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Database: UniProt
Entry: S3X8H1_9ACTN
LinkDB: S3X8H1_9ACTN
Original site: S3X8H1_9ACTN 
ID   S3X8H1_9ACTN            Unreviewed;       339 AA.
AC   S3X8H1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=HMPREF1531_01046 {ECO:0000313|EMBL:EPH05617.1};
OS   Propionibacterium sp. oral taxon 192 str. F0372.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH05617.1, ECO:0000313|Proteomes:UP000014567};
RN   [1] {ECO:0000313|EMBL:EPH05617.1, ECO:0000313|Proteomes:UP000014567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0372 {ECO:0000313|EMBL:EPH05617.1,
RC   ECO:0000313|Proteomes:UP000014567};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL   Submitted (MAY-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:EPH05617.1}.
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DR   EMBL; ATFL01000005; EPH05617.1; -; Genomic_DNA.
DR   RefSeq; WP_016668851.1; NZ_KE340297.1.
DR   AlphaFoldDB; S3X8H1; -.
DR   STRING; 1203605.HMPREF1531_01046; -.
DR   PATRIC; fig|1203605.3.peg.1091; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_11; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000014567; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000014567};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          7..337
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  35568 MW;  888F89F92FC48E68 CRC64;
     MRGVIMHAPK DVRVDDVPTP GIVEPTDAII KLSAACICGS DLWPYRGQEP TNNAPMGHEY
     VGVVTEVGSE VTTVAPGDLV IGSFCLSCGK CEICRSGYPS RCINGGFISG TQAEMARVPL
     ADGTLVKASS ATPLTPQKLR SYLAASDVLG TGWFGAVAAE TGPGKTVVVV GDGAVGLMAV
     LAAKQLGAER IIAMSRHADR QQLAREFGAT DIVAERGDEG VAKVKELTGG LGAHSVVEAV
     GTHASMQQAI SCCRPGGHVG FVGVSHDQTL DGLQLFFSQI HLHGGPAPVR RFLPDLIKLI
     DDEVIDPGKV FTLTLPLEEA ARGYEAMDKR EAIKVFLEV
//
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