ID A0A1A0U8W6_9MYCO Unreviewed; 665 AA.
AC A0A1A0U8W6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Short chain dehydrogenase {ECO:0000313|EMBL:OBB67488.1};
GN ORFNames=A5758_13805 {ECO:0000313|EMBL:OBB67488.1};
OS Mycobacterium sp. 852014-50255_SCH5639931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB67488.1, ECO:0000313|Proteomes:UP000092113};
RN [1] {ECO:0000313|EMBL:OBB67488.1, ECO:0000313|Proteomes:UP000092113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB67488.1,
RC ECO:0000313|Proteomes:UP000092113};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OBB67488.1}.
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DR EMBL; LZSV01000017; OBB67488.1; -; Genomic_DNA.
DR RefSeq; WP_067739935.1; NZ_LZSV01000017.1.
DR AlphaFoldDB; A0A1A0U8W6; -.
DR STRING; 1834112.A5758_13805; -.
DR OrthoDB; 9810734at2; -.
DR Proteomes; UP000092113; 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 5..227
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT REGION 625..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 72563 MW; 0BC94C21A278A95A CRC64;
MRYVVTGGTG FIGRRVVDRL LETRPDAQVW VLVRRQSLGR FERLAAGWGE RAKALVAGLP
ELELTDETLA ELGRIDHVVH CAAIYDITAG EAEQRATNVE GTRAVIELAQ RLGATLHHVS
SIAVAGDFSG EYTEDDFDVG QQLPTPYHQT KFEAELLVRS APGLHYRIYR PAVVVGDSRT
GEMDKVDGPY YFFGVLAKLA LLPSLTPILL PDTGRTNIVP VDYVADALVA LMHAEGLDGR
TFHLTAPKTV GLRGIYRGVA KAAGLPPARG SLPGSVAAPV LKVRGRARVL RNMAATQLGI
PAEVFDLVDL KPTFVSDQTR KALRGTGIDV PEFSSYAPQL WRYWAEHLDP DRARRDDPKG
PLRGRHVIIT GASSGIGRAA AIAVAERGAT VFALARNAEA LDELVAEIRA GGGDAHAFTC
DVTDSTSVEH TIKDILGRFD HVDYLVNNAG RSIRRSVVNS TDRLHDYERV MAVNYFGSVR
MVLALLPHWR ERRFGHVVNV SSAGVQARNP KYSSYLPTKA ALDAFADVVG SETLSDHITF
TNIHMPLVRT PMIAPSHRLN PVPAISPERA AAMVVRGLVE KPARIDTPLG TLAEVGNYFA
PRTSRRILHQ LYLGYPDSAA ARGLTTEPVA APPRKPRRPA RGVTRGIRTP RSVKRLVRLM
PGVHW
//
