ID FDEH_PSEPU STANDARD; PRT; 361 AA. AC P09347; DT 01-MAR-1989 (REL. 10, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE 5-EXO-ALCOHOL DEHYDROGENASE (EC 1.1.1.-) (FDEH). GN CAMD. OS PSEUDOMONAS PUTIDA. OC BACTERIA; PROTEOBACTERIA; GAMMA SUBDIVISION; PSEUDOMONAS GROUP; OC PSEUDOMONAS. RN [1] RP SEQUENCE FROM N.A., AND REVISIONS TO 97-100. RC STRAIN=ATCC 17453; RX MEDLINE; 93326643. 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 SEQUENCE OF 1-100 FROM N.A., AND SEQUENCE OF 1-45. RC STRAIN=ATCC 17453; RX MEDLINE; 86223770. 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). CC -!- CATALYTIC ACTIVITY: 5-EXO-HYDROXYCAMPHOR + NAD(+) = CC 2,5-DIKETOCAMPHOR + NADH. CC -!- COFACTOR: THIS IS A ZINC-CONTAINING DEHYDROGENASE. CC -!- PATHWAY: SECOND STEP FOR CATABOLISM OF CAMPHOR. CC -!- INDUCTION: BY CAMPHOR. CC -!- SIMILARITY: BELONGS TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G473746; -. DR EMBL; M13471; G551925; ALT_SEQ. DR PIR; A29844; A29844. DR PROSITE; PS00059; ADH_ZINC; 1. DR PFAM; PF00107; adh_zinc; 1. DR HSSP; P07846; 1SDG. KW OXIDOREDUCTASE; ZINC; NAD. FT METAL 40 40 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 62 62 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 98 98 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 101 101 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 104 104 ZINC (SECOND ATOM) (BY SIMILARITY). FT METAL 170 170 ZINC (CATALYTIC) (BY SIMILARITY). SQ SEQUENCE 361 AA; 38460 MW; E46D28F7 CRC32; 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 //