[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=7484379 [NCBI, ExPASy, EBI, Israel, Japan] Flynn T.G., Green N.C., Bhatia M.B., El-Kabbani O.; "Structure and mechanism of aldehyde reductase."; Adv. Exp. Med. Biol. 372:193-201(1995).
[2]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1038/nsb0895-687; PubMed=7552731 [NCBI, ExPASy, EBI, Israel, Japan] el-Kabbani O., Judge K., Ginell S.L., Myles D.A., DeLucas L.J., Flynn T.G.; "Structure of porcine aldehyde reductase holoenzyme."; Nat. Struct. Biol. 2:687-692(1995).
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1002/(SICI)1097-0134(199710)29:2<186::AID-PROT6>3.0.CO;2-B; PubMed=9329083 [NCBI, ExPASy, EBI, Israel, Japan] El-Kabbani O., Carper D.A., McGowan M.H., Devedjiev Y., Rees-Milton K.J., Flynn T.G.; "Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex."; Proteins 29:186-192(1997).

Comments

CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the aldo/keto reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U46064; AAB60266.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999055.1; -.

UniGene

Ssc.14521

3D structure databases

PDB

1AE4; X-ray; 2.40 A; A=1-325.	[ExPASy / RCSB / EBI]
1CWN; X-ray; 2.00 A; A=1-325.	[ExPASy / RCSB / EBI]
1HQT; X-ray; 2.20 A; A=1-325.	[ExPASy / RCSB / EBI]
2AO0; X-ray; 1.85 A; A=1-325.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AE4; -.
1CWN; -.
1HQT; -.
2AO0; -.

ModBase

P50578.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.100; Aldo/ket_red; 1.

PANTHER

PTHR11732; Aldo/ket_red; 1.

Pfam

PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00069; ALDKETRDTASE.

ProDom

PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.

BLOCKS

P50578.

Genome annotation databases

GeneID

396924; -.

KEGG

ssc:396924; -.

Phylogenomic databases

HOVERGEN

P50578; -.

Other

P50578; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 325`	`324`	`Alcohol dehydrogenase [NADP+].`	`PRO_0000124619`
`NP_BIND`	`11 20`	`10`	`NADP (Potential).`
`NP_BIND`	`211 273`	`63`	`NADP.`
`ACT_SITE`	`50 50`		`Proton donor.`
`BINDING`	`113 113`		`Substrate.`
`SITE`	`80 80`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`VARIANT`	`165 165`	`1`	`S -> N.`
`STRAND`	`5 7`	`3`
`TURN`	`9 10`	`2`
`STRAND`	`13 17`	`5`
`TURN`	`22 23`	`2`
`TURN`	`26 28`	`3`
`HELIX`	`29 38`	`10`
`TURN`	`39 40`	`2`
`STRAND`	`43 45`	`3`
`HELIX`	`48 50`	`3`
`HELIX`	`53 63`	`11`
`TURN`	`66 67`	`2`
`STRAND`	`68 70`	`3`
`HELIX`	`72 74`	`3`
`STRAND`	`76 81`	`6`
`HELIX`	`83 85`	`3`
`HELIX`	`88 102`	`15`
`TURN`	`103 103`	`1`
`STRAND`	`107 113`	`7`
`STRAND`	`115 118`	`4`
`STRAND`	`120 122`	`3`
`TURN`	`129 130`	`2`
`HELIX`	`140 152`	`13`
`TURN`	`153 154`	`2`
`STRAND`	`155 157`	`3`
`STRAND`	`159 163`	`5`
`HELIX`	`166 173`	`8`
`TURN`	`174 175`	`2`
`STRAND`	`182 186`	`5`
`TURN`	`189 190`	`2`
`HELIX`	`194 203`	`10`
`TURN`	`204 204`	`1`
`STRAND`	`206 211`	`6`
`TURN`	`212 213`	`2`
`TURN`	`216 217`	`2`
`HELIX`	`228 230`	`3`
`HELIX`	`232 241`	`10`
`TURN`	`242 242`	`1`
`HELIX`	`245 255`	`11`
`TURN`	`256 257`	`2`
`HELIX`	`267 274`	`8`
`HELIX`	`283 290`	`8`
`TURN`	`291 292`	`2`
`STRAND`	`311 313`	`3`
`TURN`	`314 315`	`2`
`TURN`	`317 318`	`2`
`HELIX`	`320 322`	`3`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 36539 Da [This is the MW of the unprocessed precursor]

CRC64: 146F2D1AE8B0A17F [This is a checksum on the sequence]

        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

P50578 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools