ID   A0A1H1RS08_9MICO        Unreviewed;       525 AA.
AC   A0A1H1RS08;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SDS38444.1};
GN   ORFNames=SAMN04489751_1891 {ECO:0000313|EMBL:SDS38444.1};
OS   Brevibacterium sandarakinum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=629680 {ECO:0000313|EMBL:SDS38444.1, ECO:0000313|Proteomes:UP000199700};
RN   [1] {ECO:0000313|EMBL:SDS38444.1, ECO:0000313|Proteomes:UP000199700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22082 {ECO:0000313|EMBL:SDS38444.1,
RC   ECO:0000313|Proteomes:UP000199700};
RA   de Groot N.N.;
RL   Submitted (OCT-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, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; LT629739; SDS38444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1RS08; -.
DR   STRING; 629680.SAMN04489751_1891; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000199700; Chromosome i.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 2.
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.
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}.
FT   DOMAIN          88..111
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   BINDING         228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   525 AA;  56170 MW;  EB9520E99A43FDAC CRC64;
     MKEDNWDIIV IGAGSAGAAF AVRSAEEGKR VLLIEAGHDY RSAEMHEAWR SPNPAVAIME
     PDAIEGMMWT GLNATRTDSQ PEAMYWRGKG VGGSSSVNGQ IAIRPPLEDF DEWSRSGCEG
     WSGAEVLPYF SKLENDEDFG AYEFHGDSGP TPIYRAPRNR WGAVDTALAD SALAAGHPWA
     ADVNAPQATG VSPYPINSHD SRRVSVNDAY LEGARGLPTL TILGEATVDR ILFENSRAVG
     VSLLTGENSE TRYADTVVLS AGVIHSPTIL LRSGIGPHHQ LESLGIDVLA DLPVGQGLQD
     HAMASITLPL NDSSGISSPD DRHTNVCVRW SSGPEEGTEI VRYNDLMFVS MNQSVISMAT
     ANTGAEYGAF GVWLNQADSR GTVTLTSADP HAQPAVAERM LSETGDRARL RAGIRAAVKL
     LEQDATQAIL GGSVKDCNEE LFSVLDDDDA LDAHLLTTVA DAQHGTSTCR MGRADDPTTV
     VDSDCRVHGI ENLYIVDASI FPSVPRANTN LASIMVGELM ADRID
//