ID H0T8W5_9BRAD Unreviewed; 567 AA.
AC H0T8W5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative oxidoreductase FAD/NAD(P)-binding domain {ECO:0000313|EMBL:CCE02892.1};
GN ORFNames=BRAS3809_6700002 {ECO:0000313|EMBL:CCE02892.1};
OS Bradyrhizobium sp. STM 3809.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCE02892.1, ECO:0000313|Proteomes:UP000004098};
RN [1] {ECO:0000313|Proteomes:UP000004098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
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:CCE02892.1}.
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DR EMBL; CAFJ01000635; CCE02892.1; -; Genomic_DNA.
DR RefSeq; WP_008965439.1; NZ_CAFJ01000635.1.
DR AlphaFoldDB; H0T8W5; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000004098; 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 107..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 418..534
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 546..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 62411 MW; 0E93B125EB910B04 CRC64;
MSDDPQATPR AIEGRAPDVF RPGGWVPMRC HRDEDAVDFV IVGTGAGGGT LACKLAEYGF
SVVALDAGPY FRPLEDFASD ESEQTKLYWT DDRISDGANP LQLGSNNSGK AVGGSTVHFA
MVSLRFRPEW FKSRTLLGYG ADWPIDWREM WNYYTEVEQA LKISGPITYP WGPKRPRYPY
RAHPLNAAAR VLAKGCEALG VSWTETPLAT LSAPRGLAHP CVYRGFCVAG CSTNAKQSAL
VTWIPRALAA GAEIRDLAMV GRIEVDDDDL VSGVHYHRGG RWHFQRARNV VVAGYAIETP
RLLLNSATDR HRDGLANSSG LVGKNLMTQS NQAVWGLMDD EIRSYKGPPS LAITEHWNYQ
DKGKDFFGGY AYMSQGPLPQ LWANTLAQAR GLWGARLVEE MTNYNHVAGL KIVGEMLPQE
RNRVTLADEV DQYGLRIPRV TYSWCDNDRR LIDHSLAFMT RALEAAGAKD IWTQDDDTCH
LNGTARMGDD PRASVVDADC RSWDIPNLWI CDGSVFPTVG GVNPSLTIQA IACRTADRIR
AMARRGELTG QRATGTRTAA HATSASS
//
