ID A0A2W2D2H9_9ACTN Unreviewed; 344 AA.
AC A0A2W2D2H9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=C1J01_42550 {ECO:0000313|EMBL:PZG06262.1};
OS Nonomuraea aridisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2070368 {ECO:0000313|EMBL:PZG06262.1, ECO:0000313|Proteomes:UP000249304};
RN [1] {ECO:0000313|EMBL:PZG06262.1, ECO:0000313|Proteomes:UP000249304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC333 {ECO:0000313|EMBL:PZG06262.1,
RC ECO:0000313|Proteomes:UP000249304};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Nonomuraea sp. KC333.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:PZG06262.1}.
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DR EMBL; POUD01000332; PZG06262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2D2H9; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000249304; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd05284; arabinose_DH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249304};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 36239 MW; F884FA2A85184C21 CRC64;
MKAVRLHEYT KRPVVEDVPD PQVRGPLDVL VEIGGAGLCR TDLHIVEGQW AQKSGVRLPY
TIGHENAGWV REIGPAVTNV RPGDAVILHP IVTCGLCRAC RAGDDVHCAN QRFPGIDTDG
GMAELLLTSA RSVVRLDESL RPADVAALAD AGLTAYHAVR KAVPLLYPGT RVVVIGAGGL
GHIGVQCLAA MTPAEVIVMD RSPAALELVK DLGAAHTVLA DGGQVEAVAD LTGGQGAHVV
LDFVGEGGAE REGVEMLRRA GSYFVIGYGG RVEIPTIDII SSEINVIGNL VGSYNDLDEL
MALAAQGKVR LHTRTYPLDA INEAMDDLDN GRLQGRGILV PGGR
//