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   13-SEP-2023, entry version 118.
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; Pseudomonadota; 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 dehydrogenase
RT   gene on the CAM plasmid of Pseudomonas putida (ATCC 17453).";
RL   Biochim. Biophys. Acta 1174:91-94(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100, AND PROTEIN SEQUENCE OF 1-45.
RC   STRAIN=G1 / ATCC 17453;
RX   PubMed=3011733; DOI=10.1128/jb.166.3.1089-1095.1986;
RA   Koga H., Aramaki H., Yamaguchi E., Takeuchi K., Horiuchi T., Gunsalus I.C.;
RT   "camR, a negative regulator locus of the cytochrome P-450cam hydroxylase
RT   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:
CC       Reaction=(1R,4R,5R)-5-hydroxycamphor + NAD(+) = (1R,4R)-bornane-2,5-
CC         dione + H(+) + NADH; Xref=Rhea:RHEA:32879, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15392, ChEBI:CHEBI:15398, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.327;
CC         Evidence={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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D14680; BAA03511.1; -; Genomic_DNA.
DR   EMBL; M13471; AAA25762.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S34613; S34613.
DR   AlphaFoldDB; P09347; -.
DR   SMR; P09347; -.
DR   KEGG; ag:BAA03511; -.
DR   BioCyc; MetaCyc:MONOMER-3022; -.
DR   BRENDA; 1.1.1.327; 5092.
DR   UniPathway; UPA00719; -.
DR   GO; GO:0018452; F:5-exo-hydroxycamphor dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019383; P:(+)-camphor catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd08231; MDR_TM0436_like; 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; PTHR43401:SF1; ALCOHOL DEHYDROGENASE, ZINC-CONTAINING; 1.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..361
FT                   /note="5-exo-hydroxycamphor dehydrogenase"
FT                   /id="PRO_0000160826"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="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
//