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Database: UniProt
Entry: B1LX15_METRJ
LinkDB: B1LX15_METRJ
Original site: B1LX15_METRJ 
ID   B1LX15_METRJ            Unreviewed;       292 AA.
AC   B1LX15;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ACB25720.1};
GN   OrderedLocusNames=Mrad2831_3745 {ECO:0000313|EMBL:ACB25720.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB25720.1, ECO:0000313|Proteomes:UP000006589};
RN   [1] {ECO:0000313|EMBL:ACB25720.1, ECO:0000313|Proteomes:UP000006589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC   0-1 {ECO:0000313|Proteomes:UP000006589};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; CP001001; ACB25720.1; -; Genomic_DNA.
DR   RefSeq; WP_012320679.1; NC_010505.1.
DR   AlphaFoldDB; B1LX15; -.
DR   STRING; 426355.Mrad2831_3745; -.
DR   KEGG; mrd:Mrad2831_3745; -.
DR   PATRIC; fig|426355.14.peg.3830; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_4_0_5; -.
DR   OrthoDB; 9809287at2; -.
DR   Proteomes; UP000006589; Chromosome.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR48107:SF16; NADPH-DEPENDENT ALDEHYDE REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  30618 MW;  4672A0E0A135BF40 CRC64;
     MTQDPREAGP RPPFPGDQQQ PRPGLTTKMT PRPDHGEESY VGKGLLTGQV ALITGGDSGI
     GRAVAIAYAR EGADVAISYL EVEQEDAEDT RAWVEKAGRR CLLLPGDIRD AAQCRDLVAR
     TVEAFGRLDI LVNNAAAQVV NEGLDDLAAP DIEGSFRANV FAMYYLAQAA VPHMKPGGAI
     VNSTSVQAKV ADPSMLIYAA TKGAIASLTI GLSNLLAPKG IRVNCVAPGP VWTPIQPIVK
     SPDQIEQLGA QTPLGRAGQP AELAPAYVLL ASREGSYMSG ALVPVTGGMP ML
//
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