ID A0A430JSU6_9ACTO Unreviewed; 340 AA.
AC A0A430JSU6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:RTE49884.1};
GN ORFNames=EKN07_05020 {ECO:0000313|EMBL:RTE49884.1};
OS Actinobaculum sp. 352.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=2490946 {ECO:0000313|EMBL:RTE49884.1, ECO:0000313|Proteomes:UP000273303};
RN [1] {ECO:0000313|EMBL:RTE49884.1, ECO:0000313|Proteomes:UP000273303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=352 {ECO:0000313|EMBL:RTE49884.1,
RC ECO:0000313|Proteomes:UP000273303};
RA Zhu W.;
RL Submitted (NOV-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|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:RTE49884.1}.
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DR EMBL; RQSN01000003; RTE49884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430JSU6; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000273303; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08287; FDH_like_ADH3; 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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000273303};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 35346 MW; 61D41736ADEA8BD5 CRC64;
MRGVIMNAPG DVTVGDREDP VIVEPTDAII KLAAACICGS DLWPYRGLEP VDQPRPMGHE
YVGTVTAVGD AVKNVKVGDF VVGSFCISDN TCEICESGYP SRCVNGGFMG DTQAEYTRVP
QADGTLVVVP GGKPDDPDII ASLLAASDVL GTGWFGAVAA EAGPGKTVAV VGDGAVGLSA
VLAAKALGAD KVIAFSRHED RAALARELGA DIVVAERGEE GAAKVKELTG GLGAHSVVEA
VGNQVSMDQA IASCRPGGHV GFVGVSHDQE IDGGALFFSE VHLHGGPAPV RRFLPDLIDR
ILKKEINPGK VFTMRIPLED AAEGYKAMDE RRAIKVLLQP
//
