ID A0A166UDK9_9RHOB Unreviewed; 523 AA.
AC A0A166UDK9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=2-keto-gluconate dehydrogenase {ECO:0000313|EMBL:KZY05586.1};
GN ORFNames=A3721_14390 {ECO:0000313|EMBL:KZY05586.1};
OS Sulfitobacter sp. HI0023.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZY05586.1, ECO:0000313|Proteomes:UP000077323};
RN [1] {ECO:0000313|EMBL:KZY05586.1, ECO:0000313|Proteomes:UP000077323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0023 {ECO:0000313|EMBL:KZY05586.1,
RC ECO:0000313|Proteomes:UP000077323};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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:KZY05586.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWEQ01000051; KZY05586.1; -; Genomic_DNA.
DR RefSeq; WP_067925028.1; NZ_LWEQ01000051.1.
DR AlphaFoldDB; A0A166UDK9; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000077323; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000077323}.
FT DOMAIN 88..305
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 391..509
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 523 AA; 57050 MW; 42B869D98CDCFC6E CRC64;
MAAPFDKNDD SVVVVIGTGA GGGVLANELA QKGISVVALE AGGRYLPEDY INDEWESFGQ
LAWLDPRTTS GDWRVAKDFS GLPAWIVKAV GGTTTHWAGA SIRFQPHEWK AKTTYGEVEG
ASLLDWPIDG EEMAPYYTKA EDKLGVTRTG GREGLPGCNN YLVFEAGAKK LGYKEVHTGK
MAINSDWYDD RMPCQQTGFC FQGCKWGAKW SAAYTDIPRG EATGNLEVRE KAHVARILHD
DSGKVTGVEY FDEKGDLQMQ KARIVAVAGN SFESPRLLLN SASNMFPNGL ANSSDQVGRN
YMRHMTGSVY GVFDKPVKMW RGTTMAGIIQ DEAKHDPSRG FVGGYELETL SLGLPFMAAF
LDPGAWGREF TTALDMYENM AGMWIVGEDM PQSDNRVTLN TEVKDQFGLP VANVHFSDHP
NDVAMRNHAY KQGAAIYDAV GATRTFPTPP YPSTHNLGTN RMSEKAEDGV VNKWGQTHDI
KNLFVSDGSQ FTTGAAENPT LTIVALAIRQ ADHIASEMGA GNI
//
