ID A0A0M6XMQ9_9RHOB Unreviewed; 549 AA.
AC A0A0M6XMQ9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alcohol dehydrogenase [acceptor] {ECO:0000313|EMBL:CTQ32436.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:CTQ32436.1};
GN Name=alkJ_1 {ECO:0000313|EMBL:CTQ32436.1};
GN ORFNames=JAN5088_01201 {ECO:0000313|EMBL:CTQ32436.1};
OS Jannaschia rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ32436.1, ECO:0000313|Proteomes:UP000048908};
RN [1] {ECO:0000313|EMBL:CTQ32436.1, ECO:0000313|Proteomes:UP000048908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ32436.1,
RC ECO:0000313|Proteomes:UP000048908};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CXPG01000013; CTQ32436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M6XMQ9; -.
DR STRING; 282197.SAMN04488517_1053; -.
DR Proteomes; UP000048908; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Oxidoreductase {ECO:0000313|EMBL:CTQ32436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000048908}.
FT DOMAIN 94..117
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 264..278
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 549 AA; 59361 MW; 50E04C5A8C4A7120 CRC64;
MTGSRGMAKR LRGQEVYDYI IVGGGSAGCV MAARLSEDPR RRVCLVEAGP RDTNPLIHMP
LGLALLVGSK RINWAYDTHP EPELNGRSLF WPRGKTLGGS SSINAMIYMR GHPKDYDGWE
AAAGPDWGWP RVRELFLRME GNTARSDAHH GTDGPLAVSD LRHVNPLSHA FVEAGTQCQY
PENPDFNGAR QEGVGLYQVT QREGRRFSAA RAFLEPARDR PNLTTLTGKP VERILFEGRR
AVGVALRDRD LRLNAGGEVI LSGGAVNSPH LLMLSGIGPA EELARHGVPV LHDAPEVGSN
LADHLDITVM ASARGREGIG LAPSFLPRAV RAAWSYWRGG TGELTSNVAE AGGFVRSDPS
RDRPNLQFHF LPALLRDHGR KLSWGYGMTL HVCDLLPKSR GRIGLNGPDT SMPARIEANY
LSHPDDIGTL LDGLKIARGI MAAPALARHV RAEILPGPEV RTDAQLIADI RARAETIYHP
VGTCRMGTDA ASVVDPEARL RGIDGLRVVD ASIMPNIVAG NTNAPTMMLA ENVADMMLGR
NGAAPEVLT
//
