ID N9H5X0_ACILW Unreviewed; 387 AA.
AC N9H5X0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=F924_02241 {ECO:0000313|EMBL:ENW27215.1};
OS Acinetobacter lwoffii ATCC 9957 = CIP 70.31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1311804 {ECO:0000313|EMBL:ENW27215.1, ECO:0000313|Proteomes:UP000013033};
RN [1] {ECO:0000313|EMBL:ENW27215.1, ECO:0000313|Proteomes:UP000013033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 70.31 {ECO:0000313|EMBL:ENW27215.1,
RC ECO:0000313|Proteomes:UP000013033};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter lwoffii CIP 70.31.";
RL Submitted (FEB-2013) 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|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:ENW27215.1}.
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DR EMBL; APQT01000046; ENW27215.1; -; Genomic_DNA.
DR RefSeq; WP_005104957.1; NZ_KB849830.1.
DR AlphaFoldDB; N9H5X0; -.
DR PATRIC; fig|1217667.3.peg.2127; -.
DR HOGENOM; CLU_026673_11_3_6; -.
DR Proteomes; UP000013033; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..385
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 387 AA; 41844 MW; 97D45E82DD56C768 CRC64;
MRALTYHGAR DVRVESVPDP VIQEPDDVIL RVTATAICGS DLHLYRGKIP ATEDGDIFGH
EFMGIVEEVG PEVTEVKKGD RVIIPFVIAC GHCFFCEHEL MAACENTNTG RGAILNKKQI
PPGAALFGFS HLYGGIPGGQ AEYVRIPKGN VGPFKVPGSL PDEKVLFLTD ILPTAWQAVN
NAQVGRGSSV AIYGAGPVGL LAAACARMLG AEQIFMVDHH PYRLSFAHQT YGVIPVNFDE
VDAAEFIIQN TTGYRGVDAV IDAVGFEAKG SMLETVMTNL KLEGSSGSAL RQCIAAVRRG
GVVSVPGVYA GPIHGFLFGD AFDKGLTFKM GQTHVHNYLP QLLEHIENGD LSPDLIITHR
MKLEDAAEGY RIFDKKEEDC RKVILTP
//
