ID   A0A109ULT9_9GAMM        Unreviewed;       551 AA.
AC   A0A109ULT9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AMD01013.1};
DE            EC=1.1.99.- {ECO:0000313|EMBL:AMD01013.1};
GN   Name=alkJ {ECO:0000313|EMBL:AMD01013.1};
GN   ORFNames=LOKO_01946 {ECO:0000313|EMBL:AMD01013.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD01013.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMD01013.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD01013.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT   Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMD01013.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD01013.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014226; AMD01013.1; -; Genomic_DNA.
DR   RefSeq; WP_066448241.1; NZ_CP014226.1.
DR   AlphaFoldDB; A0A109ULT9; -.
DR   STRING; 507626.LOKO_01946; -.
DR   KEGG; hco:LOKO_01946; -.
DR   PATRIC; fig|507626.3.peg.1942; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000063387; 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; 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   Oxidoreductase {ECO:0000313|EMBL:AMD01013.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387}.
FT   DOMAIN          271..285
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   551 AA;  61190 MW;  3FD7C00DA5AE1EBC CRC64;
     MAEQEFDYIV VGAGTAGCLL ANRLSADPNN RVLLIEAGGR DNYHWVHIPV GYLYCINNPR
     TDWCFRTEPD KGLNGRSLIF PRGKTLGGCS SINGMLYMRG QARDYDGWAE LVGDDAWRWE
     NCLPDFMKHE HHYRLDEGGD ADAAHRDYHG HGGEWRVEKQ RLKWEVLDDF AEAAVQAGIP
     RTRDFNRGDN EGVDYFEVNQ RSGWRWNAAK AFLRPTCVKR DNFVLWHSTQ VHRLLFESGS
     EGKPRATGVE LERDGVISQV RATREVILAA GAIGSPQLLQ LSGVGPASLL AEHDIPLVHE
     LPGVGENLQD HLQIRSVYKV TGAKTLNTLA ASWMGKAKIG MEYVLKRTGP MSMAPSQLCA
     FTRSSDEYEH PNIEYHVQPL SLEAFGQPLH DYPAITASVC NLNPTSRGSV RIKSRDPRQA
     PAIAPNYLST EEDRKVAADS LRVTRRIAEQ PAFAKYRPEE VKPGLEYQTD DELARLAGDI
     GTTIFHPVGT AKMGRDDDPT AVVDSHLRVR GVEGLRVVDA SIMPTITSGN TNSPTLMIAE
     KAAGWILAER S
//