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}.
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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 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
//