ID H8GRP2_DEIGI Unreviewed; 230 AA.
AC H8GRP2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:AFD25089.1};
GN Name=fabG {ECO:0000313|EMBL:AFD25089.1};
GN OrderedLocusNames=DGo_CA1162 {ECO:0000313|EMBL:AFD25089.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD25089.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD25089.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CP002191; AFD25089.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GRP2; -.
DR STRING; 745776.DGo_CA1162; -.
DR KEGG; dgo:DGo_CA1162; -.
DR PATRIC; fig|745776.4.peg.1197; -.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_010194_2_10_0; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05233; SDR_c; 1.
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; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR PANTHER; PTHR44196:SF5; POSSIBLE MULTI-FUNCTIONAL ENZYME WITH ACYL-COA-REDUCTASE ACTIVITY ACRA1; 1.
DR Pfam; PF00106; adh_short; 1.
DR PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
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}.
SQ SEQUENCE 230 AA; 23716 MW; 11D1C3122B55384F CRC64;
MTGAGKGIGL AVAEALAREG VHVALLARDR AALETAAGDL AGRYGVKTLA LSADVADRAA
VDTAVAQAAQ HLGGLDIVVN NAGTAQFGSV LDMDPEDWER MIQVNLLGTY YVTRAALPHM
VRQGGGNIVN VASTAGEKGA ATASAYAASK AGVIALTEAL MPEVRRHDIR VILLNPSTVN
TDLAANLGLR IGAEDHMLQP SDVADVLVSA LKLPARALVR NLSLLTTNPQ
//
