ID H0TK38_9BRAD Unreviewed; 522 AA.
AC H0TK38;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative oxydoreductase, GMC family {ECO:0000313|EMBL:CCE06826.1};
GN ORFNames=BRAS3843_1840010 {ECO:0000313|EMBL:CCE06826.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE06826.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCE06826.1}.
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DR EMBL; CAFK01000095; CCE06826.1; -; Genomic_DNA.
DR RefSeq; WP_008969348.1; NZ_CAFK01000095.1.
DR AlphaFoldDB; H0TK38; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000002686; 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:UP000002686}.
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; 56612 MW; C23F9AE27BE8593E CRC64;
MAKFDQNDSS VVVIIGSGAG GGTLGNELAQ KGIKVVILEA GDRYEIPDFI NDEWDSFTQL
AWKDMRTTSG TWRVHQDFPN LPAWIVKAVG GSTVHWAGAS LRFDEHEFKA RTTYGAVPGA
NLMDWPVTLA EMEPWYAKAE FKMGVTRTNG IPGLPGNNNF KVLEAGAKRL GYKTVHTGNM
AINSEPRDGR GSCQQIGFCF QGCKSGAKWS TLYTEIPKGE ATGNLEVRPN SMAIKIEHDA
SGKVTGVVYA DGQGQMQLQK ARVVAVAGNS IESPRLLLNS ASNLFPDGLA NSSGQVGRNY
MRHMTGSVYA SFEQPVHMYR GTTMAGIIRD EAAHNPKRGF VGGYEMETLS LGLPFMAAFL
NPGAWGRSFT AAMETYPRMA GMWLVGEDMP QETNRITLDP TAKDKFGMPV ASVHFDDHPN
DLAMRAHAYK QGAAVYEAVG ATVTYPTTPY PSTHNLGTNR MSEKAKDGVV NKFGQTHDIK
NLFVSDGSQF TSGAACNPTL TIVALAIRQA DTIAGMMQKK EI
//
