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Database: UniProt
Entry: K5UTR2_PHACS
LinkDB: K5UTR2_PHACS
Original site: K5UTR2_PHACS 
ID   K5UTR2_PHACS            Unreviewed;       774 AA.
AC   K5UTR2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=PHACADRAFT_259608 {ECO:0000313|EMBL:EKM53326.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM53326.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM53326.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM53326.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; JH930474; EKM53326.1; -; Genomic_DNA.
DR   RefSeq; XP_007398018.1; XM_007397956.1.
DR   AlphaFoldDB; K5UTR2; -.
DR   STRING; 650164.K5UTR2; -.
DR   GeneID; 18917469; -.
DR   KEGG; pco:PHACADRAFT_259608; -.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   InParanoid; K5UTR2; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR005018; DOMON_domain.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR47190:SF4; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..774
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003887507"
FT   DOMAIN          317..340
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          485..499
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          208..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  82763 MW;  90AD39248F077B74 CRC64;
     MLRRSLLALL PLIGVAFSQS ASQFTDPVTG FQFTGLTDPV HDVTYGFVFP PLVTSGNQST
     EFIGEVVAPI EAQWIGIALG GEMIGDLLLV AWPNGNEIVS STRWATDYIQ PIAYTGQATL
     TTLSETKVNS THWQWVFRCQ GCTEWNNGEG IDVTSEGVLA WAFSNVAVDD PSDAESTFSE
     HTDFGFFGID YSSAHSSNYQ NYLAGNAGNP TTTSSTPTST SSSTSTGPTA SATPYDYIVV
     GAGPGGIISA DRLSQAGKKV LLLERGGPST QETGGTYVAP WAEGSGLTKF DIPGLFESLF
     TDPDDFWWCK DVTVFAGCLV GGGTSVNGAL YWYPNTQDFS SSVGWPSSWE NHTPYTSMVQ
     ARLPSTDHPS TDGERYLEQT FGVMSQLLSG QGYSNITIND NPNYKDHVYG YSSFDFLNGK
     RAGPVATYLQ TALARPNFTF KQNVMVSNVV RNGSQILGVQ TNDTTLGPNG FIPLTTNGRV
     VLSGGAFGTS RILFQSGIGP TDMLQIVQGS STAAAALPPQ DQWIDLPVGY NAQDNPSINL
     VFTHPSVDAY ENWADVWSDP RPADAAQYLE NQSGVFASAS PRVNFWRAYS GSDGFTRYAQ
     GTVRPGASLP LNTSLSYNSS QLFTITVYLS TGIQSRGRVG IDAALRGTVL TAPWLVNADD
     KTVILQALND VISNMDSVPG LTLVVPDNTL TMEEYVNEYD PSTMNSNHWV STTTIGSSAQ
     NAVVDENAKV FNTNNLFVVD AGIIPHLPTG NPQGTLMSAA EHAVANILAL AGGP
//
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