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
//