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Database: UniProt
Entry: B2HLS8_MYCMM
LinkDB: B2HLS8_MYCMM
Original site: B2HLS8_MYCMM 
ID   B2HLS8_MYCMM            Unreviewed;       286 AA.
AC   B2HLS8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Short-chain type dehydrogenase/reductase {ECO:0000313|EMBL:ACC38827.1};
GN   OrderedLocusNames=MMAR_0360 {ECO:0000313|EMBL:ACC38827.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC38827.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC38827.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; CP000854; ACC38827.1; -; Genomic_DNA.
DR   RefSeq; WP_011742271.1; NC_010612.1.
DR   AlphaFoldDB; B2HLS8; -.
DR   STRING; 216594.MMAR_0360; -.
DR   GeneID; 72436407; -.
DR   KEGG; mmi:MMAR_0360; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_14_0_11; -.
DR   OrthoDB; 9808187at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 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; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
SQ   SEQUENCE   286 AA;  29786 MW;  17548ADA7473B12B CRC64;
     MPGVQDRVVV VTGAGGGLGR EYALTLAREG ASVVVNDLGG ARDGTGAGSA MADQVVTEIR
     EGGGRAVANY DSVATEDGAA NIIKTALDEF GAVHGVVSNA GILRDGTFHK MTSENWDAVL
     KVHLYGGYNV VRAAWPHFRE QSYGRVVVAT STSGLFGNFG QTNYGAAKLG LVGLINTLAL
     EGAKYNIHSN AVAPIAATRM TQDIMPPEVL EKLTPEFVAP VVAYLCTEEC ADNGSVFIVG
     GGKVQRAALF QNDGANFQTP PSVQDIAAQW AQITDLSGAQ KAGFKL
//
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