ID A0A086H3H5_STRSC Unreviewed; 594 AA.
AC A0A086H3H5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:KFG02193.1};
GN ORFNames=IQ62_03035 {ECO:0000313|EMBL:KFG02193.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG02193.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG02193.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG02193.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KFG02193.1}.
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DR EMBL; JPPX01000040; KFG02193.1; -; Genomic_DNA.
DR RefSeq; WP_037689557.1; NZ_KL997396.1.
DR AlphaFoldDB; A0A086H3H5; -.
DR OrthoDB; 4220752at2; -.
DR Proteomes; UP000028722; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43391:SF12; OXIDOREDUCTASE EPHD-RELATED; 1.
DR PANTHER; PTHR43391; RETINOL DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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}.
FT DOMAIN 39..288
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 594 AA; 64702 MW; B05D4AC28974C33C CRC64;
MTEGGDVTDA VTLEGVRERR VRSGGVELCV AELGDPEQPT VVLVHGYPDT KEVWSEVAVR
LAERFHVVLY DVRGHGGSTA PEPLRGGFTL EKLTDDFLAV VDAVSPGHPV HLVGHDWGSV
QGWEFATVER TEGRIASFTS MSGPSLDHLG HWIKRRVKRP TPRRIGQLLG QGAKSWYVYV
LHTPVLPELA WRGPLGKQWP RLVRRAEKLP RGDYPSPSLP TDAAHGAWLY RDNMRARLAR
PRDDAYAHAP VQLITPLADQ FLSEQLYEDL ESWAPQLLRR TLPAKHWVPR TRPDQLAAWI
TEFVTATEGG RPAPVATGKY TDRFGGQLVL VTGAAGGIGR ATAFAFAEAG ARVVAVDLDT
EGAARTAELS RLIGAPEAWA EAVDVSDEQA MEKLSEKVAA EYGVVDVLVN NAGIGLSGSF
LDTTPEDWRK VLDVNLWGVI HGCRLFGRQM AERGQGGHIV NTASAAAYLP SRSLPAYSTS
KAAVLMLSEC LRAELAGQGI GVSAICPGIV NTNITSTARF AGVDAEEEKR RQRKTTRLYG
LRNYPPEKVA DAVLRAVVRN QAVVPVTPEA HGGRFMSRFA PRALRALARL EPPL
//