ID   Q0P877_CAMJE            Unreviewed;       358 AA.
AC   Q0P877;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=NADP-dependent alcohol dehydrogenase {ECO:0000313|EMBL:CAL35648.1};
DE            EC=1.1.1.2 {ECO:0000313|EMBL:CAL35648.1};
GN   OrderedLocusNames=Cj1548c {ECO:0000313|EMBL:CAL35648.1};
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL35648.1, ECO:0000313|Proteomes:UP000000799};
RN   [1] {ECO:0000313|EMBL:CAL35648.1, ECO:0000313|Proteomes:UP000000799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA   Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA   Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA   Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AL111168; CAL35648.1; -; Genomic_DNA.
DR   PIR; B81302; B81302.
DR   RefSeq; WP_002851455.1; NZ_SZUC01000003.1.
DR   RefSeq; YP_002344920.1; NC_002163.1.
DR   AlphaFoldDB; Q0P877; -.
DR   STRING; 192222.Cj1548c; -.
DR   PaxDb; 192222-Cj1548c; -.
DR   EnsemblBacteria; CAL35648; CAL35648; Cj1548c.
DR   GeneID; 904495; -.
DR   KEGG; cje:Cj1548c; -.
DR   PATRIC; fig|192222.6.peg.1525; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_2_7; -.
DR   OrthoDB; 5295340at2; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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   ECO:0000313|EMBL:CAL35648.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          18..353
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   358 AA;  38962 MW;  DD44C777F86D0CFA CRC64;
     MQYKILENNR IASKGYAMLS KDAKFTPFEF SRHAIGDNDI LIKILYAGIC HSDIHTARSE
     WGEATYPCVP GHEIAGEVIA VGKNVSKFKV GDYAGVGCMV NSCGECDACK RSQEQFCENG
     KTIFTYNSCD VFHGNENTYG GYSNNIVVSE KFAVCVPKDA PMEKVAPLLC AGITTYSPLK
     FSNIKEGSSV AVAGFGGLGM MAVKYAVKMG AKVSVFARNE NKKADALAMG VSSFYTSCDK
     NAVKERFDLI ISTIPTPYNP AIYLDLLKFG GEMAIVGLPP HEVAPSISVI TFVHKAGKKV
     YGSLIGGIAE TQEMLDFSLK HGIYPETELI TPQEIDKAYE NLTSGKAKFR YVIDMTKE
//