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Database: UniProt
Entry: V9GIC3_9BACL
LinkDB: V9GIC3_9BACL
Original site: V9GIC3_9BACL 
ID   V9GIC3_9BACL            Unreviewed;       372 AA.
AC   V9GIC3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:GAE08419.1};
GN   ORFNames=JCM10914_4712 {ECO:0000313|EMBL:GAE08419.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE08419.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE08419.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE08419.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, 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:GAE08419.1}.
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DR   EMBL; BAUO01000022; GAE08419.1; -; Genomic_DNA.
DR   RefSeq; WP_023964071.1; NZ_BAZR01000022.1.
DR   AlphaFoldDB; V9GIC3; -.
DR   STRING; 1236974.GCA_001315105_04609; -.
DR   OrthoDB; 9806940at2; -.
DR   Proteomes; UP000018028; 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; cd08278; benzyl_alcohol_DH; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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:UP000018028};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          9..362
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   372 AA;  39841 MW;  B6EC4D6D384C221F CRC64;
     MKVKAAVINE VDSPYVLEEL TLSDIREDEI LVKMVASGIC HSDAVARAGG YPWYPVVLGH
     EGSGIVEKVG SAVRGFEPGD HVVLSYLYCG HCSNCLTGLP ASCEEWMNFN LSGAREDGSL
     YFQREDGSPV YNFVSQSSFS THTIVYERNL TKVDKSVDLR LVGPLGCGFL TGSGTVLNGL
     KPSPGSTIAI FGTGAVGLAA MMAAKISGCS QIIGVDIHDN RLEVAKQLGA THTINSKDVD
     VLSEIKRLTN DKGVNYSIDT TGVPSVARTS IEILAVGGVA APIASSKHGV EVNFNADLNM
     LNRTIKGVLM GNAVPQLSIP QLIQFYKDGQ FSFDQLVKFY KFDEINEASH DSSTGKTIKP
     ILIIDEDYVP GT
//
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