ID   A0A109K1C9_9BRAD        Unreviewed;       522 AA.
AC   A0A109K1C9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2-keto-gluconate dehydrogenase {ECO:0000313|EMBL:KWV58943.1};
GN   ORFNames=AS156_32625 {ECO:0000313|EMBL:KWV58943.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV58943.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV58943.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV58943.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:KWV58943.1}.
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DR   EMBL; LNCU01000034; KWV58943.1; -; Genomic_DNA.
DR   RefSeq; WP_066502459.1; NZ_LNCU01000034.1.
DR   AlphaFoldDB; A0A109K1C9; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000057737; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          87..304
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          390..508
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   522 AA;  56621 MW;  349CAB6306E1E12D CRC64;
     MAKFDLNDSG VVVIVGSGAG GGTLGNELAQ KGIKVVILEA GPRIENQDFI NDEWESFGQL
     AWSDMRTTSG TWRVHKDFPN IPAWIVKAVG GSTVHWAGAS LRFDEHEFKT KSAYGNMPGA
     NLLDWPITLA EMEPYYAKAE DKMGVTRTNG IPGLPGNNNF KVLEAGAKKL GYKEVHTGRM
     AINSEPRDGR GSCQQIGFCF QGCKSGAKWS TLYTEIPKGE ATGNLEVRPS SMVIKIEHDQ
     SGKVTGVVYA DATGAMQRQK ARVVAVAGNS IESPRLLLNS ASSMFPDGLA NSSGQVGRNY
     MRHMTGSVYA VFEKSVHMYR GTTMAGIIRD EAKNDPKRGF VGGYEMETLS LGLPFMAAFL
     NPGAWGRSFT SAMDGYSRMA GMWLVGEDMP RETNRVTLDP TIKDKFGMPV ASVHFDDHPN
     DVAMREHAYK QGAAVYEAVG ATVTYPTPPY PSTHNMGTNR MSEKPRDGVV NKFGQTHDIK
     NLFVSDGSQF TSGAACNPTL TIVSLAIRQA DTIAGAMQRK EI
//