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Database: UniProt
Entry: A0A0F4JV07_9ACTN
LinkDB: A0A0F4JV07_9ACTN
Original site: A0A0F4JV07_9ACTN 
ID   A0A0F4JV07_9ACTN        Unreviewed;       534 AA.
AC   A0A0F4JV07;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KJY37674.1};
GN   ORFNames=VR44_05325 {ECO:0000313|EMBL:KJY37674.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY37674.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY37674.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY37674.1};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00010790}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJY37674.1}.
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DR   EMBL; JZWV01000097; KJY37674.1; -; Genomic_DNA.
DR   RefSeq; WP_045946186.1; NZ_JZWV01000097.1.
DR   AlphaFoldDB; A0A0F4JV07; -.
DR   STRING; 68223.GCA_002028425_01372; -.
DR   PATRIC; fig|68223.7.peg.1701; -.
DR   eggNOG; COG2303; Bacteria.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000033551; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          280..294
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   534 AA;  57233 MW;  F164170FCC619945 CRC64;
     MATEQYDYVI VGSGTAGSVL ADRLSADPDV SVLVLEAGGD RIPPEVDDPS SWYKLLGGPV
     DWGYTSVPQP GLGGRRTYEP RGKAPGGSSN LYIMMHIRGH ASDFDNWAYQ GAAGWAYEDV
     LPYFALLEAQ EDVTAATTGT AGPQRVTNAG RHGPNPVSRA FIDAAVELGH QEIADFNTDG
     PRGGLFGTGW HHIDVADGRR QGTLASYLEP ALTRPNLTLR TSAQSTRLLF EGDTCTGVEY
     VQLQPPAEVP GRTVRDRHST AAAPGLHIVR ARREVIVAAG AIESPKLLLL SGIGHPEQLR
     EHGIAVTAAV PGVGENFHNH VLTGLMAEVT QELPAPAQNL SESALFLSSR PGLPAPDLQI
     AFVHVPFDVI VGQNHPNTVS ILPGVVRPVS RGSIRLASAD PLAHPLIDPN YLGDRWDLER
     MVQGVKIARE IFATSAFSPW YKQELQPGPG AVTDEDLRTF VRQKAESYHH QAGSCRMGVD
     DLAVVDPELR VHGVRNLRVV DASVMPAVPS GNCHTAIAMI AERAADFLRG VSRA
//
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