ID   FDEH_PSEPU              Reviewed;         361 AA.
AC   P09347;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   09-DEC-2015, entry version 96.
DE   RecName: Full=5-exo-hydroxycamphor dehydrogenase;
DE            EC=1.1.1.327;
DE   AltName: Full=FDEH;
GN   Name=camD;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 97-100.
RC   STRAIN=G1 / ATCC 17453;
RX   PubMed=8334169; DOI=10.1016/0167-4781(93)90098-X;
RA   Aramaki H., Koga H., Sagara Y., Hosoi M., Horiuchi T.;
RT   "Complete nucleotide sequence of the 5-exo-hydroxycamphor
RT   dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC
RT   17453).";
RL   Biochim. Biophys. Acta 1174:91-94(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100, AND PROTEIN SEQUENCE OF
RP   1-45.
RC   STRAIN=G1 / ATCC 17453;
RX   PubMed=3011733;
RA   Koga H., Aramaki H., Yamaguchi E., Takeuchi K., Horiuchi T.,
RA   Gunsalus I.C.;
RT   "camR, a negative regulator locus of the cytochrome P-450cam
RT   hydroxylase operon.";
RL   J. Bacteriol. 166:1089-1095(1986).
RN   [3]
RP   CATALYTIC ACTIVITY.
RX   PubMed=4351810; DOI=10.1073/pnas.70.3.885;
RA   Rheinwald J.G., Chakrabarty A.M., Gunsalus I.C.;
RT   "A transmissible plasmid controlling camphor oxidation in Pseudomonas
RT   putida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:885-889(1973).
CC   -!- CATALYTIC ACTIVITY: 5-exo-hydroxycamphor + NAD(+) = bornane-2,5-
CC       dione + NADH. {ECO:0000269|PubMed:4351810}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; (R)-camphor degradation.
CC   -!- INDUCTION: By camphor.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; D14680; BAA03511.1; -; Genomic_DNA.
DR   EMBL; M13471; AAA25762.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S34613; S34613.
DR   RefSeq; WP_032488636.1; NG_034612.1.
DR   RefSeq; YP_009074425.1; NG_034612.1.
DR   ProteinModelPortal; P09347; -.
DR   KEGG; ag:BAA03511; -.
DR   KO; K19649; -.
DR   BioCyc; MetaCyc:MONOMER-3022; -.
DR   BRENDA; 1.1.1.327; 5092.
DR   UniPathway; UPA00719; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019383; P:(+)-camphor catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.180.10; -; 1.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002085; ADH_SF_Zn-type.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR11695; PTHR11695; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    361       5-exo-hydroxycamphor dehydrogenase.
FT                                /FTId=PRO_0000160826.
FT   METAL        40     40       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        98     98       Zinc 2. {ECO:0000250}.
FT   METAL       101    101       Zinc 2. {ECO:0000250}.
FT   METAL       104    104       Zinc 2. {ECO:0000250}.
FT   METAL       170    170       Zinc 1; catalytic. {ECO:0000250}.
SQ   SEQUENCE   361 AA;  38460 MW;  283B1A72328B5F39 CRC64;
     MQYARAAVMV EQNRVETWEV PIFDPAPGGA LVRVVLGGVC GSDVHIVSGE AGAMPFPIIL
     GHEGIGRIEK LGTGVTTDYA GVPVKQGDMV YWAPIALCHR CHSCTVLDET PWDNSTFFEH
     AQKPNWGSYA DFACLPNGMA FYRLPDHAQP EALAALGCAL PTVLRGYDRC GPVGLDDTVV
     VQGAGPVGLA AVLVAAASGA KDIIAIDHSP IRLDMARSLG ATETISLADT TPEERQRIVQ
     ERFGKRGASL VVEAAGALPA FPEGVNLTGN HGRYVILGLW GAIGTQPISP RDLTIKNMSI
     AGATFPKPKH YYQAMQLAAR LQDRYPLADL ITQRFSIDEA SKALELVKAG ALIKPVIDST
     L
//