ID Q63J31_BURPS Unreviewed; 413 AA.
AC Q63J31;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Aromatic hydrocarbons catabolism-related reductase {ECO:0000313|EMBL:CAH39363.1};
GN OrderedLocusNames=BPSS1885 {ECO:0000313|EMBL:CAH39363.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH39363.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH39363.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH39363.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; BX571966; CAH39363.1; -; Genomic_DNA.
DR RefSeq; WP_004556319.1; NZ_CP009537.1.
DR RefSeq; YP_111891.1; NC_006351.1.
DR AlphaFoldDB; Q63J31; -.
DR STRING; 272560.BPSS1885; -.
DR KEGG; bps:BPSS1885; -.
DR PATRIC; fig|272560.51.peg.5351; -.
DR eggNOG; COG0446; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR049657; AndAa.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR NCBIfam; NF041682; ant_diox_AndAa; 1.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT DOMAIN 7..303
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 323..408
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 413 AA; 43900 MW; 55B81DBE7CB761B4 CRC64;
MSTADPYLIA GGGHAARRAA ETLRERDAAA RIVMIGAEPE LPYDRPVLSK EALVGGDAGE
RRAFVRDAAW YRERDIELRL GVRVEAIERG ARRVRLSDGA RLGYARLLIA TGSRVRRFAG
PVDAGVHVHY VRTLADTRAL RAALAPGKRV AVLGGGFIGL EVAASAVRLG CRATVVDPAP
RLLQRGMPEA VGAFALALHA RHGVDVRLGA LPERIRRAAN GSAVVETSAG GIVADVVVAG
IGVVPNVELA QAAGLDVDDG VCVDEMCRTT DPAIFAAGEV TRHFNPLVGR ALRIESWQIA
ENQPAVAAAN MLGAAETYAQ WPWLWSDQYD CNLQTLGLFG GEQTLVLRGS PERDRAFCVF
ALNARRELAA VAAVNAGREI AVCRRLMTAG VALDPARLAD PSDALRAMLP RGV
//
