ID A0A101D1Q5_9GAMM Unreviewed; 549 AA.
AC A0A101D1Q5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KUJ87340.1};
DE EC=4.1.2.10 {ECO:0000313|EMBL:KUJ87340.1};
GN ORFNames=XD36_2224 {ECO:0000313|EMBL:KUJ87340.1};
OS Halomonas sp. 54_146.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ87340.1, ECO:0000313|Proteomes:UP000053192};
RN [1] {ECO:0000313|Proteomes:UP000053192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
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:KUJ87340.1}.
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DR EMBL; LGEN01000025; KUJ87340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101D1Q5; -.
DR STRING; 1635257.XD36_2224; -.
DR PATRIC; fig|1635257.4.peg.1949; -.
DR Proteomes; UP000053192; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046593; F:mandelonitrile lyase activity; IEA:UniProtKB-EC.
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; 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 Lyase {ECO:0000313|EMBL:KUJ87340.1}.
FT DOMAIN 272..286
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 549 AA; 60775 MW; CE1B4DB07EB45CF8 CRC64;
MSESTNNKFD YIVIGAGTAG CLLANRLSAN PNNKVLLIEA GGRDNYHWIH IPVGYLYCIN
NPRTDWLFRT EPDKGLNGRS LIYPRGKTLG GCSSINGMLY LRGQARDYDH WAELTGDDAW
RWENCLPDFM KHEDHHRLDE GGDGDAEHRR YHGHGGEWRI EKQRLSWEVL DDFAEAAVQA
GIPRTEDFNR GDNEGVNYFE VNQRGGWRWN TSKAFLRPIK ERSNLTVWHS THVNRLLFEQ
QGGKPGCVGA ELLREGKALN VAANKEVVLS AGAIGSPQIL QLSGIGDPEL LQRHGIDVVA
VLPGVGENLQ DHLQIRSVYK VKGAKTLNTM ASTLLGKAKI GLEYVFKRSG PMSMAPSQLC
IFTRSSDDYQ HANIEYHVQP LSLDAFGQPL HPYPAITASV CNLNPTSRGS VRIKNRDPQA
APAIEPNYLS TEEDRKVAAD SLRVTRRIAE QQAFAKYQPE EFKPGLQYQS DDELAKLAGD
IGTTIFHPVG TTKMGRDDDP MAVVDSKLRV KGVNGLRVVD AGVMPTITSG NTNSPTLMIA
EKAAGWILA
//
