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Database: UniProt
Entry: A0A0Q5LRS0_9MICO
LinkDB: A0A0Q5LRS0_9MICO
Original site: A0A0Q5LRS0_9MICO 
ID   A0A0Q5LRS0_9MICO        Unreviewed;       339 AA.
AC   A0A0Q5LRS0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:KQR47337.1};
GN   ORFNames=ASF82_05365 {ECO:0000313|EMBL:KQR47337.1};
OS   Frigoribacterium sp. Leaf164.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR47337.1, ECO:0000313|Proteomes:UP000051005};
RN   [1] {ECO:0000313|EMBL:KQR47337.1, ECO:0000313|Proteomes:UP000051005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47337.1,
RC   ECO:0000313|Proteomes:UP000051005};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR47337.1, ECO:0000313|Proteomes:UP000051005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47337.1,
RC   ECO:0000313|Proteomes:UP000051005};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQR47337.1}.
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DR   EMBL; LMOX01000001; KQR47337.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5LRS0; -.
DR   STRING; 1736282.ASF82_05365; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000051005; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051005};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          5..337
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  35966 MW;  C004B5B547ED9BD0 CRC64;
     MYKSGDVRVV EVPDPVIQQP TEALIRVTYA CVCGSDLHPY HDLGDTPEGR RMGHEAIGVV
     EEIGEDVRTL SVGDTVIVPF AWSDGTCPFC QDGITTACIH GGFFDGAASA TQAEKLIVPQ
     ADGTAVVIPE GTDEALMPSL LTLSDVYLTG YHAAIRGDVE HGKTVTVIGD GAVGLSAVLA
     SKQLGAETII LMGRHTTRTD LGREFGATHV VPERGDEGVA KVMEITGGEG SHVVLEAVGH
     MPAYEQAYKI VRAGGTISRV GVPQYEEAAV GMASLFGKNV TLTGGPATVR AYLEQVLPQV
     LDGSIDPGRV FDREMPLDDI AEAYRLMDDR EALKVLIRP
//
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