ID D5HBY9_SALRM Unreviewed; 455 AA.
AC D5HBY9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:CBH25544.1};
GN OrderedLocusNames=SRM_02623 {ECO:0000313|EMBL:CBH25544.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH25544.1, ECO:0000313|Proteomes:UP000000933};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M8;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-95(2010).
RN [2] {ECO:0000313|EMBL:CBH25544.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH25544.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [3] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FP565814; CBH25544.1; -; Genomic_DNA.
DR AlphaFoldDB; D5HBY9; -.
DR KEGG; srm:SRM_02623; -.
DR PATRIC; fig|761659.10.peg.2861; -.
DR HOGENOM; CLU_023205_2_1_10; -.
DR Proteomes; UP000000933; Chromosome.
DR CDD; cd19076; AKR_AKR13A_13D; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43625; AFLATOXIN B1 ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR43625:SF77; ALDO-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE 4: Predicted;
FT DOMAIN 145..436
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 50493 MW; C6DC4B2F50E79154 CRC64;
MRPGPAARRR SCTRPRTGSR HSWTCCWSTG PTPRRRTSRA KRPPSRPPRK GTRRSPSGCG
RPRRGREHQR TGTRPCIRRR VSERAARSAP FGPVDAAPRR AAQQPVGGGV GLRGTSFYYA
ILSPDPTRTV KQRTLGTSTL TVSAVGLGCM GMSDFYGTPD ENRAIKTLQR ALDRGLTFFD
SADIYGPFTN EKLLGRVLDA HRHRVTIATK FGIVRDEAGE MHGLNGRPSY VKTACEDSLQ
RLGVDTIDLY YLHRVDPEVP IEHTVGAMGR LVEEGKVRHL GLSEVAADTL RRANEEHSIT
ALQTEYSLWS RDPEDDILPT CRELGIGFVP YSPLGRGFLT GRFQSPEDLP EDDWRRHNPR
FQGENFQKNL DLVAEVNRLA DAKDVTPAQL ALAWVLHQGD DIVPIPGTTD PDHLDENIAA
LDVSLSEEEL ARIDEIAPQG VAAGDRYPDM STVNR
//
