ID   A0A100W1A9_9MYCO        Unreviewed;       685 AA.
AC   A0A100W1A9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Short chain dehydrogenase {ECO:0000313|EMBL:GAS89814.1};
GN   ORFNames=RMCB_3910 {ECO:0000313|EMBL:GAS89814.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS89814.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS89814.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS89814.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAS89814.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BCSX01000035; GAS89814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100W1A9; -.
DR   STRING; 146020.RMCB_3910; -.
DR   Proteomes; UP000069620; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05263; MupV_like_SDR_e; 1.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   Pfam; PF07993; NAD_binding_4; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          8..236
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   REGION          629..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  73733 MW;  5F83CA00F9A51BAC CRC64;
     MSGMRYVVTG GTGFIGRRVV SEILARDAYA EVWVLVRRAS LARFEQLAGE WGERAKPLVG
     DLTASDLGLT DADIADLGSG DDGISHVVHC AAIYDITVGE AEQQAANVEG TRAVIGLARR
     LDATLHHVSS IAVAGSYPGV YTEDDFDVAQ DLPTPYHQTK FEAELLVRSS PGLRYRVYRP
     AVVVGDSTTG EMDKVDGPYY FFGVLARLAA LPRFTPVMLP DSGRTNIVPV DYVVRALVHL
     MHAEGRDGET FHLTAPKTIG LRGIYRGVAE AAGLPPLRGS LPRAAAAPVL QVSGRAKTVR
     NMVATQLGIP GEVLDVVDLM PTFTAEHTTE ALRGTGITVP EFSSYAPQLW RYWAQHLNPD
     RARRDDPAGP LVGKHVIITG ASSGIGRASA IAVAERGGCV FALARNGQAL DDLVAEIRAA
     GGQAYAFTCD VTDSASVEHT VKDILGRFGH VDYLVNNAGR SIRRSVVNST DRLHDYERVM
     AVNYFGAVRM VLALLPHWRE RRFGHVVNVS SAGVQANSPK YSAYLPSKAA LDAFSEVVGT
     ETLSDHITFT NIHMPLVKTP MIAPSRKLNP VPPISAEHAA AMVVRGLVDK PARIDTPLGT
     LADFGNYLTP KLSRRVLHQL YLGYPDSAAA RGEAPPEPPA ALAPVSSSPM RRPKRPARTG
     ASLRVPRAVS RPVKRAVRLV PGVHW
//