ID A0A0B4BXH0_9RHOB Unreviewed; 560 AA.
AC A0A0B4BXH0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=RA20_15950 {ECO:0000313|EMBL:KIC16911.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC16911.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(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, ECO:0000256|RuleBase:RU003968}.
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:KIC16911.1}.
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DR EMBL; JWLD01000047; KIC16911.1; -; Genomic_DNA.
DR RefSeq; WP_039130881.1; NZ_JWLD01000047.1.
DR AlphaFoldDB; A0A0B4BXH0; -.
DR STRING; 1577896.RA20_15950; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000031177; 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.
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 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 249..263
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 560 AA; 59559 MW; 19188E031251E169 CRC64;
MSPEFDYIIA GGGSAGCVLA ARLCENPKLK VLLVEAGGPG KSIFARMPAG VGMIHSNPKY
DWCYMSTPQA ALGGRQLYYP RGKGLGGSSL MNGMIYIRGN AGDYDRWRQK GLTGWSYGDV
LPYYRRAAGA AHRAGEAHHG TKGPLKITPA GNYDRINQVF VEACHQAGAP LNPDFNGASQ
AGTGRMDVKT SGGVRQSTAE AYLTPHPKNL TVLTGTPVLK VLTEGRRATG ILTGQGKFHA
RGEVILSLGA FESPKLLMLS GIGPGAHLQE HGIQVVNDLP GVGQSLLDHP NMPVQFGLTD
PSLSMARFQR LDKAALMGAQ WLLTKSGPAA SPFWASVLFH SIRDRDMPEL EVFFTPMVVR
EDSAAGAKGF SLQTFNHLGK AMIARGKIAG PGLQFDVNLL RPRSSGTVTL ASPGPLQPPR
IDAGYFSDES DFLDLIEGIK HTRKVVRQKA FQGLADEELS PGAAKQSDAD LRQSIRGLVT
TGHHPACTAR IGADSDPGAV LDLDFRVRGM EGLRVVDAAA LPDMVSGNIG APVIMLAERA
ADMILGRPQL SADDPRETAA
//
