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Database: UniProt
Entry: A0A095SN50_9GAMM
LinkDB: A0A095SN50_9GAMM
Original site: A0A095SN50_9GAMM 
ID   A0A095SN50_9GAMM        Unreviewed;       538 AA.
AC   A0A095SN50;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KGD66012.1};
GN   ORFNames=Y5S_00484 {ECO:0000313|EMBL:KGD66012.1};
OS   Alcanivorax nanhaiticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD66012.1, ECO:0000313|Proteomes:UP000029444};
RN   [1] {ECO:0000313|EMBL:KGD66012.1, ECO:0000313|Proteomes:UP000029444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19-m-6 {ECO:0000313|EMBL:KGD66012.1,
RC   ECO:0000313|Proteomes:UP000029444};
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL   Submitted (SEP-2012) 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, ECO:0000256|RuleBase:RU003968}.
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:KGD66012.1}.
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DR   EMBL; ARXV01000002; KGD66012.1; -; Genomic_DNA.
DR   RefSeq; WP_035230177.1; NZ_ARXV01000002.1.
DR   AlphaFoldDB; A0A095SN50; -.
DR   STRING; 1177154.Y5S_00484; -.
DR   PATRIC; fig|1177154.3.peg.492; -.
DR   eggNOG; COG2303; Bacteria.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000029444; 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; 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|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968}.
FT   DOMAIN          81..104
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   538 AA;  58297 MW;  7B2C64E6948BC38C CRC64;
     MEFDYVIVGG GSAGAVLAAR LSEDPSVSVC LLEAGGKGDH ILIRAPAGVV AMMPNGRVSN
     WAFETEPQPG LQGRLGYQPR GKALGGSSAI NAMLYVRGQK QDYDSWAEQG CEGWSWDEVL
     PYFIKSENNE NGSNAFHGAD GPLHVSNQKS PRPVTHAFVE SARQAGYPVV EDFNTGDNEG
     AGIYQVTQFH GQPKNGERCS TAAGFLHPVM DRSNLTVLTD AHATRILFEG KRAVGVAYRQ
     KGQDAEVRAR REVLVAGGAF GSPQLLQLSG VGRAEDITPH GIALVHELPG VGQNLQDHID
     FILSYKSRDT DNFGIGLTAT FNLIKHTLQW KKDGTGMIAT PFAEGGVFMK SDAAVDRPDL
     QLHFVISVVD DHARKLTLGH GFSCHVCVLR PHSRGRVFLK TGDPLAAPGI DPNFLSDERD
     LETLLKGAKI TRDILEGEPL SKYREEPLFG LRGDFNDDEW KEHLRSRADT VYHPVGTCKM
     GQDEMAVVDP QLKVRGLNGL RVVDASVMPS LVSGNTNAPT IMIAEKAADM IKADQIQA
//
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