ID   A0A2V5LKA5_9MICC        Unreviewed;       537 AA.
AC   A0A2V5LKA5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=2-keto-gluconate dehydrogenase {ECO:0000313|EMBL:PYI67690.1};
GN   ORFNames=CVV68_09685 {ECO:0000313|EMBL:PYI67690.1};
OS   Arthrobacter livingstonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI67690.1, ECO:0000313|Proteomes:UP000247832};
RN   [1] {ECO:0000313|EMBL:PYI67690.1, ECO:0000313|Proteomes:UP000247832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LI2 {ECO:0000313|EMBL:PYI67690.1,
RC   ECO:0000313|Proteomes:UP000247832};
RA   Liu Q., Xin Y.-H.;
RT   "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT   and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT   glacialis sp. nov.";
RL   Submitted (MAY-2018) 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:PYI67690.1}.
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DR   EMBL; QJVD01000008; PYI67690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5LKA5; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000247832; 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   Pfam; PF13450; NAD_binding_8; 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          103..319
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          405..523
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   537 AA;  58072 MW;  44A8F103E93A274C CRC64;
     MSNETQQAFD AGSYESAHFE LDDDSVVVVV GSGAGGGTLA AELTRQGAKV VVLEAGPLLR
     NSDYINDEWP AFNQMAWLDP RTTSGSWRIA KDFPNLPTWL VKAVGGTTTH WAGATPRFKA
     HEFKARSTYG RIDGANLLDW PITLEDMAPY YDRAEQKIGS THRHGRPPLP ANNNYTVLAN
     GARLLGYRHY ATGPYGTNAE PYDGRPGSVQ DGFNFQGDRN GSKWSTLVAE LPKAVRTGLL
     DLRPDSQAIQ LTHTPAGVVD GVVYADGDGL LHRQLARTVA VAGNSIETPR LLLLSSSPLF
     PDGLANSSGQ VGRNYMRHTT GSVYARFEKP VHMYRGETMA GLIADESRFD ATRGFAGGYY
     LQTIALGPAF LASFIDPGAW GPDFTQMLDA YLNTAGLWIV GEDMPQEGNR VTLNTTVADK
     LGLPVPNVHV DDHPNDEAMR AHAYRQSELV YEAAGGVGTV RTPPYPSTHN LGTARMSERA
     EDGVCNKFGQ AHDVKNLFIS DGSAFTTGAA ANPTLTIVAL AIRQAEYIIN QMSTRAI
//