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Database: UniProt
Entry: A0A254QJV2_9RHOB
LinkDB: A0A254QJV2_9RHOB
Original site: A0A254QJV2_9RHOB 
ID   A0A254QJV2_9RHOB        Unreviewed;       542 AA.
AC   A0A254QJV2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OWU71561.1};
GN   ORFNames=ATO1_23350 {ECO:0000313|EMBL:OWU71561.1};
OS   Phaeobacter sp. 22II1-1F12B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU71561.1, ECO:0000313|Proteomes:UP000197279};
RN   [1] {ECO:0000313|EMBL:OWU71561.1, ECO:0000313|Proteomes:UP000197279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU71561.1,
RC   ECO:0000313|Proteomes:UP000197279};
RA   Lai Q., Li G., Shao Z.;
RT   "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL   Submitted (APR-2013) 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}.
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:OWU71561.1}.
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DR   EMBL; AQQP01000024; OWU71561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254QJV2; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000197279; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197279}.
FT   DOMAIN          79..102
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          255..269
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         89..92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         218
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   542 AA;  59351 MW;  8C3E1B1E064928F3 CRC64;
     MYDYIIVGAG SAGCVLANRL SANPAKRVAL IEAGPKDKSP LIHMPLGIAL LANSKKLNWA
     FDTEPQEHLN GRKLFWPRGK TLGGSSSINA MVYIRGHKAD YDYWASEAGT DVWGWDRMTD
     LFKRIEDNHR FGATETHGRG GELSVSELKT VNPLSRDFVQ AGRELQIPHN GDFNSAEQEG
     LGMYQVTQKD GRRWSSAQAF LRGAEARSNL EIFTDARVTR VVMEEKTATG VTLQKSGEYR
     QLRLNDGGEV ILSGGAVNSP QLLLLSGIGD AQEIKRHGLA VVHDLPEVGK NMADHLDVTI
     MHAASSRRPI GVAPSFLPRG IGGLFSYIFR RKGFLTSNVA ESGGFIKSSP ERDRPNVQFH
     FLPTYLKDHG RKIAFGYGYT LHICDLLPKS RGYIGLKSPD PMDDPLIQPN YLSDPEDMGT
     MIAAFKAGRR ILEAPAMSVH SKYEVHPGKS VQTDDEIAAF IRESAETIYH PVGTCRMGAD
     KDSVVDPELK VRGVSGLRVV DASIMPSLVA GNTNAPTMVI AENAAEIILG QVRIFNRSRS
     VA
//
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