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Database: UniProt
Entry: A4TD52_MYCGI
LinkDB: A4TD52_MYCGI
Original site: A4TD52_MYCGI 
ID   A4TD52_MYCGI            Unreviewed;       261 AA.
AC   A4TD52;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ABP47013.1};
GN   OrderedLocusNames=Mflv_4545 {ECO:0000313|EMBL:ABP47013.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47013.1};
RN   [1] {ECO:0000313|EMBL:ABP47013.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47013.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP47013.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47013.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; CP000656; ABP47013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TD52; -.
DR   STRING; 350054.Mflv_4545; -.
DR   KEGG; mgi:Mflv_4545; -.
DR   eggNOG; COG0300; Bacteria.
DR   HOGENOM; CLU_010194_2_1_11; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43899; RH59310P; 1.
DR   PANTHER; PTHR43899:SF13; RH59310P; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   261 AA;  27901 MW;  2FD0517631227FB6 CRC64;
     MTKYGPWAVI AGGSEGVGAE FAKALAEDGA NLVLIARKPQ PLDETAQECR RLGAQVRTIA
     LDLLDADSTS RIVDATSDVE VGLLIYNAGA STCNERFLDA ELSEFGKVID LNTTRMLELT
     QHFGRRMAAM SRGGIVLVGS LSGYMGAERH SVYAGAKAFS RVFAESLWLE LREHGVDVLE
     LVLGVTRTPA MERAGLNFDA PGIIVNDPAD VAREGLRHIA DGPVFIAGGN AERAARSSAP
     DRAAVVLGSH EMIKRLRGMR P
//
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