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Database: UniProt
Entry: F0KF50_ACICP
LinkDB: F0KF50_ACICP
Original site: F0KF50_ACICP 
ID   F0KF50_ACICP            Unreviewed;       535 AA.
AC   F0KF50;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ADY81918.1};
GN   Name=alkJ {ECO:0000313|EMBL:ADY81918.1};
GN   OrderedLocusNames=BDGL_001332 {ECO:0000313|EMBL:ADY81918.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY81918.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY81918.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY81918.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP002177; ADY81918.1; -; Genomic_DNA.
DR   RefSeq; WP_014206903.1; NC_016603.1.
DR   RefSeq; YP_004995600.1; NC_016603.1.
DR   AlphaFoldDB; F0KF50; -.
DR   STRING; 871585.BDGL_001332; -.
DR   GeneID; 11639513; -.
DR   KEGG; acc:BDGL_001332; -.
DR   PATRIC; fig|871585.3.peg.1326; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000007477; Chromosome.
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; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007477}.
FT   DOMAIN          80..103
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          254..268
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         82
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         218
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   535 AA;  58608 MW;  1A5E7763C4145FB5 CRC64;
     MNQQYDYIVI GAGSAGCVVA ARLLEAMAGR VLVLEAGSRD SSMFHTIPAT VVKVFQQKSW
     QYMTVPQKYC NHREMILAQG KVLGGGSSVN GMIYCRGQRQ DYDLWSSEWG CNQWSYQHVL
     PFFKKAEKNE SLADEYHGQD GILPVSENRY RHPLTLACIK AGQQMGMNYV NDINGWDQAG
     VGFYQTTTQN GSRASTSKTY LKSVENHPDL TVITDALVHK IETQGDQVTG VTYSVGGKSP
     ITVQVQKEVI LSAGAIGSPK VLLLSGIGPK QHLDELGIEC IRDLPVGENF HDHLHMSVNA
     IVTTNNSLLG EDQGLTAVRH FLQWCFTRSG LLTTNILEGG GFIDTNNNGR PDVQFHFLPV
     LDNFDNTPGE KATAQAHGLT IKVGHVQPKA RGILRLSSKD PKDLPVIDPN YLGHQEDIDA
     NIRAVQAGLR LLQQPALKAI VKEVAEPANI DPDDIEAIDK WMRQNIKTVY HPAGSCKMGN
     APQDSVTDQT LKVHGFKNLR VVDCSICPQV PSGNTNAIAI MIGERGADFI LNQVA
//
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