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Database: UniProt
Entry: A0A0D5M0V6_9GAMM
LinkDB: A0A0D5M0V6_9GAMM
Original site: A0A0D5M0V6_9GAMM 
ID   A0A0D5M0V6_9GAMM        Unreviewed;       556 AA.
AC   A0A0D5M0V6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AJY49840.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:AJY49840.1};
GN   ORFNames=KO116_01351 {ECO:0000313|EMBL:AJY49840.1};
OS   Halomonas sp. KO116.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49840.1, ECO:0000313|Proteomes:UP000028645};
RN   [1] {ECO:0000313|EMBL:AJY49840.1, ECO:0000313|Proteomes:UP000028645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KO116 {ECO:0000313|EMBL:AJY49840.1,
RC   ECO:0000313|Proteomes:UP000028645};
RX   PubMed=25953187;
RA   O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT   "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT   Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL   Genome Announc. 3:0-0(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}.
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DR   EMBL; CP011052; AJY49840.1; -; Genomic_DNA.
DR   RefSeq; WP_035559866.1; NZ_CP011052.1.
DR   AlphaFoldDB; A0A0D5M0V6; -.
DR   STRING; 1504981.KO116_01351; -.
DR   KEGG; hak:KO116_01351; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000028645; Chromosome.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:AJY49840.1}.
FT   DOMAIN          276..290
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   556 AA;  61527 MW;  F0EE03A4BB0ADBDD CRC64;
     MSEPTNNNFD YIVIGAGTAG CLLANRLSTN PNNKVLLIEA GGRDNYHWIH IPVGYLYCIN
     NPRTDWLFRT EPDKGLNGRS LIYPRGKTLG GCSSINGMIY MRGQARDYDH WAEVTGDDAW
     RWENCLPDFI KHEDHYRLDE GGDADAKHRN FHGHGGEWRI EKQRLKWQVL DDFAEAAVQA
     GIPRTDDFNR GSNEGVAYFE VNQRSGWRWN TAKAFLRPAL KRGNLTLWHS TQVNRLLFEQ
     AEALRCTGVE VERGGKTQHA ILTKEGGNAE VVLCAGAIGT PHLLQLSGVG PAETLREHGV
     EVVHELPGVG ENLQDHLQIR SIYRITNGKT LNAMASTLWG KAGIGLEYLL KRSGPMSMAP
     SQLGAFTRST QDQTHPNIEY HVQPLSLEAF GQPLHPYPAI TASVCNLNPT SRGTVRLKSS
     DPRQAPAISP NYLSTPEDRK VAADSLRVTR RIAEQPAFAK YAPEEVKPGV EYQSDDELAR
     LAGDIGTTIF HPVGTARMGR EDDAMAVVDA RLRVRGVRGL RVADASIMPT ITSGNTNSPT
     LMIAEKAAGW MLAERR
//
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