ID A0A0R3MB25_9BRAD Unreviewed; 522 AA.
AC A0A0R3MB25;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2-keto-gluconate dehydrogenase {ECO:0000313|EMBL:KRR17508.1};
GN ORFNames=CQ14_36750 {ECO:0000313|EMBL:KRR17508.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR17508.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR17508.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR17508.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-2014) 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:KRR17508.1}.
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DR EMBL; LLYB01000120; KRR17508.1; -; Genomic_DNA.
DR RefSeq; WP_057862032.1; NZ_LLYB01000120.1.
DR AlphaFoldDB; A0A0R3MB25; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000051660; 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; 56504 MW; 9781F49646E2B006 CRC64;
MAKFDLNDSG VVVIVGSGAG GGTLGNELAQ KGVKVVILEA GSRIELQDFV NDEWESFTQL
AWSDMRTTSG SWRVAKDFPN LPAWIVKAVG GSTTHWAGAS LRFDEHEFKV KSAYGDIAGA
NLLDWPITLA EMEPWYTKAE DKMGVTRTNG IAGLPGNNNF KVMEAGAKKL GYKTVHTGNM
AINSEPRDGR GACQQIGFCF QGCKSGAKWS TLYTEIPRGE ATGNLEVRPN SMVIKIEHDA
SGKVTGVVYA DESGAMQRQK ARVVAVAGNS IESPRLLLNS ASNMFPNGLA NSSGQVGRNY
MRHMTGSVYA AFEKSVHMYR GTTMAGIIRD ESKNDPKRGF VGGYEMETLS IGVPFMAAFL
NPGAWGRSFT SAMESYPRMA GMWLVGEDMP QETNRITLDP KAKDKFGMPV ASVHFDDHPN
DVAMRNHAYK QGAAVYEAVG ATVTYPTPPY PSTHNLGTNR MSEKPKDGVV NKFGQTHDVK
NLFISDGSQF TSGAACNPTL TIVSLAIRQA DHIAGAMQRK EI
//
