|
Name |
Accession |
Description |
Interval |
E-value |
| SE |
pfam08491 |
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ... |
219-490 |
1.86e-156 |
|
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: 446.39 E-value: 1.86e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 219 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGE-MPR- 296
Cdd:pfam08491 1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 297 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 373
Cdd:pfam08491 81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 374 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 767953485 454 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 490
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
65-514 |
9.68e-131 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 391.52 E-value: 9.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 143
Cdd:PTZ00367 33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 144 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 214
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 215 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 275
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 276 IYQISSSETRVLVDIRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 351
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 352 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 422
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 423 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 482
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499
|
490 500 510
....*....|....*....|....*....|..
gi 767953485 483 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 514
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
63-432 |
2.75e-23 |
|
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: 100.40 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 142
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 221
Cdd:COG0654 80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDIRGEmprnlrey 301
Cdd:COG0654 151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 302 mVEKIYPQIPDHLKEpFLEATDNSHLRSmpASFLPPSSVKKRgVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 379
Cdd:COG0654 188 -LRARLAAAGPRLGE-LLELSPRSAFPL--RRRRAERWRRGR-VVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 380 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 432
Cdd:COG0654 262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
64-369 |
3.06e-15 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 77.64 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 142
Cdd:PRK07045 4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 211
Cdd:PRK07045 84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 212 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 287
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 288 V-----DIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 362
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304
|
....*..
gi 767953485 363 MTVAFKD 369
Cdd:PRK07045 305 MNLAIED 311
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
68-97 |
2.23e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 49.90 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
67-233 |
2.65e-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: 49.32 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 106
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 107 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 180
Cdd:pfam01266 81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767953485 181 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 233
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
67-430 |
1.52e-05 |
|
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
Pssm-ID: 273914 [Multi-domain] Cd Length: 437 Bit Score: 47.44 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 129
Cdd:TIGR01989 2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 130 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 203
Cdd:TIGR01989 81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 204 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 258
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 259 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDIRGEMPR-NLREYMVEKIY 307
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 308 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 377
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 767953485 378 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 430
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
|
|
| mannonate_red_SDR_c |
cd08935 |
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ... |
64-113 |
8.28e-03 |
|
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: 38.21 E-value: 8.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767953485 64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:cd08935 5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG 54
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SE |
pfam08491 |
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ... |
219-490 |
1.86e-156 |
|
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: 446.39 E-value: 1.86e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 219 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGE-MPR- 296
Cdd:pfam08491 1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 297 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 373
Cdd:pfam08491 81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 374 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 767953485 454 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 490
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
65-514 |
9.68e-131 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 391.52 E-value: 9.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 143
Cdd:PTZ00367 33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 144 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 214
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 215 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 275
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 276 IYQISSSETRVLVDIRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 351
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 352 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 422
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 423 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 482
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499
|
490 500 510
....*....|....*....|....*....|..
gi 767953485 483 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 514
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
|
|
| PLN02985 |
PLN02985 |
squalene monooxygenase |
67-473 |
3.08e-106 |
|
squalene monooxygenase
Pssm-ID: 178566 [Multi-domain] Cd Length: 514 Bit Score: 326.86 E-value: 3.08e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHdqESKS 146
Cdd:PLN02985 45 DVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVY--KDGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 147 EVQIPYPLSENN--QVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELhAPLTV 224
Cdd:PLN02985 123 EAVAPFPVDNNNfpYEPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTAL-APLTV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 225 VADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDI---------RGEMP 295
Cdd:PLN02985 202 VCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTMLYQISSTDVRCVFEVlpdnipsiaNGEMS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 296 rnlrEYMVEKIYPQIPDHLKEPFLEATDN-SHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWR 374
Cdd:PLN02985 282 ----TFVKNTIAPQVPPKLRKIFLKGIDEgAHIKVVPTKRMSATLSDKKGVIVLGDAFNMRHPAIASGMMVLLSDILILR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 375 KLLKGIPDLYDDAAIFEAKKSFYWARKtSHSFVVNILAQALYE-LFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:PLN02985 358 RLLQPLSNLGNANKVSEVIKSFYDIRK-PMSATVNTLGNAFSQvLVASTDEAKEAMRQGCYDYLCSGGFRTSGMMALLGG 436
|
410 420
....*....|....*....|
gi 767953485 454 LSPNPLVLIGHFFAVAIYAV 473
Cdd:PLN02985 437 MNPRPLSLIYHLCAITLSSI 456
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
63-432 |
2.75e-23 |
|
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: 100.40 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 142
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 221
Cdd:COG0654 80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDIRGEmprnlrey 301
Cdd:COG0654 151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 302 mVEKIYPQIPDHLKEpFLEATDNSHLRSmpASFLPPSSVKKRgVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 379
Cdd:COG0654 188 -LRARLAAAGPRLGE-LLELSPRSAFPL--RRRRAERWRRGR-VVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 380 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 432
Cdd:COG0654 262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
73-368 |
1.32e-17 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 83.09 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 73 AGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEgldaQVVNGYMIHDQeSKSEVQIPY 152
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSP-GGKSVELPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 153 PLSENNQVQsgRAfhhgRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMgVqykdkETGDIKELHAPLTVVADGLFS 231
Cdd:COG0644 76 GRGGGYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 232 KFRKSLVSNKVSVSSHFVGFLMKnapqfkanhaelilanpspvliyqissseTRVLVDIRGEMPRNLREYMVEKIYPQ-- 309
Cdd:COG0644 143 LLARKLGLKRRSDEPQDYALAIK-----------------------------EHWELPPLEGVDPGAVEFFFGEGAPGgy 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953485 310 ---IPdhlkepfleATDNSHLRSMPASFLPPSSVkKRGVLLLGDAYNMRHPLTGGGMTVAFK 368
Cdd:COG0644 194 gwvFP---------LGDGRVSVGIPLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIHLAMK 245
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
64-369 |
3.06e-15 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 77.64 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 142
Cdd:PRK07045 4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 211
Cdd:PRK07045 84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 212 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 287
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 288 V-----DIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 362
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304
|
....*..
gi 767953485 363 MTVAFKD 369
Cdd:PRK07045 305 MNLAIED 311
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
67-236 |
6.96e-13 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 70.27 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIE------RDLKepdrivGEFLQPGGYHVLKDLGLGDTVEGLDaqvvngymiH 140
Cdd:PRK06185 8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDFR------GDTVHPSTLELMDELGLLERFLELP---------H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSEVQIPyplseNNQVQS---GRAFHHGRFIM---------SLRKAAMAEPNAKFIEGV-VLQLLEEDDVVMGVQY 207
Cdd:PRK06185 73 QKVRTLRFEIG-----GRTVTLadfSRLPTPYPYIAmmpqwdfldFLAEEASAYPNFTLRMGAeVTGLIEEGGRVTGVRA 147
|
170 180
....*....|....*....|....*....
gi 767953485 208 KDKEtGDIkELHAPLTVVADGLFSKFRKS 236
Cdd:PRK06185 148 RTPD-GPG-EIRADLVVGADGRHSRVRAL 174
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
62-249 |
6.19e-12 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 67.37 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIErdlkEPDRIvGEF-----LQPGGYHVLKDLGLGDTVEGLdaQVVNG 136
Cdd:PRK08163 1 MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLE----QAAEI-GEIgagiqLGPNAFSALDALGVGEAARQR--AVFTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 137 YMI-HDQESKSEV-QIPyplsennqvqSGRAF-----------HHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDD--V 201
Cdd:PRK08163 74 HLTmMDAVDAEEVvRIP----------TGQAFrarfgnpyaviHRADIHLSLLEAVLDHPLVEFRTSTHVVGIEQDGdgV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767953485 202 VMGVQYKDKETGDIkelhaplTVVADGLFSKFRKSLVSNKVSVSSHFV 249
Cdd:PRK08163 144 TVFDQQGNRWTGDA-------LIGCDGVKSVVRQSLVGDAPRVTGHVV 184
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
65-369 |
3.66e-11 |
|
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: 64.65 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIV---GEFLQPGGYHVLKDLGLGDTVegLDAQVVNGYMIHd 141
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERH---ATTSVlprAHGLNQRTMELLRQAGLEDRI--LAEGVPHEGMGL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 142 qesksEVQIPYPLSENNQVQSGRAFH---HGRFIMSLRKAAMAEPnAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKEL 218
Cdd:pfam01494 75 -----AFYNTRRRADLDFLTSPPRVTvypQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRDRRDGEEYTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 219 HAPLTVVADGLFSKFRKSL---VSNKVSVSSHFVG--FLMKNAPQFKANHA--ELILANPSPVLIYQISSSETR---VLV 288
Cdd:pfam01494 149 RAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDvlFDAPDLSDPVERAFvhYLIYAPHSRGFMVGPWRSAGReryYVQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 289 DIRGEMPRNLREymvekiyPQIPDHLKEPFLEAT--DNSHLRSMPASFLPpssVKKR--------GVLLLGDAYNmRHPL 358
Cdd:pfam01494 229 VPWDEEVEERPE-------EFTDEELKQRLRSIVgiDLALVEILWKSIWG---VASRvatryrkgRVFLAGDAAH-IHPP 297
|
330
....*....|..
gi 767953485 359 TGG-GMTVAFKD 369
Cdd:pfam01494 298 TGGqGLNTAIQD 309
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
68-237 |
1.98e-06 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 49.94 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD----LKEPD---RIVGefLQPGGYHVLKDLGLGDTVEG------LDAQVV 134
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQplaaLADPAfdgREIA--LTHASREILQRLGAWDRIPEdeisplRDAKVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 135 NG---YMIH-DQESKSEVQIPYpLSENNQVQsgRAfhhgrfimsLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDK 210
Cdd:PRK09126 84 NGrspFALTfDARGRGADALGY-LVPNHLIR--RA---------AYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANG 151
|
170 180
....*....|....*....|....*..
gi 767953485 211 ETgdikeLHAPLTVVADGLFSKFRKSL 237
Cdd:PRK09126 152 RR-----LTARLLVAADSRFSATRRQL 173
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
68-97 |
2.23e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 49.90 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
67-233 |
2.65e-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: 49.32 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 106
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 107 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 180
Cdd:pfam01266 81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767953485 181 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 233
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
68-363 |
4.20e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 49.10 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTV-------EGLDAQVVNGYMIH 140
Cdd:PRK06847 7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECleagfgfDGVDLFDPDGTLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSEVQIPYPlsenNQVQSGR-AFHHgrfImsLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETGdikelH 219
Cdd:PRK06847 87 ELPTPRLAGDDLP----GGGGIMRpALAR---I--LADAARAA-GADVRLGTTVTAIEQDDDGVTVTFSDGTTG-----R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 220 APLTVVADGLFSKFRKSLVSNK--------------VSVSSHFVGFLMKNAPQFKANhaelilANP-SPVLIYQ--ISSS 282
Cdd:PRK06847 152 YDLVVGADGLYSKVRSLVFPDEpepeytgqgvwravLPRPAEVDRSLMYLGPTTKAG------VVPlSEDLMYLfvTEPR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 283 ETRVLVDiRGEMPRNLREYMVEKIYPQIPDhLKEPfleATDNSHL--RSMPASFLPPSSVKKRgVLLLGDAYnmrHPLT- 359
Cdd:PRK06847 226 PDNPRIE-PDTLAALLRELLAPFGGPVLQE-LREQ---ITDDAQVvyRPLETLLVPAPWHRGR-VVLIGDAA---HATTp 296
|
....*...
gi 767953485 360 ----GGGM 363
Cdd:PRK06847 297 hlaqGAGM 304
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
68-125 |
7.93e-06 |
|
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: 47.75 E-value: 7.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHV----------LKDLGLGDT 125
Cdd:COG0569 98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD---PERV--ERLAEEDVLVivgdatdeevLEEAGIEDA 160
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
67-430 |
1.52e-05 |
|
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
Pssm-ID: 273914 [Multi-domain] Cd Length: 437 Bit Score: 47.44 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 129
Cdd:TIGR01989 2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 130 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 203
Cdd:TIGR01989 81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 204 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 258
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 259 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDIRGEMPR-NLREYMVEKIY 307
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 308 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 377
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 767953485 378 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 430
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
62-102 |
3.48e-05 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 46.29 E-value: 3.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767953485 62 SQNDPEVIIVGAGVLGSALAAVLSR-DGRKVTVIErdlKEPD 102
Cdd:COG0579 1 MMEMYDVVIIGAGIVGLALARELSRyEDLKVLVLE---KEDD 39
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
68-136 |
3.63e-05 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 46.27 E-value: 3.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQpggyhvlkdlglgdtvEGLDAQVVNG 136
Cdd:PRK09496 3 IIIVGAGQVGYTLAENLSGENNDVTVIDTD---EERL--RRLQ----------------DRLDVRTVVG 50
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
68-250 |
5.58e-05 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 45.50 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIER--DLKEPDRIVgEFLQPgGYHVLKDLGLGDTVEGLDAQVVNgymIHDQESK 145
Cdd:PRK07588 3 VAISGAGIAGPTLAYWLRRYGHEPTLIERapELRTGGYMV-DFWGV-GYEVAKRMGITDQLREAGYQIEH---VRSVDPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 146 SEVqipyplSENNQVQSGRAFHHGRFImSLRKAAMAEPNAKFIEGVVLQLL---------EEDDVVMGVQYKDKETGDik 216
Cdd:PRK07588 78 GRR------KADLNVDSFRRMVGDDFT-SLPRGDLAAAIYTAIDGQVETIFddsiatideHRDGVRVTFERGTPRDFD-- 148
|
170 180 190
....*....|....*....|....*....|....
gi 767953485 217 elhapLTVVADGLFSKFRkSLVSNKVSVSSHFVG 250
Cdd:PRK07588 149 -----LVIGADGLHSHVR-RLVFGPERDFEHYLG 176
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
70-136 |
7.05e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 45.26 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 70 IVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVG-----EFlqpGG------YH-----------VLKDLGLGDTV- 126
Cdd:PRK07233 4 IVGGGIAGLAAAYRLAKRGHEVTVFEAD----DQLGGlaasfEF---GGlpierfYHhifksdealleLLDELGLEDKLr 76
|
90
....*....|..
gi 767953485 127 --EGLDAQVVNG 136
Cdd:PRK07233 77 wrETKTGYYVDG 88
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
68-132 |
9.04e-05 |
|
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: 44.42 E-value: 9.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyHVLKDLG----LGDTVEGLDAQ 132
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLE----EELREHGvelrLGETVVAIDGD 194
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
70-96 |
9.23e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.59 E-value: 9.23e-05
10 20
....*....|....*....|....*..
gi 767953485 70 IVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
|
|
| PRK06184 |
PRK06184 |
hypothetical protein; Provisional |
63-155 |
1.09e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235728 [Multi-domain] Cd Length: 502 Bit Score: 44.59 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERdLKEP---DRivGEFLQPGGYHVLKDLGLGDTVEGL---------- 129
Cdd:PRK06184 1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEK-APEPfpgSR--GKGIQPRTQEVFDDLGVLDRVVAAgglyppmriy 77
|
90 100
....*....|....*....|....*...
gi 767953485 130 --DAQVVNGYMIHDQESKSEvqIPYPLS 155
Cdd:PRK06184 78 rdDGSVAESDMFAHLEPTPD--EPYPLP 103
|
|
| ubiF |
PRK08020 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed |
62-235 |
1.74e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
Pssm-ID: 181199 [Multi-domain] Cd Length: 391 Bit Score: 43.82 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDL-------KEPD-RIVGefLQPGGYHVLKDLGLGDTVEGL---- 129
Cdd:PRK08020 2 TNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAApapfdadSQPDvRISA--ISAASVALLKGLGVWDAVQAMrshp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 130 ----------DAQVVN----------GYMIhdqesksevqipyplsENNQVQsgrafhhgrfiMSLRKAAMAEPNAKFIE 189
Cdd:PRK08020 80 yrrletweweTAHVVFdaaelklpelGYMV----------------ENRVLQ-----------LALWQALEAHPNVTLRC 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767953485 190 GVVLQLLEEDDVVMGVQYKDKEtgdikELHAPLTVVADGLFSKFRK 235
Cdd:PRK08020 133 PASLQALQRDDDGWELTLADGE-----EIQAKLVIGADGANSQVRQ 173
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
67-97 |
1.98e-04 |
|
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: 44.07 E-value: 1.98e-04
10 20 30
....*....|....*....|....*....|.
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
58-237 |
2.15e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 43.74 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 58 TSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGeflQPGGYH-------VLKDLGLGDTVeGLD 130
Cdd:PRK06183 3 AQHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW----PTLYD---LPRAVGiddealrVLQAIGLADEV-LPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 131 AQVVNGYMIHDQESKSEVQIPYPlsennqvqSGRafHHG---RFIMS-------LRKAAMAEPNAKFIEGV-VLQLLEED 199
Cdd:PRK06183 75 TTPNHGMRFLDAKGRCLAEIARP--------STG--EFGwprRNAFHqplleavLRAGLARFPHVRVRFGHeVTALTQDD 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 767953485 200 DVVMgVQYKDkETGDIKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK06183 145 DGVT-VTLTD-ADGQRETVRARYVVGCDGANSFVRRTL 180
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
68-110 |
2.83e-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: 425450 [Multi-domain] Cd Length: 80 Bit Score: 39.49 E-value: 2.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIER---DLKEPDRIVGEFLQ 110
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERrdrLLPGFDPEIAKILQ 47
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
68-117 |
3.00e-04 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 40.59 E-value: 3.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGrKVTVIERDlkePDRIvgEFLQPGGYHVL 117
Cdd:pfam02254 1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKD---EERV--EELREEGVPVV 44
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
68-237 |
3.85e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 42.96 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIE--RDLKEPDriVGEFLQPGGYHVLKDLGLGDTvegLDAQVVNGYMI-----H 140
Cdd:PRK07538 3 VLIAGGGIGGLTLALTLHQRGIEVVVFEaaPELRPLG--VGINLLPHAVRELAELGLLDA---LDAIGIRTRELayfnrH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSE---VQIPYPLSennQVqsgrAFHHGRFIMSLRKAAMAEPNAKFIE---GVVLQLLEEDDVVMGVQykDKETGD 214
Cdd:PRK07538 78 GQRIWSEprgLAAGYDWP---QY----SIHRGELQMLLLDAVRERLGPDAVRtghRVVGFEQDADVTVVFLG--DRAGGD 148
|
170 180
....*....|....*....|...
gi 767953485 215 IKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK07538 149 LVSVRGDVLIGADGIHSAVRAQL 171
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
68-113 |
4.01e-04 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 42.19 E-value: 4.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:PRK08277 14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
|
|
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
68-96 |
6.37e-04 |
|
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: 42.51 E-value: 6.37e-04
10 20 30
....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRD-GRKVTVIER 96
Cdd:COG2303 7 YVIVGAGSAGCVLANRLSEDaGLRVLLLEA 36
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
68-121 |
6.74e-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: 6.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIE---RDLKEPDRIVGEFLQpggyHVLKDLG 121
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEaldRLLRAFDEEISAALE----KALEKNG 207
|
|
| PRK10157 |
PRK10157 |
putative oxidoreductase FixC; Provisional |
67-250 |
7.37e-04 |
|
putative oxidoreductase FixC; Provisional
Pssm-ID: 182273 [Multi-domain] Cd Length: 428 Bit Score: 41.82 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIV--GEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIhdqeS 144
Cdd:PRK10157 7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVtgGRLYAHSLEHIIPGFADSAPVERLITHEKLAFMT----E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 145 KSEVQIPYpLSENNQVQSGRAFH--HGRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMGVQykdkETGDIKElhAP 221
Cdd:PRK10157 83 KSAMTMDY-CNGDETSPSQRSYSvlRSKFDAWLMEQA-EEAGAQLITGIrVDNLVQRDGKVVGVE----ADGDVIE--AK 154
|
170 180 190
....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSL-VSNKVSVSSHFVG 250
Cdd:PRK10157 155 TVILADGVNSILAEKLgMAKRVKPTDVAVG 184
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
68-96 |
8.43e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 41.76 E-value: 8.43e-04
10 20
....*....|....*....|....*....
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEK 34
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
68-117 |
9.19e-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: 9.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHVL 117
Cdd:COG1226 127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLD---PERV--EELRRFGIKVY 171
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
68-130 |
1.06e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 41.28 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQpggyHVLKDLG----LGDTVEGLD 130
Cdd:COG1251 145 VVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLlprqldeeAGALLQ----RLLEALGvevrLGTGVTEIE 211
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
67-96 |
1.07e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 41.32 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:PRK00711 2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
68-108 |
1.54e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 40.93 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIVGEF 108
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSRLGVKVTVFER----GDRILPLE 208
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
70-126 |
1.81e-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: 40.61 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485 70 IVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIvgEFLQPGGYHVLKDLGLGDTV 126
Cdd:COG1893 5 ILGAGAIGGLLGARLARAGHDVTLVAR----GAHA--EALRENGLRLESPDGDRTTV 55
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
62-97 |
2.36e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 40.55 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|....*.
gi 767953485 62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG3573 2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQE 37
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
66-108 |
2.51e-03 |
|
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: 40.46 E-value: 2.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767953485 66 PE-VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGEF 108
Cdd:COG1249 168 PKsLVVIGGGYIGLEFAQIFARLGSEVTLVERG----DRLLPGE 207
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
68-235 |
3.64e-03 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 39.58 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLsRDGR---KVTVIERDLKEP--DRIVGEFLQPGGYHVLKDLGLGDTVEGlDAQVVNGYMIHDQ 142
Cdd:PRK07333 4 VVIAGGGYVGLALAVAL-KQAAphlPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAP-EAQPITDMVITDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEVQiPYPLSENNQVQSGRAFHH----GRFIMSLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeL 218
Cdd:PRK07333 82 RTSDPVR-PVFLTFEGEVEPGEPFAHmvenRVLINALRKRAEAL-GIDLREATSVTDFETRDEGVTVTLSDGSV-----L 154
|
170
....*....|....*..
gi 767953485 219 HAPLTVVADGLFSKFRK 235
Cdd:PRK07333 155 EARLLVAADGARSKLRE 171
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
58-95 |
4.03e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 39.62 E-value: 4.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 767953485 58 TSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE 95
Cdd:PRK07364 11 LPSTRSLTYDVAIVGGGIVGLTLAAALKDSGLRIALIE 48
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
67-237 |
4.50e-03 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 39.37 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKE------PDRIVGEfLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH 140
Cdd:PRK08850 6 DVAIIGGGMVGLALAAALKESDLRIAVIEGQLPEealnelPDVRVSA-LSRSSEHILRNLGAWQGIEARRAAPYIAMEVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESksevqipyplsennqvqsgraFHHGRFimslRKAAMAEPN-AKFIEGVVLQL------LEEDDVVM-------GVQ 206
Cdd:PRK08850 85 EQDS---------------------FARIEF----DAESMAQPDlGHIVENRVIQLalleqvQKQDNVTLlmparcqSIA 139
|
170 180 190
....*....|....*....|....*....|....*
gi 767953485 207 YKDKET----GDIKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK08850 140 VGESEAwltlDNGQALTAKLVVGADGANSWLRRQM 174
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
66-96 |
4.52e-03 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 39.09 E-value: 4.52e-03
10 20 30
....*....|....*....|....*....|.
gi 767953485 66 PEVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEK 34
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
64-97 |
4.60e-03 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 39.21 E-value: 4.60e-03
10 20 30
....*....|....*....|....*....|....*
gi 767953485 64 NDPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERD 97
Cdd:PRK07688 23 REKHVLIIGAGALGTANAEMLVRAGvGKVTIVDRD 57
|
|
| Sacchrp_dh_NADP |
pfam03435 |
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
68-105 |
5.34e-03 |
|
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 36.80 E-value: 5.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767953485 68 VIIVGAGVLGSALAAVLSRDG--RKVTVIERDLKEPDRIV 105
Cdd:pfam03435 1 VLIIGAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALA 40
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
69-98 |
5.71e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 39.03 E-value: 5.71e-03
10 20 30
....*....|....*....|....*....|
gi 767953485 69 IIVGAGVLGSALAAVLSRDGRKVTVIERDL 98
Cdd:PRK06370 9 IVIGAGQAGPPLAARAAGLGMKVALIERGL 38
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
43-95 |
5.91e-03 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 39.14 E-value: 5.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767953485 43 GTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE 95
Cdd:PRK09754 122 GERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIE 174
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
66-124 |
6.15e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 39.05 E-value: 6.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953485 66 PEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQPGGYHV-----------LKDLGLGD 124
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS----DRVgglirtveVDGFRIDRGPHSfltrdpevlelLRELGLGD 75
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
67-205 |
6.35e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.22 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 67 EVIIVGAGVLGSALAAVLSRD-GRKVTVIERDLkepdrivgeflQPGGyhvlkdlGLGdtvegLDAQVVNgYMIHDQESK 145
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSV-----------SPGG-------GAW-----LGGQLFS-AMVVRKPAH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 146 ---SEVQIPYPLSENNQVQSgrafHHGRFIMSLRKAAMAEPNAKFIEGVVLQ--LLEEDDVVMGV 205
Cdd:pfam01946 75 lflDEFGIPYEDEGDYVVVK----HAALFTSTLMSKALQLPNVKLFNATSVEdlIVRPGVGVAGV 135
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
59-131 |
6.41e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 39.12 E-value: 6.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953485 59 STSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPgGYHVLKDLGLGDTVEGLDA 131
Cdd:PRK07494 1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGP-SIRFLERLGLWARLAPHAA 72
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
60-96 |
6.81e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 39.08 E-value: 6.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 767953485 60 TSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
68-130 |
6.87e-03 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 38.74 E-value: 6.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485 68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLG----LGDTVEGLD 130
Cdd:PRK04965 144 VLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGvhllLKSQLQGLE 210
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
60-97 |
7.22e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 38.75 E-value: 7.22e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767953485 60 TSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE-RD 97
Cdd:COG1231 2 SRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD 40
|
|
| PRK12475 |
PRK12475 |
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
65-100 |
8.22e-03 |
|
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 38.56 E-value: 8.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 767953485 65 DPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERDLKE 100
Cdd:PRK12475 24 EKHVLIVGAGALGAANAEALVRAGiGKLTIADRDYVE 60
|
|
| mannonate_red_SDR_c |
cd08935 |
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ... |
64-113 |
8.28e-03 |
|
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: 38.21 E-value: 8.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767953485 64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:cd08935 5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG 54
|
|
|