLKDAVEDI------DAQVV 191
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQplaaLADPAfdgREIA--LTHASREILQRLGAWDRIPEDeisplrDAKVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 192 DG---YIIH-DQDSKSEVQIPYPVSeNSQVRsgRAfhhgrfimgLRKAAMAEPNTKFIEGIVLQLLEEDDAVMGVQYRDK 267
Cdd:PRK09126 84 NGrspFALTfDARGRGADALGYLVP-NHLIR--RA---------AYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANG 151
|
170 180
....*....|....*....|....*..
gi 545520806 268 ETgdvkeLHAPLTVVADGLFSKFRKNL 294
Cdd:PRK09126 152 RR-----LTARLLVAADSRFSATRRQL 173
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
124-369 |
4.43e-06 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 48.93 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 163
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 164 EFLQPGGYRVLEDLGLKDAVEDIDAQVVDGYIIHDQDSKSEVQIpYPVSENSQ----VRSGRAFHHGRFIMGLRKAAMAE 239
Cdd:pfam01266 81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAELLDAEELREL-EPLLPGLRgglfYPDGGHVDPARLLRALARAAEAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 240 pNTKFIEGIVLQLLEEDDAVMGVQyrdkETGDVKELhapltVVADGLFSKF-RKNLISNKVSVSSHFVGFLMKnaPQFKA 318
Cdd:pfam01266 160 -GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADLlALPGLRLPVRPVRGQVLVLEP--LPEAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545520806 319 NHAELILTNPSPVLIYQISSNETRVLV--------DIRGEMPRNLREYM---AEKIYPQLPD 369
Cdd:pfam01266 228 LILPVPITVDPGRGVYLRPRADGRLLLggtdeedgFDDPTPDPEEIEELleaARRLFPALAD 289
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
125-154 |
1.06e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 47.98 E-value: 1.06e-05
10 20 30
....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD 154
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
125-182 |
1.64e-05 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 46.98 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYRV----------LEDLGLKDA 182
Cdd:COG0569 98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD---PERV--ERLAEEDVLVivgdatdeevLEEAGIEDA 160
|
|
| PRK10157 |
PRK10157 |
putative oxidoreductase FixC; Provisional |
124-411 |
3.04e-05 |
|
putative oxidoreductase FixC; Provisional
Pssm-ID: 182273 [Multi-domain] Cd Length: 428 Bit Score: 46.44 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIV--GEFLQPGGYRVLEDLGLKDAVEDIdaqvvdgyIIHDQ-- 199
Cdd:PRK10157 7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVtgGRLYAHSLEHIIPGFADSAPVERL--------ITHEKla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 --DSKSEVQIPYpVSENSQVRSGRAFH--HGRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMGVQyrdkETGDVKE 274
Cdd:PRK10157 79 fmTEKSAMTMDY-CNGDETSPSQRSYSvlRSKFDAWLMEQA-EEAGAQLITGIrVDNLVQRDGKVVGVE----ADGDVIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 275 lhAPLTVVADGLFSKFRKNL-ISNKVSVSSHFVGF---------LMKNAPQFKANHAELILTNPSPV-------LIYqis 337
Cdd:PRK10157 153 --AKTVILADGVNSILAEKLgMAKRVKPTDVAVGVkelielpksVIEDRFQLQGNQGAACLFAGSPTdglmgggFLY--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 338 SNETRVLVDIRGEMpRNLREymAEKIYPQLPDHLKEPFLEA--IQNSRLRSMPASFLPSSPVNKR------GVLLLGDAY 409
Cdd:PRK10157 228 TNENTLSLGLVCGL-HHLHD--AKKSVPQMLEDFKQHPAVAplIAGGKLVEYSAHVVPEAGINMLpelvgdGVLIAGDAA 304
|
..
gi 545520806 410 NM 411
Cdd:PRK10157 305 GM 306
|
|
| PRK06184 |
PRK06184 |
hypothetical protein; Provisional |
120-294 |
6.03e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235728 [Multi-domain] Cd Length: 502 Bit Score: 45.75 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERdLKEP---DRivGEFLQPGGYRVLEDLGLKDAV-----------ED 185
Cdd:PRK06184 1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEK-APEPfpgSR--GKGIQPRTQEVFDDLGVLDRVvaagglyppmrIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 186 IDAQVVDGYIIHDqDSKSEVQIPYPvseNS----QVRSGRafhhgrfIMGLRKAAMA---EPNTKFIEgivlqlLEEDDA 258
Cdd:PRK06184 78 RDDGSVAESDMFA-HLEPTPDEPYP---LPlmvpQWRTER-------ILRERLAELGhrvEFGCELVG------FEQDAD 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 545520806 259 vmGVQYRDKETGDVKELHAPLTVVADGLFSKFRKNL 294
Cdd:PRK06184 141 --GVTARVAGPAGEETVRARYLVGADGGRSFVRKAL 174
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
124-292 |
6.28e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 45.66 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPgGYRVLEDLGLKDAVEDIDA-----QVVDgyiihd 198
Cdd:PRK07494 9 DIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGP-SIRFLERLGLWARLAPHAAplqsmRIVD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 199 qDSKSEVQIPyPVSENSQVRSGRAFhhG------RFIMGLRKAAMAEPN-TKFiegivlqlleeDDAVMGVQYRDKE--- 268
Cdd:PRK07494 82 -ATGRLIRAP-EVRFRAAEIGEDAF--GynipnwLLNRALEARVAELPNiTRF-----------GDEAESVRPREDEvtv 146
|
170 180
....*....|....*....|....*
gi 545520806 269 -TGDVKELHAPLTVVADGLFSKFRK 292
Cdd:PRK07494 147 tLADGTTLSARLVVGADGRNSPVRE 171
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
118-285 |
7.11e-05 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 45.67 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 118 PSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGeflQPGG-------YRVLEDLGLkdaVEDIDAQV 190
Cdd:PRK06183 6 PDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW----PTLYD---LPRAvgiddeaLRVLQAIGL---ADEVLPHT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 191 VDGYIIHDQDSKSEV--QIPYPvsensqvrSGRafHHG-----RFIM-----GLRKAAMAEPNTKFIEGI-VLQLLEEDD 257
Cdd:PRK06183 76 TPNHGMRFLDAKGRClaEIARP--------STG--EFGwprrnAFHQplleaVLRAGLARFPHVRVRFGHeVTALTQDDD 145
|
170 180
....*....|....*....|....*...
gi 545520806 258 AVMgVQYRDkETGDVKELHAPLTVVADG 285
Cdd:PRK06183 146 GVT-VTLTD-ADGQRETVRARYVVGCDG 171
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
125-180 |
7.50e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 41.42 E-value: 7.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIER---DLKEPDRIVGEFLQpggyRVLEDLGLK 180
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERrdrLLPGFDPEIAKILQ----EKLEKNGIE 56
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
125-186 |
8.81e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 45.27 E-value: 8.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIE--RDLKEPDriVGEFLQPGGYRVLEDLGLKDAVEDI 186
Cdd:PRK07538 3 VLIAGGGIGGLTLALTLHQRGIEVVVFEaaPELRPLG--VGINLLPHAVRELAELGLLDALDAI 64
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
125-182 |
1.12e-04 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 44.73 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDR------------IVGEFLQPggyRVLEDLGLKDA 182
Cdd:PRK09496 3 IIIVGAGQVGYTLAENLSGENNDVTVIDTD---EERlrrlqdrldvrtVVGNGSSP---DVLREAGAEDA 66
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
127-153 |
1.72e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 39.82 E-value: 1.72e-04
10 20
....*....|....*....|....*..
gi 545520806 127 IVGSGVLGSALAAVLSRDGRKVTVIER 153
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
125-170 |
1.74e-04 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 43.74 E-value: 1.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 170
Cdd:PRK08277 14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
|
|
| mannonate_red_SDR_c |
cd08935 |
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ... |
121-189 |
1.77e-04 |
|
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187640 [Multi-domain] Cd Length: 271 Bit Score: 43.60 E-value: 1.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545520806 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG------YRVLEDLGLKDAVEDIDAQ 189
Cdd:cd08935 5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGraialaADVLDRASLERAREEIVAQ 79
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
123-209 |
2.08e-04 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 43.92 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 123 PE-VIIVGSGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyRVLEDLGLK-------DAVEDIDaqvv 191
Cdd:COG1249 168 PKsLVVIGGGYIGLEFAQIFARLGSEVTLVERGdrlLPGEDPEISEALE----KALEKEGIDiltgakvTSVEKTG---- 239
|
90
....*....|....*...
gi 545520806 192 DGYIIHDQDSKSEVQIPY 209
Cdd:COG1249 240 DGVTVTLEDGGGEEAVEA 257
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
119-159 |
3.11e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 43.21 E-value: 3.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 545520806 119 SQNDPEVIIVGSGVLGSALAAVLSR-DGRKVTVIErdlKEPD 159
Cdd:COG0579 1 MMEMYDVVIIGAGIVGLALARELSRyEDLKVLVLE---KEDD 39
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
125-180 |
6.49e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 41.92 E-value: 6.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIE---RDLKEPDRIVGEFLQpggyRVLEDLGLK 180
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEaldRLLRAFDEEISAALE----KALEKNGVE 209
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
125-184 |
8.20e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 42.14 E-value: 8.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRI---VGEFLQPG---------------GYRVLEDLGLKDAVE 184
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKN----DTPggrARTFERPGfrfdvgpsvltmpgvLERLFRELGLEDYLE 79
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
125-189 |
8.47e-04 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 41.72 E-value: 8.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyRVLEDLG----LKDAVEDIDAQ 189
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLE----EELREHGvelrLGETVVAIDGD 194
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
112-182 |
9.07e-04 |
|
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 41.25 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 112 AAASSIPSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYRV----------LEDLGLKD 181
Cdd:COG1226 114 AEAAEDAIDLEGHVIIAGFGRVGQIVARLLRAEGIPFVVIDLD---PERV--EELRRFGIKVyygdatrpdvLEAAGIER 188
|
.
gi 545520806 182 A 182
Cdd:COG1226 189 A 189
|
|
| ubiF |
PRK08020 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed |
119-292 |
9.51e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
Pssm-ID: 181199 [Multi-domain] Cd Length: 391 Bit Score: 41.89 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 119 SQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDL-------KEPD-RIVGefLQPGGYRVLEDLGLKDAVEDI---- 186
Cdd:PRK08020 2 TNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAApapfdadSQPDvRISA--ISAASVALLKGLGVWDAVQAMrshp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 187 ----------DAQVVdgyiiHDQDSKSEVQIPYPVsENSQVRsgrafhhgrfiMGLRKAAMAEPNTKFIEGIVLQLLEED 256
Cdd:PRK08020 80 yrrletweweTAHVV-----FDAAELKLPELGYMV-ENRVLQ-----------LALWQALEAHPNVTLRCPASLQALQRD 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 545520806 257 DAVMGVQYRDKEtgdvkELHAPLTVVADGLFSKFRK 292
Cdd:PRK08020 143 DDGWELTLADGE-----EIQAKLVIGADGANSQVRQ 173
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
124-153 |
1.01e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 41.71 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIER 153
Cdd:PRK00711 2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
|
|
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
125-153 |
1.50e-03 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 41.35 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRD-GRKVTVIER 153
Cdd:COG2303 7 YVIVGAGSAGCVLANRLSEDaGLRVLLLEA 36
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
124-154 |
1.96e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 40.99 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|.
gi 545520806 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD 154
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
125-187 |
2.21e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 40.51 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQpggyRVLEDLG----LKDAVEDID 187
Cdd:COG1251 145 VVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLlprqldeeAGALLQ----RLLEALGvevrLGTGVTEIE 211
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
123-165 |
2.30e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 40.55 E-value: 2.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 545520806 123 PE-VIIVGSGVLGSALAAVLSRDGRKVTVIERdlkePDRIVGEF 165
Cdd:PRK06292 169 PKsLAVIGGGVIGLELGQALSRLGVKVTVFER----GDRILPLE 208
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
125-184 |
2.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 40.64 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRIVG-----EFlqpGGYRV-----------------LEDLGLKDA 182
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEAD----DQLGGlaasfEF---GGLPIerfyhhifksdeallelLDELGLEDK 74
|
..
gi 545520806 183 VE 184
Cdd:PRK07233 75 LR 76
|
|
| SDR_a4 |
cd05266 |
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ... |
125-191 |
3.40e-03 |
|
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187576 [Multi-domain] Cd Length: 251 Bit Score: 39.61 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545520806 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPggyrVLEDLGLKDAVEDIDAQVV 191
Cdd:cd05266 1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTP----LAADLTQPGLLADVDHLVI 63
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
127-178 |
5.79e-03 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 39.07 E-value: 5.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 545520806 127 IVGSGVLGSALAAVLSRDGRKVTVIERdlkePDRIvgEFLQPGGYRVLEDLG 178
Cdd:COG1893 5 ILGAGAIGGLLGARLARAGHDVTLVAR----GAHA--EALRENGLRLESPDG 50
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
125-292 |
7.32e-03 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 38.81 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 125 VIIVGSGVLGSALAAVLsRDGR---KVTVIERDLKEP--DRIVGEFLQPGGYRVLEDLGLKDAVEDiDAQVVDGYIIHDQ 199
Cdd:PRK07333 4 VVIAGGGYVGLALAVAL-KQAAphlPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAP-EAQPITDMVITDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545520806 200 DSKSEVQiPYPVSENSQVRSGRAFHH----GRFIMGLRKAAMAEpNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeL 275
Cdd:PRK07333 82 RTSDPVR-PVFLTFEGEVEPGEPFAHmvenRVLINALRKRAEAL-GIDLREATSVTDFETRDEGVTVTLSDGSV-----L 154
|
170
....*....|....*..
gi 545520806 276 HAPLTVVADGLFSKFRK 292
Cdd:PRK07333 155 EARLLVAADGARSKLRE 171
|
|
|