ADH8_PELPE
ID ADH8_PELPE Reviewed; 373 AA.
AC O57380;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=NADP-dependent alcohol dehydrogenase;
DE EC=1.1.1.2;
GN Name=ADH8;
OS Pelophylax perezi (Perez's frog) (Rana perezi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8403;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-373.
RC TISSUE=Stomach;
RX PubMed=10473548; DOI=10.1074/jbc.274.37.26021;
RA Peralba J.M., Cederlund E., Crosas B., Moreno A., Julia P., Martinez S.E.,
RA Persson B., Farres J., Pares X., Joernvall H.;
RT "Structural and enzymatic properties of a gastric NADP(H)-dependent and
RT retinal-active alcohol dehydrogenase.";
RL J. Biol. Chem. 274:26021-26026(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12554944; DOI=10.1107/s090744490201661x;
RA Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I.,
RA Pares X., Ochoa W.F.;
RT "Crystallization and preliminary X-ray analysis of NADP(H)-dependent
RT alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi.";
RL Acta Crystallogr. D 59:334-337(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
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 -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-IV subfamily. {ECO:0000305}.
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DR EMBL; AJ002554; CAA05553.1; -; mRNA.
DR PDB; 1P0C; X-ray; 2.20 A; A/B=1-373.
DR PDB; 1P0F; X-ray; 1.80 A; A/B=1-373.
DR PDBsum; 1P0C; -.
DR PDBsum; 1P0F; -.
DR AlphaFoldDB; O57380; -.
DR SMR; O57380; -.
DR SABIO-RK; O57380; -.
DR EvolutionaryTrace; O57380; -.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Metal-binding; NADP;
KW Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10473548"
FT CHAIN 2..373
FT /note="NADP-dependent alcohol dehydrogenase"
FT /id="PRO_0000160756"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 68
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 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 74
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="V -> M (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1P0F"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1P0F"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1P0F"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:1P0F"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1P0F"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:1P0F"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:1P0F"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1P0F"
SQ SEQUENCE 373 AA; 39168 MW; 954A502267E8DE49 CRC64;
MCTAGKDITC KAAVAWEPHK PLSLETITVA PPKAHEVRIK ILASGICGSD SSVLKEIIPS
KFPVILGHEA VGVVESIGAG VTCVKPGDKV IPLFVPQCGS CRACKSSNSN FCEKNDMGAK
TGLMADMTSR FTCRGKPIYN LVGTSTFTEY TVVADIAVAK IDPKAPLESC LIGCGFATGY
GAAVNTAKVT PGSTCAVFGL GGVGFSAIVG CKAAGASRII GVGTHKDKFP KAIELGATEC
LNPKDYDKPI YEVICEKTNG GVDYAVECAG RIETMMNALQ STYCGSGVTV VLGLASPNER
LPLDPLLLLT GRSLKGSVFG GFKGEEVSRL VDDYMKKKIN VNFLVSTKLT LDQINKAFEL
LSSGQGVRSI MIY
