ID A0A1Q4W177_9ACTN Unreviewed; 584 AA.
AC A0A1Q4W177;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:OKI03798.1};
GN ORFNames=AMK13_26065 {ECO:0000313|EMBL:OKI03798.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI03798.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI03798.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI03798.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(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:OKI03798.1}.
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; LIPD01000009; OKI03798.1; -; Genomic_DNA.
DR RefSeq; WP_074004313.1; NZ_LIPD01000009.1.
DR AlphaFoldDB; A0A1Q4W177; -.
DR OrthoDB; 4220752at2; -.
DR Proteomes; UP000186379; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186379}.
FT DOMAIN 38..151
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 584 AA; 63265 MW; D6247ABCF733398D CRC64;
MTFPTKPQAQ AKPPVRRRTV HSGGLPLAVF EQGDPAAPTV LLVHGYPDTH TVWDDIAADL
ARDHHVVRYD VRGAGESAAP ADRSGYRLEH LAEDLFAVAD AVSPDRPVHL LAHDWGSIQS
WEAVTASGAE RRIASYTTLS GPSLDHMGHW LRHRLRRPTP RHLGQLLHQG LHSWYITAFH
LPYLAPGVWR LGLARAWPRV LRDLEHVTPR ADHPQPTLRR DAVRGIELYR ANFRPTLGSP
RERPTEVPVQ LITLTRDRYV GTYLSEGLER WAPNLTRRTL HAGHWSALLE KGATVAGLVR
EFTTRTDEGR ARPEEGDGRL VVVTGGGSGI GRATALAFAE DGARVVVCDL DLAAAERTAE
LASLIGPQAH AYRVDVSDGA AVDAFAQTVA AEHGVPDVMV NNAGIGHSGT FLQTTEKEWQ
RVLDVNLWGV IHGCRAFGTL MADRGQGGHI VNVSSAAAYL PSKALTAYAT SKAAVFMLSD
CLRAEFVGHG IGVSTICPGI VNTNITRTST FSATTSTEQA AKQARAAKLY ARRGFPPEKV
ATAIVTAVRT GRPVVPVTPE AKAARFLSRL SPGLLRLAAR LNIT
//