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Conserved domains on  [gi|350632776|gb|EHA21143|]
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hypothetical protein ASPNIDRAFT_213409 [Aspergillus niger ATCC 1015]

Protein Classification

FAD-dependent phenol hydoxylase family protein( domain architecture ID 1008557)

FAD-dependent phenol hydoxylase (PHOX) family protein is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen

EC:  1.14.13.-
Gene Ontology:  GO:0006725

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK08294 super family cl35676
phenol 2-monooxygenase; Provisional
7-622 6.14e-119

phenol 2-monooxygenase; Provisional


The actual alignment was detected with superfamily member PRK08294:

Pssm-ID: 236223 [Multi-domain]  Cd Length: 634  Bit Score: 367.78  E-value: 6.14e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   7 EKYDIVIVGAGPVGIVLSLCMSRW-GYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDVAFWDP 85
Cdd:PRK08294  31 DEVDVLIVGCGPAGLTLAAQLSAFpDITTRIVERKPGRLELGQADGIACRTMEMFQAFGFAERILK-EAYWINETAFWKP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LPGGQD-IHRTGswpscpRFIDT-----RYPFTtLVHQGKIERVFLDEIQKAGTTVErP---WTIVGFKNDGlDETYPVE 156
Cdd:PRK08294 110 DPADPStIVRTG------RVQDTedglsEFPHV-IVNQARVHDYFLDVMRNSPTRLE-PdygREFVDLEVDE-EGEYPVT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 157 VQLKSID---TNVIETVRTKYLFSGEGARSFIRQQLGIQIQyKDPISYVWGVMDGVVRTNFPDIETKCTIHS-DAGSIMV 232
Cdd:PRK08294 181 VTLRRTDgehEGEEETVRAKYVVGCDGARSRVRKAIGRELR-GDSANHAWGVMDVLAVTDFPDIRLKCAIQSaSEGSILL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 233 IPREDN-MVRLYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEWDRVEWYSVYPIGQGISEKY---------TLD 302
Cdd:PRK08294 260 IPREGGyLVRLYVDLGEVPPDERVAVRNTTVEEVIAKAQRILHPYTLDVKEVAWWSVYEVGQRLTDRFddvpaeeagTRL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 303 ERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKrRPTA 382
Cdd:PRK08294 340 PRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIAQELIDFDREWSTMMAA-PPKE 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 383 GEVGEASHTtaaaggeEDEFVKTfkssCEFTSGYGVAYKPNVFTWDATHPAQSPLFDVpgvrltpGRAFTPTTVTRLADS 462
Cdd:PRK08294 419 GGGVDPAEL-------QDYFVKH----GRFTAGTATHYAPSLLTGEATHQDLATGFPI-------GKRFHSAPVIRLADA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 463 NHVHLEQEIPANGAFRIFIFAGKQDKTSK--AITDLAANLEK-ERSFLSVYRR--ADIADVsffenhlphsklFSICLVY 537
Cdd:PRK08294 481 KPVHLGHAATADGRWRIYAFADAADPAGPgsALDALCEFLAEsPDSPLRRFTPsgADIDAV------------IDVRAIF 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 538 AGEKNQIDVDSIPKI---------LRDYHHHLYAD----NIPDVRvpqatyaaheklGFDVEKGGVVVTRPDSHVACTIQ 604
Cdd:PRK08294 549 QQPHRELDLEDVPALllprkgrfgLTDYEKVFCADlsgaDIFDLR------------GIDRDRGAVVVVRPDQYVANVLP 616
                        650
                 ....*....|....*...
gi 350632776 605 LSEgsgtVDALNAFFGSF 622
Cdd:PRK08294 617 LDA----HAELAAFFAGF 630
 
Name Accession Description Interval E-value
PRK08294 PRK08294
phenol 2-monooxygenase; Provisional
7-622 6.14e-119

phenol 2-monooxygenase; Provisional


Pssm-ID: 236223 [Multi-domain]  Cd Length: 634  Bit Score: 367.78  E-value: 6.14e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   7 EKYDIVIVGAGPVGIVLSLCMSRW-GYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDVAFWDP 85
Cdd:PRK08294  31 DEVDVLIVGCGPAGLTLAAQLSAFpDITTRIVERKPGRLELGQADGIACRTMEMFQAFGFAERILK-EAYWINETAFWKP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LPGGQD-IHRTGswpscpRFIDT-----RYPFTtLVHQGKIERVFLDEIQKAGTTVErP---WTIVGFKNDGlDETYPVE 156
Cdd:PRK08294 110 DPADPStIVRTG------RVQDTedglsEFPHV-IVNQARVHDYFLDVMRNSPTRLE-PdygREFVDLEVDE-EGEYPVT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 157 VQLKSID---TNVIETVRTKYLFSGEGARSFIRQQLGIQIQyKDPISYVWGVMDGVVRTNFPDIETKCTIHS-DAGSIMV 232
Cdd:PRK08294 181 VTLRRTDgehEGEEETVRAKYVVGCDGARSRVRKAIGRELR-GDSANHAWGVMDVLAVTDFPDIRLKCAIQSaSEGSILL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 233 IPREDN-MVRLYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEWDRVEWYSVYPIGQGISEKY---------TLD 302
Cdd:PRK08294 260 IPREGGyLVRLYVDLGEVPPDERVAVRNTTVEEVIAKAQRILHPYTLDVKEVAWWSVYEVGQRLTDRFddvpaeeagTRL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 303 ERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKrRPTA 382
Cdd:PRK08294 340 PRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIAQELIDFDREWSTMMAA-PPKE 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 383 GEVGEASHTtaaaggeEDEFVKTfkssCEFTSGYGVAYKPNVFTWDATHPAQSPLFDVpgvrltpGRAFTPTTVTRLADS 462
Cdd:PRK08294 419 GGGVDPAEL-------QDYFVKH----GRFTAGTATHYAPSLLTGEATHQDLATGFPI-------GKRFHSAPVIRLADA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 463 NHVHLEQEIPANGAFRIFIFAGKQDKTSK--AITDLAANLEK-ERSFLSVYRR--ADIADVsffenhlphsklFSICLVY 537
Cdd:PRK08294 481 KPVHLGHAATADGRWRIYAFADAADPAGPgsALDALCEFLAEsPDSPLRRFTPsgADIDAV------------IDVRAIF 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 538 AGEKNQIDVDSIPKI---------LRDYHHHLYAD----NIPDVRvpqatyaaheklGFDVEKGGVVVTRPDSHVACTIQ 604
Cdd:PRK08294 549 QQPHRELDLEDVPALllprkgrfgLTDYEKVFCADlsgaDIFDLR------------GIDRDRGAVVVVRPDQYVANVLP 616
                        650
                 ....*....|....*...
gi 350632776 605 LSEgsgtVDALNAFFGSF 622
Cdd:PRK08294 617 LDA----HAELAAFFAGF 630
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
8-368 2.17e-59

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: 202.56  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776    8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWDPLP 87
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYNTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   88 GGQDIHrtgswpscprfIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGldetYPVEVQLKSIDTNVI 167
Cdd:pfam01494  81 RRADLD-----------FLTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSLEQDG----DGVTAVVRDRRDGEE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  168 ETVRTKYLFSGEGARSFIRQQLGIQIQYKDPISyvWGVMDGVVRT-NFPDIETKCTIH-----SDAGSIMVIPREDNMVR 241
Cdd:pfam01494 146 YTVRAKYLVGCDGGRSPVRKTLGIEFEGFEGVP--FGSLDVLFDApDLSDPVERAFVHyliyaPHSRGFMVGPWRSAGRE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  242 LYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEwDRVEWYSVYPIGQGISEKYTLDeRVFMGGDACHTHSPKAGQ 321
Cdd:pfam01494 224 RYYVQVPWDEEVEERPEEFTDEELKQRLRSIVGIDLAL-VEILWKSIWGVASRVATRYRKG-RVFLAGDAAHIHPPTGGQ 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 350632776  322 GMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFD 368
Cdd:pfam01494 302 GLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
6-382 3.92e-50

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: 177.05  E-value: 3.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   6 QEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDVAFWDP 85
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLA-RGAPIRGIRVRDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LPGGQdIHRTgswpscpRFIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGldetYPVEVQLKSidtn 165
Cdd:COG0654   80 SDGRV-LARF-------DAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTGLEQDA----DGVTVTLAD---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 166 vIETVRTKYLFSGEGARSFIRQQLGIQIQYKD-PISYVWGVMDGVVRTNFPDietkctIHSDAGSIMviprednmvrlyv 244
Cdd:COG0654  144 -GRTLRADLVVGADGARSAVRRLLGIGFTGRDyPQRALWAGVRTELRARLAA------AGPRLGELL------------- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 245 qiassddpdfdprktataedvqatarkilqpywvewdRVEWYSVYPIGQGISEKYTlDERVFMGGDACHTHSPKAGQGMN 324
Cdd:COG0654  204 -------------------------------------ELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGAN 245
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 350632776 325 TAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKRRPTA 382
Cdd:COG0654  246 LALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADALGRLFHPDSPPL 303
PHOX_C cd02979
FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of ...
448-622 7.65e-38

FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of proteins similar to PHOX from the aerobic topsoil yeast Trichosporon cutaneum. PHOX is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen. This is the first step in the biodegradation and detoxification of phenolic compounds. PHOX contains three domains. The substrate and FAD/NAD(P) binding sites are contained in the first two domains, which adopt a complicated folding pattern. The third or C-terminal domain contains a TRX fold and is involved in dimerization. The functional unit of PHOX is a dimer, although active tetramers of the recombinant enzyme can be isolated when overproduced in bacteria.


Pssm-ID: 239277 [Multi-domain]  Cd Length: 167  Bit Score: 137.80  E-value: 7.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 448 GRAFTPTTVTRLADSNHVHLEQEIPANGAFRIFIFAGKQDK--TSKAITDLAANLEKERSFLSVYRRAdiadvsffenHL 525
Cdd:cd02979    1 GRRFPSAPVVRQADALPVHLGHRLPADGRFRIYVFAGDIAPaqQKSRLTQLCDALDSPDSFPLRYTPR----------GA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 526 PHSKLFSICLVYAGEKNQIDVDSIPKILR-------DYHHHLYADnipDVRVPQATYAAHEKLGFDVEKGGVVVTRPDSH 598
Cdd:cd02979   71 DPDSVFDVVTIHAAPRREIELLDLPAVLRpfgekkgWDYEKIYAD---DDSYHEGHGDAYEKYGIDPERGAVVVVRPDQY 147
                        170       180
                 ....*....|....*....|....
gi 350632776 599 VACTIQLsegsGTVDALNAFFGSF 622
Cdd:cd02979  148 VALVGPL----DDVEALEAYFAGF 167
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
10-380 4.09e-15

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 77.63  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPV-----PTATGRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWD 84
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARSGLKVALIEATPLpapadPGFDNRVSALSAASIRLLEKLGVWDKIEPARAQPIRDIHVSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   85 PLPGGQ------DIHRTgswpscprfidtryPFTTLVHQGKIERVFLDEIQKA-GTTVERPWTIVGFKNDGlDEtypVEV 157
Cdd:TIGR01988  81 GGSFGAlrfdadEIGLE--------------ALGYVVENRVLQQALWERLQELpNVTLLCPARVVELPRHS-DH---VEL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  158 QLKSIDtnvieTVRTKYLFSGEGARSFIRQQLGIQIQYKDpisYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMVIPRED 237
Cdd:TIGR01988 143 TLDDGQ-----QLRARLLVGADGANSKVRQLAGIPTTGWD---YGQSAVVANVKHERPHQGTAWERFTPTGPLALLPLPD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  238 NMVRLyV---------QIASSDDPDFdprktaTAEdVQATARKILQPYWVEWDRvewySVYPIGQGISEKYtLDERVFMG 308
Cdd:TIGR01988 215 NRSSL-VwtlppeeaeRLLALSDEEF------LAE-LQRAFGSRLGAITLVGER----HAFPLSLTHAKRY-VAPRLALI 281
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350632776  309 GDACHTHSPKAGQGMNTAFHDALNMAWKLH-AVESG--LAKRSILSTYETERK-DIAETLLSFDnKYAALFSKRRP 380
Cdd:TIGR01988 282 GDAAHTIHPLAGQGLNLGLRDVAALAEVLEdARRRGedIGSLRVLQRYERRRRfDNAAMLGATD-GLNRLFSNDFP 356
 
Name Accession Description Interval E-value
PRK08294 PRK08294
phenol 2-monooxygenase; Provisional
7-622 6.14e-119

phenol 2-monooxygenase; Provisional


Pssm-ID: 236223 [Multi-domain]  Cd Length: 634  Bit Score: 367.78  E-value: 6.14e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   7 EKYDIVIVGAGPVGIVLSLCMSRW-GYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDVAFWDP 85
Cdd:PRK08294  31 DEVDVLIVGCGPAGLTLAAQLSAFpDITTRIVERKPGRLELGQADGIACRTMEMFQAFGFAERILK-EAYWINETAFWKP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LPGGQD-IHRTGswpscpRFIDT-----RYPFTtLVHQGKIERVFLDEIQKAGTTVErP---WTIVGFKNDGlDETYPVE 156
Cdd:PRK08294 110 DPADPStIVRTG------RVQDTedglsEFPHV-IVNQARVHDYFLDVMRNSPTRLE-PdygREFVDLEVDE-EGEYPVT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 157 VQLKSID---TNVIETVRTKYLFSGEGARSFIRQQLGIQIQyKDPISYVWGVMDGVVRTNFPDIETKCTIHS-DAGSIMV 232
Cdd:PRK08294 181 VTLRRTDgehEGEEETVRAKYVVGCDGARSRVRKAIGRELR-GDSANHAWGVMDVLAVTDFPDIRLKCAIQSaSEGSILL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 233 IPREDN-MVRLYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEWDRVEWYSVYPIGQGISEKY---------TLD 302
Cdd:PRK08294 260 IPREGGyLVRLYVDLGEVPPDERVAVRNTTVEEVIAKAQRILHPYTLDVKEVAWWSVYEVGQRLTDRFddvpaeeagTRL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 303 ERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKrRPTA 382
Cdd:PRK08294 340 PRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIAQELIDFDREWSTMMAA-PPKE 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 383 GEVGEASHTtaaaggeEDEFVKTfkssCEFTSGYGVAYKPNVFTWDATHPAQSPLFDVpgvrltpGRAFTPTTVTRLADS 462
Cdd:PRK08294 419 GGGVDPAEL-------QDYFVKH----GRFTAGTATHYAPSLLTGEATHQDLATGFPI-------GKRFHSAPVIRLADA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 463 NHVHLEQEIPANGAFRIFIFAGKQDKTSK--AITDLAANLEK-ERSFLSVYRR--ADIADVsffenhlphsklFSICLVY 537
Cdd:PRK08294 481 KPVHLGHAATADGRWRIYAFADAADPAGPgsALDALCEFLAEsPDSPLRRFTPsgADIDAV------------IDVRAIF 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 538 AGEKNQIDVDSIPKI---------LRDYHHHLYAD----NIPDVRvpqatyaaheklGFDVEKGGVVVTRPDSHVACTIQ 604
Cdd:PRK08294 549 QQPHRELDLEDVPALllprkgrfgLTDYEKVFCADlsgaDIFDLR------------GIDRDRGAVVVVRPDQYVANVLP 616
                        650
                 ....*....|....*...
gi 350632776 605 LSEgsgtVDALNAFFGSF 622
Cdd:PRK08294 617 LDA----HAELAAFFAGF 630
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
8-368 2.17e-59

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: 202.56  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776    8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWDPLP 87
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYNTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   88 GGQDIHrtgswpscprfIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGldetYPVEVQLKSIDTNVI 167
Cdd:pfam01494  81 RRADLD-----------FLTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSLEQDG----DGVTAVVRDRRDGEE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  168 ETVRTKYLFSGEGARSFIRQQLGIQIQYKDPISyvWGVMDGVVRT-NFPDIETKCTIH-----SDAGSIMVIPREDNMVR 241
Cdd:pfam01494 146 YTVRAKYLVGCDGGRSPVRKTLGIEFEGFEGVP--FGSLDVLFDApDLSDPVERAFVHyliyaPHSRGFMVGPWRSAGRE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  242 LYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEwDRVEWYSVYPIGQGISEKYTLDeRVFMGGDACHTHSPKAGQ 321
Cdd:pfam01494 224 RYYVQVPWDEEVEERPEEFTDEELKQRLRSIVGIDLAL-VEILWKSIWGVASRVATRYRKG-RVFLAGDAAHIHPPTGGQ 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 350632776  322 GMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFD 368
Cdd:pfam01494 302 GLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
PRK07190 PRK07190
FAD-binding protein;
10-420 9.01e-52

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 185.79  E-value: 9.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAF-KPAKVYDVafWdplPG 88
Cdd:PRK07190   7 DVVIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGPLEVGRADALNARTLQLLELVDLFDELYPLgKPCNTSSV--W---AN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  89 GQDIHRTGSW----PSC--PRFIdtrypfttLVHQGKIERVFLDEIQKAGTTVERPWTIVGfkndgldetypVEVQLKSI 162
Cdd:PRK07190  82 GKFISRQSSWweelEGClhKHFL--------MLGQSYVEKLLDDKLKEAGAAVKRNTSVVN-----------IELNQAGC 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 163 DTNVI--ETVRTKYLFSGEGARSFIRQQLGIQIQYKDPiSYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMVIPREDNMV 240
Cdd:PRK07190 143 LTTLSngERIQSRYVIGADGSRSFVRNHFNVPFEIIRP-QIIWAVIDGVIDTDFPKVPEIIVFQAETSDVAWIPREGEID 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 241 RLYVQIassDDPDFdprktaTAEDVQATARKILQPYWVEWDRVEWYSVYPIGQGISEKYTLDERVFMGGDACHTHSPKAG 320
Cdd:PRK07190 222 RFYVRM---DTKDF------TLEQAIAKINHAMQPHRLGFKEIVWFSQFSVKESVAEHFFIQDRIFLAGDACHIHSVNGG 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 321 QGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSfdnkyaalfskrrpTAGEVGEASHTTaAAGGEED 400
Cdd:PRK07190 293 QGLNTGLADAFNLIWKLNMVIHHGASPELLQSYEAERKPVAQGVIE--------------TSGELVRSTKYS-ANGTHAQ 357
                        410       420
                 ....*....|....*....|
gi 350632776 401 EFVKTFKSSCEFTSGYGVAY 420
Cdd:PRK07190 358 DYVKIVEKRAGYITGMGIRY 377
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
6-382 3.92e-50

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: 177.05  E-value: 3.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   6 QEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDVAFWDP 85
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLA-RGAPIRGIRVRDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LPGGQdIHRTgswpscpRFIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGldetYPVEVQLKSidtn 165
Cdd:COG0654   80 SDGRV-LARF-------DAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTGLEQDA----DGVTVTLAD---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 166 vIETVRTKYLFSGEGARSFIRQQLGIQIQYKD-PISYVWGVMDGVVRTNFPDietkctIHSDAGSIMviprednmvrlyv 244
Cdd:COG0654  144 -GRTLRADLVVGADGARSAVRRLLGIGFTGRDyPQRALWAGVRTELRARLAA------AGPRLGELL------------- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 245 qiassddpdfdprktataedvqatarkilqpywvewdRVEWYSVYPIGQGISEKYTlDERVFMGGDACHTHSPKAGQGMN 324
Cdd:COG0654  204 -------------------------------------ELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGAN 245
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 350632776 325 TAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKRRPTA 382
Cdd:COG0654  246 LALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADALGRLFHPDSPPL 303
Phe_hydrox_dim pfam07976
Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to ...
412-588 2.19e-45

Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerization interface. The domain adopts a thioredoxin-like fold.


Pssm-ID: 429765  Cd Length: 166  Bit Score: 158.47  E-value: 2.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  412 FTSGYGVAYKPNVFTWDATHPAQSPlfdvpgvRLTPGRAFTPTTVTRLADSNHVHLEQEIPANGAFRIFIFAG--KQDKT 489
Cdd:pfam07976   1 FTSGVGVDYGPSILVAGTSHQNLAS-------GLPVGRRFPSAKVVRQADANPVHLQDELPSDGRFRILVFAGdiSDPAQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  490 SKAITDLAANLEKERSFLSVYRRADIadvsffenhlPHSKLFSICLVYAGEKNQIDVDSIPKILR--------DYhHHLY 561
Cdd:pfam07976  74 KSRLEALADYLSSSSSFLSRYTPAGA----------DIDSVFDVLLIHSAPRTEVELEDLPEVLRpfdgklgwDY-WKVY 142
                         170       180
                  ....*....|....*....|....*..
gi 350632776  562 ADNIPDVRVPQatyAAHEKLGFDVEKG 588
Cdd:pfam07976 143 VDDESYHEGGG---DAYEKYGIDPKRG 166
PRK06184 PRK06184
hypothetical protein; Provisional
10-365 2.12e-44

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 165.54  E-value: 2.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMA----FKPAKVY----DVA 81
Cdd:PRK06184   5 DVLIVGAGPTGLTLAIELARRGVSFRLIEKAPEPFPGSRGKGIQPRTQEVFDDLGVLDRVVAagglYPPMRIYrddgSVA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  82 FWDPLPGGQDIHrtgswpscprfiDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDglDETypVEVQLKS 161
Cdd:PRK06184  85 ESDMFAHLEPTP------------DEPYPLPLMVPQWRTERILRERLAELGHRVEFGCELVGFEQD--ADG--VTARVAG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 162 IDTNviETVRTKYLFSGEGARSFIRQQLGIQIQYK----DPISYVWGVMDGVVRTN---FPdietkctiHSDAGSIMVIP 234
Cdd:PRK06184 149 PAGE--ETVRARYLVGADGGRSFVRKALGIGFPGEtlgiDRMLVADVSLTGLDRDAwhqWP--------DGDMGMIALCP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 235 -REDNMVRLYVQIASSDDPDFdprktaTAEDVQA-----TARKilqpyWVEWDRVEWYSVYPIGQGISEKYTlDERVFMG 308
Cdd:PRK06184 219 lPGTDLFQIQAPLPPGGEPDL------SADGLTAllaerTGRT-----DIRLHSVTWASAFRMNARLADRYR-VGRVFLA 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350632776 309 GDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGlAKRSILSTYETERKDIAETLL 365
Cdd:PRK06184 287 GDAAHVHPPAGGQGLNTSVQDAYNLGWKLAAVLAG-APEALLDTYEEERRPVAAAVL 342
PHOX_C cd02979
FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of ...
448-622 7.65e-38

FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of proteins similar to PHOX from the aerobic topsoil yeast Trichosporon cutaneum. PHOX is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen. This is the first step in the biodegradation and detoxification of phenolic compounds. PHOX contains three domains. The substrate and FAD/NAD(P) binding sites are contained in the first two domains, which adopt a complicated folding pattern. The third or C-terminal domain contains a TRX fold and is involved in dimerization. The functional unit of PHOX is a dimer, although active tetramers of the recombinant enzyme can be isolated when overproduced in bacteria.


Pssm-ID: 239277 [Multi-domain]  Cd Length: 167  Bit Score: 137.80  E-value: 7.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 448 GRAFTPTTVTRLADSNHVHLEQEIPANGAFRIFIFAGKQDK--TSKAITDLAANLEKERSFLSVYRRAdiadvsffenHL 525
Cdd:cd02979    1 GRRFPSAPVVRQADALPVHLGHRLPADGRFRIYVFAGDIAPaqQKSRLTQLCDALDSPDSFPLRYTPR----------GA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 526 PHSKLFSICLVYAGEKNQIDVDSIPKILR-------DYHHHLYADnipDVRVPQATYAAHEKLGFDVEKGGVVVTRPDSH 598
Cdd:cd02979   71 DPDSVFDVVTIHAAPRREIELLDLPAVLRpfgekkgWDYEKIYAD---DDSYHEGHGDAYEKYGIDPERGAVVVVRPDQY 147
                        170       180
                 ....*....|....*....|....
gi 350632776 599 VACTIQLsegsGTVDALNAFFGSF 622
Cdd:cd02979  148 VALVGPL----DDVEALEAYFAGF 167
PRK08244 PRK08244
monooxygenase;
8-365 1.53e-36

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 143.35  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQimaFKPAKvydvafwDPLP 87
Cdd:PRK08244   2 KYEVIIIGGGPVGLMLASELALAGVKTCVIERLKETVPYSKALTLHPRTLEILDMRGLLER---FLEKG-------RKLP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  88 GGqdiH----RTGSWPSCprfIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGldetypVEVQLKSID 163
Cdd:PRK08244  72 SG---HfaglDTRLDFSA---LDTSSNYTLFLPQAETEKVLEEHARSLGVEIFRGAEVLAVRQDG------DGVEVVVRG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 164 TNVIETVRTKYLFSGEGARSFIRQQLGIQIQYKDpiSYVWGVMDGVVRTNFPD--IETKCTihsDAGSIMVIPREDNMVR 241
Cdd:PRK08244 140 PDGLRTLTSSYVVGADGAGSIVRKQAGIAFPGTD--ATFTAMLGDVVLKDPPPssVLSLCT---REGGVMIVPLSGGIYR 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 242 lyVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEWDRVeWYSVYPIGQGISEKYTlDERVFMGGDACHTHSPKAGQ 321
Cdd:PRK08244 215 --VLIIDPERPQVPKDEPVTLEELKTSLIRICGTDFGLNDPV-WMSRFGNATRQAERYR-SGRIFLAGDAAHIHFPAGGQ 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 350632776 322 GMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLL 365
Cdd:PRK08244 291 GLNVGLQDAMNLGWKLAAAIKGWAPDWLLDSYHAERHPVGTALL 334
PRK06126 PRK06126
hypothetical protein; Provisional
2-362 8.04e-33

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 133.19  E-value: 8.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   2 APSQQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMA--FKPAKVYD 79
Cdd:PRK06126   1 AMENTSETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFNPKANTTSARSMEHFRRLGIADEVRSagLPVDYPTD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  80 VAFWDPLpGGQDIHR-----TGSWPSCPRFIDTRYPFTTLVHQgkIERVFLDEI------QKAGTTVERPWTIVGFKNDG 148
Cdd:PRK06126  81 IAYFTRL-TGYELARfrlpsAREAITPVGGPDGSWPSPELPHR--IPQKYLEPIllehaaAQPGVTLRYGHRLTDFEQDA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 149 lDEtypVEVQLKSIDTNVIETVRTKYLFSGEGARSFIRQQLGIQIQYKDPISYVWGVMdgvVRTnfPDIETKCTiHSDAG 228
Cdd:PRK06126 158 -DG---VTATVEDLDGGESLTIRADYLVGCDGARSAVRRSLGISYEGTSGLQRDLSIY---IRA--PGLAALVG-HDPAW 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 229 SIMVIPREDNMVrlYVQIASSDD------PDFDPRKTATAEDVQATARKIL-QPYWVEWDRVE-WYSVypigQGISEKYT 300
Cdd:PRK06126 228 MYWLFNPDRRGV--LVAIDGRDEwlfhqlRGGEDEFTIDDVDARAFVRRGVgEDIDYEVLSVVpWTGR----RLVADSYR 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350632776 301 lDERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAE 362
Cdd:PRK06126 302 -RGRVFLAGDAAHLFTPTGGYGMNTGIGDAVNLAWKLAAVLNGWAGPALLDSYEAERRPIAA 362
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
2-367 1.10e-25

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 111.15  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   2 APSQQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAF-KPAkvYDV 80
Cdd:PRK06183   4 QHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAVGIDDEALRVLQAIGLADEVLPHtTPN--HGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  81 AFWDPlpGGQ---DIHRTGS----WPscprfidTRYPFttlvHQGKIERVFLDEIQK-AGTTVERPWTIVGFKNDGldet 152
Cdd:PRK06183  82 RFLDA--KGRclaEIARPSTgefgWP-------RRNAF----HQPLLEAVLRAGLARfPHVRVRFGHEVTALTQDD---- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 153 YPVEVQLKSIDTNViETVRTKYLFSGEGARSFIRQQLGIQIQYKDPiSYVWGVMDGVVRTN---FPDIETKCtihsDAgs 229
Cdd:PRK06183 145 DGVTVTLTDADGQR-ETVRARYVVGCDGANSFVRRTLGVPFEDLTF-PERWLVVDVLIANDplgGPHTYQYC----DP-- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 230 imviprednmVRLYVQIASSDD---------PDFDPRKTATAEdvqaTARKILQPYWVEWDRVEW--YSVYPIGQGISEK 298
Cdd:PRK06183 217 ----------ARPYTSVRLPHGrrrwefmllPGETEEQLASPE----NVWRLLAPWGPTPDDAELirHAVYTFHARVADR 282
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 350632776 299 YTlDERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSF 367
Cdd:PRK06183 283 WR-SGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLAWKLAAVLRGRAGDALLDTYEQERRPHARAMIDL 350
PRK06834 PRK06834
hypothetical protein; Provisional
8-365 4.29e-25

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 108.95  E-value: 4.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATG-RADGIQPRSTEILRNLGL-KRQIMAFKPAKVYDVAfWDP 85
Cdd:PRK06834   3 EHAVVIAGGGPTGLMLAGELALAGVDVAIVERRPNQELVGsRAGGLHARTLEVLDQRGIaDRFLAQGQVAQVTGFA-ATR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  86 LpggqDIhrtGSWPscprfidTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGLDetypVEVQLKSIdtn 165
Cdd:PRK06834  82 L----DI---SDFP-------TRHNYGLALWQNHIERILAEWVGELGVPIYRGREVTGFAQDDTG----VDVELSDG--- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 166 viETVRTKYLFSGEGARSFIRQQLGIQIQYKDP-ISYVWGV--MDGvvrtnfpdiETKCTIHSDAGSIMVIPRE--DNMV 240
Cdd:PRK06834 141 --RTLRAQYLVGCDGGRSLVRKAAGIDFPGWDPtTSYLIAEveMTE---------EPEWGVHRDALGIHAFGRLedEGPV 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 241 RLYV---QIASSDDPDFDPRKTA-TAedVQATARKILQPYWVewdrvewySVYPIGQGISEKYTlDERVFMGGDACHTHS 316
Cdd:PRK06834 210 RVMVtekQVGATGEPTLDDLREAlIA--VYGTDYGIHSPTWI--------SRFTDMARQAASYR-DGRVLLAGDAAHVHS 278
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 350632776 317 PKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLL 365
Cdd:PRK06834 279 PVGGQGLNTGVQDAVNLGWKLAQVVKGTSPESLLDTYHAERHPVAARVL 327
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
8-357 1.77e-17

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 86.08  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMA-----------FKPAK 76
Cdd:PRK08132  23 RHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLSTGSRAICFAKRSLEIFDRLGCGERMVDkgvswnvgkvfLRDEE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  77 VYDvafWDPLPggQDIHRtgswpscprfidtRYPFTTLvHQGKIERVFLDEIQkAGTTVERPW----TIVGFKNDGldet 152
Cdd:PRK08132 103 VYR---FDLLP--EPGHR-------------RPAFINL-QQYYVEGYLVERAQ-ALPNIDLRWknkvTGLEQHDDG---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 153 ypveVQLkSIDT-NVIETVRTKYLFSGEGARSFIRQQLGIQIQ---YKDpiSYVwgVMDGVVRTNFPdieTKCTIHSD-- 226
Cdd:PRK08132 159 ----VTL-TVETpDGPYTLEADWVIACDGARSPLREMLGLEFEgrtFED--RFL--IADVKMKADFP---TERWFWFDpp 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 227 --AG-SIMVIPREDNMVRLYVQIAssddPDFDPRKTATAEDVQATARKILQPYwVEWDrVEWYSVYPIGQGISEKYTLDe 303
Cdd:PRK08132 227 fhPGqSVLLHRQPDNVWRIDFQLG----WDADPEAEKKPENVIPRVRALLGED-VPFE-LEWVSVYTFQCRRMDRFRHG- 299
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 350632776 304 RVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETER 357
Cdd:PRK08132 300 RVLFAGDAAHQVSPFGARGANSGIQDADNLAWKLALVLRGRAPDSLLDSYASER 353
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
10-380 4.09e-15

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 77.63  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPV-----PTATGRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWD 84
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARSGLKVALIEATPLpapadPGFDNRVSALSAASIRLLEKLGVWDKIEPARAQPIRDIHVSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   85 PLPGGQ------DIHRTgswpscprfidtryPFTTLVHQGKIERVFLDEIQKA-GTTVERPWTIVGFKNDGlDEtypVEV 157
Cdd:TIGR01988  81 GGSFGAlrfdadEIGLE--------------ALGYVVENRVLQQALWERLQELpNVTLLCPARVVELPRHS-DH---VEL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  158 QLKSIDtnvieTVRTKYLFSGEGARSFIRQQLGIQIQYKDpisYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMVIPRED 237
Cdd:TIGR01988 143 TLDDGQ-----QLRARLLVGADGANSKVRQLAGIPTTGWD---YGQSAVVANVKHERPHQGTAWERFTPTGPLALLPLPD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  238 NMVRLyV---------QIASSDDPDFdprktaTAEdVQATARKILQPYWVEWDRvewySVYPIGQGISEKYtLDERVFMG 308
Cdd:TIGR01988 215 NRSSL-VwtlppeeaeRLLALSDEEF------LAE-LQRAFGSRLGAITLVGER----HAFPLSLTHAKRY-VAPRLALI 281
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350632776  309 GDACHTHSPKAGQGMNTAFHDALNMAWKLH-AVESG--LAKRSILSTYETERK-DIAETLLSFDnKYAALFSKRRP 380
Cdd:TIGR01988 282 GDAAHTIHPLAGQGLNLGLRDVAALAEVLEdARRRGedIGSLRVLQRYERRRRfDNAAMLGATD-GLNRLFSNDFP 356
PRK07364 PRK07364
FAD-dependent hydroxylase;
9-378 4.44e-13

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 71.59  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   9 YDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTAT--GRADGIQPRSTEILRNLG----LKRQIMAFKPAKVYDVAF 82
Cdd:PRK07364  19 YDVAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAakGQAYALSLLSARIFEGIGvwekILPQIGKFRQIRLSDADY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  83 wdplpggqdihrtgswPSCPRFIDTRYPFTTLVHQGKiERVFLDEIQKAGTTVER-----PWTIVGFKNdgldETYPVEV 157
Cdd:PRK07364  99 ----------------PGVVKFQPTDLGTEALGYVGE-HQVLLEALQEFLQSCPNitwlcPAEVVSVEY----QQDAATV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 158 QLKSIDTNviETVRTKYLFSGEGARSFIRQQLGIQIQ-YKDPISYVwgvmDGVVRTNFPDIETKCTIHSDAGSIMVIPRE 236
Cdd:PRK07364 158 TLEIEGKQ--QTLQSKLVVAADGARSPIRQAAGIKTKgWKYWQSCV----TATVKHEAPHNDIAYERFWPSGPFAILPLP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 237 DNMVRLyVQIAssddPDFDPRKTATAEDVQATARkiLQPYWVEW--------DRvewySVYPIGQGISEKYTLDeRVFMG 308
Cdd:PRK07364 232 GNRCQI-VWTA----PHAQAKALLALPEAEFLAE--LQQRYGDQlgklellgDR----FLFPVQLMQSDRYVQH-RLALV 299
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350632776 309 GDACHTHSPKAGQGMNTAFHDALNMAWKLH-AVESG--LAKRSILSTYETERKDIAETLLSFDNKYAALFSKR 378
Cdd:PRK07364 300 GDAAHCCHPVGGQGLNLGIRDAAALAQVLQtAHQRGedIGSLAVLKRYERWRKRENWLILGFTDLLDRLFSNQ 372
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
5-366 1.59e-10

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 63.43  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   5 QQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATG-----RADGIQPRSTEILRNLGLKRQIMAFKPAKVYD 79
Cdd:PRK07608   2 YHMKFDVVVVGGGLVGASLALALAQSGLRVALLAPRAPPRPADdawdsRVYAISPSSQAFLERLGVWQALDAARLAPVYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  80 V-AFWDplpGGQDIHRTGSWPSCPR--FIdtrypfttlVHQGKIERVFLDEIQKAGTTVERPWTIVGFkndgldETYPVE 156
Cdd:PRK07608  82 MrVFGD---AHARLHFSAYQAGVPQlaWI---------VESSLIERALWAALRFQPNLTWFPARAQGL------EVDPDA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 157 VQLKSIDTNVIetvRTKYLFSGEGARSFIRQQLGIQIqykDPISYvwgVMDGVVrTNF----PDIETKCTIHSDAGSIMV 232
Cdd:PRK07608 144 ATLTLADGQVL---RADLVVGADGAHSWVRSQAGIKA---ERRPY---RQTGVV-ANFkaerPHRGTAYQWFRDDGILAL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 233 IPREDNMVRLyVQIASSDDPD----FDPRKTAtAEDVQATARkilqpywvEWDRVEwySVYPiGQG-----ISEKYTLDE 303
Cdd:PRK07608 214 LPLPDGHVSM-VWSARTAHADellaLSPEALA-ARVERASGG--------RLGRLE--CVTP-AAGfplrlQRVDRLVAP 280
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350632776 304 RVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVES--GLAKRSILSTYETERkdiAETLLS 366
Cdd:PRK07608 281 RVALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAGREPfrDLGDLRLLRRYERAR---REDILA 342
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
16-257 4.54e-09

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 58.06  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  16 AGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMafkpAKVYDVAFWdpLPGGQDIHrt 95
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFY--SPGGKSVE-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  96 gswpscprfIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGLDetypVEVQLKSidtnvIETVRTKYL 175
Cdd:COG0644   73 ---------LPPGRGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGR----VVVRTGD-----GEEIRADYV 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 176 FSGEGARSFIRQQLGIQIQYKDPISY---VWGVMDGVVRTNFPDIETKCTIHSDA--GSIMVIPREDNMVRLYVQIASSD 250
Cdd:COG0644  135 VDADGARSLLARKLGLKRRSDEPQDYalaIKEHWELPPLEGVDPGAVEFFFGEGApgGYGWVFPLGDGRVSVGIPLGGPR 214

                 ....*..
gi 350632776 251 DPDFDPR 257
Cdd:COG0644  215 PRLVGDG 221
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
10-357 5.69e-09

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 58.69  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADG-IQPR-------STEILRNLGLKRQIMAFKPAKVYDVA 81
Cdd:PRK05714   4 DLLIVGAGMVGSALALALQGSGLEVLLLDGGPLSVKPFDPQApFEPRvsalsaaSQRILERLGAWDGIAARRASPYSEMQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  82 FWDPLPGGQdIHRTGSwpscprfidtrypfttLVHQ---GKI--ERV----FLDEIQKAGTTVerpwtIVGFKNDGLDET 152
Cdd:PRK05714  84 VWDGSGTGQ-IHFSAA----------------SVHAevlGHIveNRVvqdaLLERLHDSDIGL-----LANARLEQMRRS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 153 yPVEVQLKSIDTnviETVRTKYLFSGEGARSFIRQQLGIQIQYKDpisYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMV 232
Cdd:PRK05714 142 -GDDWLLTLADG---RQLRAPLVVAADGANSAVRRLAGCATREWD---YLHHAIVTSVRCSEPHRATAWQRFTDDGPLAF 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 233 IPREDNMVRLYVQIASSDDPDFDPRktATAEDVQATARKILQPYwvEWDRVEWYSV-----YPIGQGISEKYtLDERVFM 307
Cdd:PRK05714 215 LPLERDGDEHWCSIVWSTTPEEAER--LMALDDDAFCAALERAF--EGRLGEVLSAdprlcVPLRQRHAKRY-VEPGLAL 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 350632776 308 GGDACHTHSPKAGQGMNTAFHDALNMAWKL-HAVESG--LAKRSILSTYETER 357
Cdd:PRK05714 290 IGDAAHTIHPLAGQGVNLGFLDAAVLAEVLlHAAERGerLADVRVLSRFERRR 342
PRK06185 PRK06185
FAD-dependent oxidoreductase;
7-330 6.76e-08

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 55.25  E-value: 6.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   7 EKYDIVIVGAGPVGIVLSLCMSRWGYKV----KHID-NRPVptatgRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVA 81
Cdd:PRK06185   5 ETTDCCIVGGGPAGMMLGLLLARAGVDVtvleKHADfLRDF-----RGDTVHPSTLELMDELGLLERFLELPHQKVRTLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  82 FwdpLPGGQDIhrtgswpscpRFID-----TRYPFTTLVHQgkieRVFLDEI-QKA----------GTTV----ERPWTI 141
Cdd:PRK06185  80 F---EIGGRTV----------TLADfsrlpTPYPYIAMMPQ----WDFLDFLaEEAsaypnftlrmGAEVtgliEEGGRV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 142 VGFKNDGLDETYpvevqlksidtnvieTVRTKYLFSGEGARSFIRQQLGIQIQYKD-PISYVWgvmdgvvrtnF-----P 215
Cdd:PRK06185 143 TGVRARTPDGPG---------------EIRADLVVGADGRHSRVRALAGLEVREFGaPMDVLW----------FrlpreP 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 216 DIETKCTIHSDAGSIMV-IPREDnmvrlYVQ----IASSDDPDF---------------DPRKTATAEDVQAtarkilqp 275
Cdd:PRK06185 198 DDPESLMGRFGPGQGLImIDRGD-----YWQcgyvIPKGGYAALraagleafrervaelAPELADRVAELKS-------- 264
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 350632776 276 ywveWDRVEWYSVYPigqGISEKYTLDERVFMgGDACHTHSPKAGQGMNTAFHDA 330
Cdd:PRK06185 265 ----WDDVKLLDVRV---DRLRRWHRPGLLCI-GDAAHAMSPVGGVGINLAIQDA 311
PRK07045 PRK07045
putative monooxygenase; Reviewed
10-398 1.18e-07

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 54.53  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAfKPAKVYDV--AFWDPLP 87
Cdd:PRK07045   7 DVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFA-AGGLRRDAmrLYHDKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  88 GGQDIHRTGSwpSCPRFIdtrypfttLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGLDETypvevqLKSIDTNVI 167
Cdd:PRK07045  86 IASLDYRSAS--ALGYFI--------LIPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDADGT------VTSVTLSDG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 168 ETVRTKYLFSGEGARSFIRQQL----GIQIQYKDPISY-VWGVMDGVVRTNfpdietKCTIHSDAGSIMVIPREDNMVRL 242
Cdd:PRK07045 150 ERVAPTVLVGADGARSMIRDDVlrmpAERVPYATPMAFgTIALTDSVRECN------RLYVDSNQGLAYFYPIGDQATRL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 243 YVQIASSDDPDFdprktaTAEDVQATARKILQPYwVEWDRVEW---------YSVYPIGQGISEKYTLDErVFMGGDACH 313
Cdd:PRK07045 224 VVSFPADEMQGY------LADTTRTKLLARLNEF-VGDESADAmaaigagtaFPLIPLGRMNLDRYHKRN-VVLLGDAAH 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 314 THSPKAGQGMNTAFHDALNMAWKLHAVESG-LAKRSILSTYETERKDIAETLLSFDNKYAALFSKRRPTAG----EVGEA 388
Cdd:PRK07045 296 SIHPITGQGMNLAIEDAGELGACLDLHLSGqIALADALERFERIRRPVNEAVISYGHALATTYHDRAALVAnfrsQLQTS 375
                        410
                 ....*....|
gi 350632776 389 SHTTAAAGGE 398
Cdd:PRK07045 376 GRDAAWLGAA 385
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
10-380 1.71e-07

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 54.01  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  10 DIVIVGAGPVGIVLSLCMSRWGYKVKHIDNR-PVPTATG----RADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWD 84
Cdd:PRK08850   6 DVAIIGGGMVGLALAAALKESDLRIAVIEGQlPEEALNElpdvRVSALSRSSEHILRNLGAWQGIEARRAAPYIAMEVWE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  85 plpggQDihrtgswpscpRFIDTRYPFTTLVHQ--GKI--ERV----FLDEIQKA-GTTVERPWTIvgfKNDGLDETypv 155
Cdd:PRK08850  86 -----QD-----------SFARIEFDAESMAQPdlGHIveNRViqlaLLEQVQKQdNVTLLMPARC---QSIAVGES--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 156 EVQLkSIDTNviETVRTKYLFSGEGARSFIRQQLGIQIQYKDpisYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMVIP- 234
Cdd:PRK08850 144 EAWL-TLDNG--QALTAKLVVGADGANSWLRRQMDIPLTHWD---YGHSALVANVRTVDPHNSVARQIFTPQGPLAFLPm 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 235 REDNMVRLY--------VQIASSDDPDFDprKTATAE-DVQATARKilqpywVEWDRvewySVYPIgqgiSEKYTLD--- 302
Cdd:PRK08850 218 SEPNMSSIVwsteplraEALLAMSDEQFN--KALTAEfDNRLGLCE------VVGER----QAFPL----KMRYARDfvr 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 303 ERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWK---LHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKRR 379
Cdd:PRK08850 282 ERVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEilaLWQQGRDIGLKRNLRGYERWRKAEAAKMIAAMQGFRDLFSGSN 361

                 .
gi 350632776 380 P 380
Cdd:PRK08850 362 P 362
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
7-358 1.73e-06

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 50.54  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   7 EKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPvPTATG-------RADGIQPRSTEILRNLGLKRQIMAFK--PAKv 77
Cdd:PRK08849   2 NKYDIAVVGGGMVGAATALGFAKQGRSVAVIEGGE-PKAFEpsqpmdiRVSAISQTSVDLLESLGAWSSIVAMRvcPYK- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  78 ydvafwdplpggqdihRTGSW--PSCprfiDTRYpfttlvHQGKIErvfLDEIqkaGTTVERPWTIVGFKN-----DGLD 150
Cdd:PRK08849  80 ----------------RLETWehPEC----RTRF------HSDELN---LDQL---GYIVENRLIQLGLWQqfaqyPNLT 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 151 ETYPVevQLKSI----DTNVI-----ETVRTKYLFSGEGARSFIRQQLGIQIQYKDpisYVWGVMDGVVRTNFPDIETKC 221
Cdd:PRK08849 128 LMCPE--KLADLefsaEGNRVtlesgAEIEAKWVIGADGANSQVRQLAGIGITAWD---YRQHCMLINVETEQPQQDITW 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 222 TIHSDAGSIMVIPREDNMVRL--YvqiassDDPDfdpR-KTATAEDVQATARKILQPYWVEWD--RVEWYSVYPIGQGIS 296
Cdd:PRK08849 203 QQFTPSGPRSFLPLCGNQGSLvwY------DSPK---RiKQLSAMNPEQLRSEILRHFPAELGeiKVLQHGSFPLTRRHA 273
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350632776 297 EKYTlDERVFMGGDACHTHSPKAGQGMNTAFHDalnMAWKLHAVE-SGLAKRSILSTYETERK 358
Cdd:PRK08849 274 QQYV-KNNCVLLGDAAHTINPLAGQGVNLGFKD---VDVLLAETEkQGVLNDASFARYERRRR 332
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
9-358 4.52e-06

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: 49.37  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776    9 YDIVIVGAGPVGI----------------VLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAF 72
Cdd:TIGR01989   1 FDVVIVGGGPVGLalaaalgnnpltkdlkVLLLDAVDNPKLKSRNYEKPDGPYSNRVSSITPASISFFKKIGAWDHIQSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   73 KPAKVYDVAFWDPLPGG--QDIHRTGSWP-SCPRFIDT-RYPFTTLVHQGKIERVFLDEIQKAgttveRPWTIVgfKNDG 148
Cdd:TIGR01989  81 RIQPFGRMQVWDGCSLAliRFDRDNGKEDmACIIENDNiQNSLYNRLQEYNGDNVKILNPARL-----ISVTIP--SKYP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  149 LDETYPVEVQLKSIDTnvietVRTKYLFSGEGARSFIRQQLGIQiqykdpiSYVWgvmdgvvrtNFPDIETKCTIHSD-- 226
Cdd:TIGR01989 154 NDNSNWVHITLSDGQV-----LYTKLLIGADGSNSNVRKAANID-------TTGW---------NYNQHAVVATLKLEea 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  227 ------------AGSIMVIPREDNMVRL-------------------------------YVQIASSDDPDFDPRKTATAE 263
Cdd:TIGR01989 213 tendvawqrflpTGPIALLPLPDNNSTLvwstspeealrllslppedfvdalnaafdlgYSDHPYSYLLDYAMEKLNEDI 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  264 DVQATARKI---LQPYWVEWDRvEWYSVYPIGQGISEKYtLDERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKL-HA 339
Cdd:TIGR01989 293 GFRTEGSKScfqVPPRVIGVVD-KSRAAFPLGLGHADEY-VTKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALaEA 370
                         410       420
                  ....*....|....*....|.
gi 350632776  340 VESGLAKRSI--LSTYETERK 358
Cdd:TIGR01989 371 VSVGADIGSIssLKPYERERY 391
PRK09126 PRK09126
FAD-dependent hydroxylase;
8-79 2.43e-05

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 46.86  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   8 KYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPV-----PTATGRADGIQPRSTEILRNLGLKRQIMA-----FKPAKV 77
Cdd:PRK09126   3 HSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQPLaaladPAFDGREIALTHASREILQRLGAWDRIPEdeispLRDAKV 82

                 ..
gi 350632776  78 YD 79
Cdd:PRK09126  83 LN 84
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
9-326 1.08e-03

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 41.54  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776    9 YDIVIVGAGPVGIVLSLCMSRWGYKV----KHIDNRPVPTatgrADGIQPRSTEILRNLGlkrqimAFKPAKVYDVAFWd 84
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVllleKKSFPRYKPC----GGALSPRALEELDLPG------ELIVNLVRGARFF- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776   85 pLPGGQDIHrtgswpscprfIDTRYPFTTLVHQGKIERVFLDEIQKAG--TTVERPWTIVGFKNDGLDETYpvevqlksi 162
Cdd:TIGR02032  70 -SPNGDSVE-----------IPIETELAYVIDRDAFDEQLAERAQEAGaeLRLGTRVLDVEIHDDRVVVIV--------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  163 DTnVIETVRTKYLFSGEGARSFIRQQLGiQIQYKDPISY---VWGVMDGVvrtnfPDIETKCTIHSD-----AGSIMVIP 234
Cdd:TIGR02032 129 RG-SEGTVTAKIVIGADGSRSIVAKKLG-LKKEPREYGVaarAEVEMPDE-----EVDEDFVEVYIDrgivpGGYGWVFP 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776  235 REDNMVRLYVQIASSDDPdFDPRKtATAEDVQatARKilqpywvEWDRVEWYSVY----PIGQGISEKYTldERVFMGGD 310
Cdd:TIGR02032 202 KGDGTANVGVGSRSAEEG-EDPKK-YLKDFLA--RRP-------ELKDAETVEVCgaliPIGRPDEKLVR--GNVLLVGD 268
                         330
                  ....*....|....*.
gi 350632776  311 ACHTHSPKAGQGMNTA 326
Cdd:TIGR02032 269 AAGHVNPLTGEGIYYA 284
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
4-65 1.66e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 41.04  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350632776   4 SQQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDnRPVPTATGRADGIQPRSTEILRNLGL 65
Cdd:PRK07494   3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALVA-PEPPYADLRTTALLGPSIRFLERLGL 63
PLN02463 PLN02463
lycopene beta cyclase
3-41 5.54e-03

lycopene beta cyclase


Pssm-ID: 178082 [Multi-domain]  Cd Length: 447  Bit Score: 39.70  E-value: 5.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 350632776   3 PSQQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRP 41
Cdd:PLN02463  23 PSKSRVVDLVVVGGGPAGLAVAQQVSEAGLSVCCIDPSP 61
PRK06996 PRK06996
UbiH/UbiF/VisC/COQ6 family ubiquinone biosynthesis hydroxylase;
1-29 6.49e-03

UbiH/UbiF/VisC/COQ6 family ubiquinone biosynthesis hydroxylase;


Pssm-ID: 235905 [Multi-domain]  Cd Length: 398  Bit Score: 39.29  E-value: 6.49e-03
                         10        20
                 ....*....|....*....|....*....
gi 350632776   1 MAPSQQEKYDIVIVGAGPVGIVLSLCMSR 29
Cdd:PRK06996   4 AASMAAPDFDIAIVGAGPVGLALAGWLAR 32
PRK08013 PRK08013
oxidoreductase; Provisional
304-380 9.81e-03

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 38.87  E-value: 9.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350632776 304 RVFMGGDACHTHSPKAGQGMNTAFHDALNMA---WKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKRRP 380
Cdd:PRK08013 283 RLALVGDAAHTIHPLAGQGVNLGFMDAAELIaelRRLHRQGKDIGQHLYLRRYERSRKHSAALMLAGMQGFRDLFAGNNP 362
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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