ID   AK1A1_PIG               Reviewed;         325 AA.
AC   P50578;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-JUL-2009, entry version 65.
DE   RecName: Full=Alcohol dehydrogenase [NADP+];
DE            EC=1.1.1.2;
DE   AltName: Full=Aldehyde reductase;
DE   AltName: Full=Aldo-keto reductase family 1 member A1;
GN   Name=AKR1A1; Synonyms=ALR, ALR1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96062952; PubMed=7484379;
RA   Flynn T.G., Green N.C., Bhatia M.B., El-Kabbani O.;
RT   "Structure and mechanism of aldehyde reductase.";
RL   Adv. Exp. Med. Biol. 372:193-201(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   MEDLINE=96022988; PubMed=7552731; DOI=10.1038/nsb0895-687;
RA   el-Kabbani O., Judge K., Ginell S.L., Myles D.A., DeLucas L.J.,
RA   Flynn T.G.;
RT   "Structure of porcine aldehyde reductase holoenzyme.";
RL   Nat. Struct. Biol. 2:687-692(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   MEDLINE=97469638; PubMed=9329083;
RX   DOI=10.1002/(SICI)1097-0134(199710)29:2<186::AID-PROT6>3.0.CO;2-B;
RA   El-Kabbani O., Carper D.A., McGowan M.H., Devedjiev Y.,
RA   Rees-Milton K.J., Flynn T.G.;
RT   "Studies on the inhibitor-binding site of porcine aldehyde reductase:
RT   crystal structure of the holoenzyme-inhibitor ternary complex.";
RL   Proteins 29:186-192(1997).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NADP(+) = an aldehyde + NADPH.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; U46064; AAB60266.1; -; mRNA.
DR   RefSeq; NP_999055.1; -.
DR   UniGene; Ssc.14521; -.
DR   PDB; 1AE4; X-ray; 2.40 A; A=1-325.
DR   PDB; 1CWN; X-ray; 2.00 A; A=2-324.
DR   PDB; 1HQT; X-ray; 2.20 A; A=1-325.
DR   PDB; 3CV7; X-ray; 2.41 A; A=1-325.
DR   PDB; 3H4G; X-ray; 1.85 A; A=1-325.
DR   PDBsum; 1AE4; -.
DR   PDBsum; 1CWN; -.
DR   PDBsum; 1HQT; -.
DR   PDBsum; 3CV7; -.
DR   PDBsum; 3H4G; -.
DR   GeneID; 396924; -.
DR   KEGG; ssc:396924; -.
DR   HOVERGEN; P50578; -.
DR   BRENDA; 1.1.1.2; 249.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; NADP; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    325       Alcohol dehydrogenase [NADP+].
FT                                /FTId=PRO_0000124619.
FT   NP_BIND      11     20       NADP (Potential).
FT   NP_BIND     211    273       NADP.
FT   ACT_SITE     50     50       Proton donor.
FT   BINDING     113    113       Substrate.
FT   SITE         80     80       Lowers pKa of active site Tyr (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   VARIANT     165    165       S -> N.
FT   STRAND        5      7
FT   STRAND       13     17
FT   TURN         26     28
FT   HELIX        29     38
FT   STRAND       43     45
FT   HELIX        48     50
FT   HELIX        53     60
FT   TURN         61     63
FT   STRAND       64     70
FT   HELIX        72     74
FT   STRAND       76     81
FT   HELIX        83     85
FT   HELIX        88    102
FT   STRAND      107    113
FT   TURN        129    131
FT   HELIX       140    152
FT   STRAND      155    157
FT   STRAND      159    163
FT   HELIX       166    173
FT   STRAND      182    186
FT   HELIX       194    203
FT   STRAND      206    211
FT   HELIX       232    240
FT   HELIX       245    255
FT   TURN        267    269
FT   HELIX       270    274
FT   HELIX       283    290
SQ   SEQUENCE   325 AA;  36539 MW;  146F2D1AE8B0A17F CRC64;
     MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALTVG YRHIDCAAIY GNELEIGEAL
     TETVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER
     GDNPFPKNAD GTIRYDATHY KDTWKALEAL VAKGLVRALG LSNFSSRQID DVLSVASVRP
     AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPNEPVLLE EPVVQALAEK
     YNRSPAQILL RWQVQRKVIC IPKSVTPSRI PQNIQVFDFT FSPEEMKQLD ALNKNLRFIV
     PMLTVDGKRV PRDAGHPLYP FNDPY
//