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
//