Reviewed, UniProtKB/Swiss-Prot P50578 (AK1A1_PIG)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase [NADP+]
    EC=1.1.1.2
Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member A1

Gene names

Name:	AKR1A1
Synonyms:	ALR, ALR1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An alcohol + NADP+ = an aldehyde + NADPH.
Subunit structure	Monomer.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 325

324

Alcohol dehydrogenase [NADP+]

PRO_0000124619

Regions

Nucleotide binding

11 – 20

10

NADP Potential

Nucleotide binding

211 – 273

63

NADP

Sites

Active site

50

1

Proton donor

Binding site

113

1

Substrate

Site

80

1

Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Natural variant

165

1

S → N

Secondary structure

1

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325

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Beta strand

13 – 17

5

Turn

26 – 28

3

Helix

29 – 38

10

Beta strand

43 – 45

3

Helix

48 – 50

3

Helix

53 – 60

8

Turn

61 – 63

3

Beta strand

64 – 70

7

Helix

72 – 74

3

Beta strand

76 – 81

6

Helix

83 – 85

3

Helix

88 – 102

15

Beta strand

107 – 113

7

Turn

129 – 131

3

Helix

140 – 152

13

Beta strand

155 – 157

3

Beta strand

159 – 163

5

Helix

166 – 173

8

Beta strand

182 – 186

5

Helix

194 – 203

10

Beta strand

206 – 211

6

Helix

232 – 240

9

Helix

245 – 255

11

Turn

267 – 269

3

Helix

270 – 274

5

Helix

283 – 290

8

Sequences

	Sequence		Length	Mass (Da)
	P50578-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 146F2D1AE8B0A17F	FASTA	325	36,539
	10 20 30 40 50 60 MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALTVG YRHIDCAAIY GNELEIGEAL 70 80 90 100 110 120 TETVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER 130 140 150 160 170 180 GDNPFPKNAD GTIRYDATHY KDTWKALEAL VAKGLVRALG LSNFSSRQID DVLSVASVRP 190 200 210 220 230 240 AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPNEPVLLE EPVVQALAEK 250 260 270 280 290 300 YNRSPAQILL RWQVQRKVIC IPKSVTPSRI PQNIQVFDFT FSPEEMKQLD ALNKNLRFIV 310 320 PMLTVDGKRV PRDAGHPLYP FNDPY

References

[1]	"Structure and mechanism of aldehyde reductase." Flynn T.G., Green N.C., Bhatia M.B., El-Kabbani O. Adv. Exp. Med. Biol. 372:193-201(1995) [PubMed: 7484379] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Structure of porcine aldehyde reductase holoenzyme." el-Kabbani O., Judge K., Ginell S.L., Myles D.A., DeLucas L.J., Flynn T.G. Nat. Struct. Biol. 2:687-692(1995) [PubMed: 7552731] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[3]	"Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex." El-Kabbani O., Carper D.A., McGowan M.H., Devedjiev Y., Rees-Milton K.J., Flynn T.G. Proteins 29:186-192(1997) [PubMed: 9329083] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U46064 mRNA. Translation: AAB60266.1.

RefSeq

NP_999055.1.

UniGene

Ssc.14521

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AE4	X-ray	2.40	A	1-325	[»]
1CWN	X-ray	2.00	A	2-324	[»]
1HQT	X-ray	2.20	A	1-325	[»]
3CV7	X-ray	2.41	A	1-325	[»]
3H4G	X-ray	1.85	A	2-324	[»]

ModBase

Search...

Genome annotation databases

GeneID

396924.

KEGG

ssc:396924.

Phylogenomic databases

HOVERGEN

P50578.

Enzyme and pathway databases

BRENDA

1.1.1.2. 249.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AK1A1_PIG

Accession

Primary (citable) accession number: P50578

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)