Reviewed, UniProtKB/Swiss-Prot Q6IMN8 (ALRA_DICDI)

Names and origin

Protein names

Recommended name:
    Aldose reductase A
      Short name=ARA
    EC=1.1.1.21
Alternative name(s):
    Aldehyde reductase A

Gene names

Name:	alrA
ORF Names:	DDB_G0293850

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies By similarity. Probably affects several metabolic pathways in addition to converting glucose to sorbitol. Affects group size.
Catalytic activity	Alditol + NAD(P)+ = aldose + NAD(P)H.
Subcellular location	Cytoplasm. Ref.2
Developmental stage	Present in vegetative cells; the levels decrease slightly upon starvation and remain constant until 10 hours of development and then decline. At 25 hours there is very little detectable protein. Ref.2
Disruption phenotype	Cells show a decrease in the ability to reduce both glyceraldehyde and glucose in an NADPH-coupled reaction and a decrease in glucose levels. They grow normally but form long unbroken streams and huge groups. They show normal adhesion but a reduced motility. They secrete low levels of countin and CF50, two component of the counting factor (CF) but are responsive to CF and partially responsive to recombinant countin and CF50. Ref.2
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde reductase 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
	Chain	1 – 297	297	Aldose reductase A		PRO_0000327645
Regions
	Nucleotide binding	10 – 19	10	NADP Potential
	Nucleotide binding	207 – 259	53	NADP By similarity
Sites
	Active site	49	1	Proton donor By similarity
	Binding site	112	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6IMN8-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4716A0B09F61D861	FASTA	297	33,649
	10 20 30 40 50 60 MEPSFKLSSG HKIPLVGFGT WKAETTLVGK AVEVALDAGY RHIDCAAVYL NEKEVGEAFT 70 80 90 100 110 120 KKFTTEATVK REDVFITSKL WNTFHKKEHV RPALERTLSD LGLQYLDLYL VHWPVAFEYT 130 140 150 160 170 180 SNDIQTSGST QEFVSIRETW EEMEKLVDAG LVKSIGLSNF NVQGLMEVLS YARIKPAANQ 190 200 210 220 230 240 VELHPFLSQP ELKKFCDKHN IHLTAYSPLG NGAFVDNEEV GAIAKKYNKT IPNVLCKWAI 250 260 270 280 290 QKNFSVIPKS STPSRVAENF DLFNFEIEEA DMLFLDKMDK NLRTCDPAKF WGVPLFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Disruption of aldehyde reductase increases group size in dictyostelium." Ehrenman K., Yang G., Hong W.-P., Gao T., Jang W., Brock D.A., Hatton R.D., Shoemaker J.D., Gomer R.H. J. Biol. Chem. 279:837-847(2004) [PubMed: 14551196] [Abstract] Cited for: IDENTIFICATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000223 Genomic DNA. Translation: EAL60496.1. BK001032 mRNA. Translation: DAA01127.1.
RefSeq	XP_628918.1.
3D structure databases
HSSP	HSSP built from PDB template 1PWL based on UniProtKB P15121.
ModBase	Search...
Genome annotation databases
GeneID	3385573.
KEGG	ddi:DDB_0215363.
Organism-specific databases
dictyBase	DDB_G0293850. alrA.
Phylogenomic databases
OMA	Q6IMN8. ETWEEME.
Enzyme and pathway databases
BRENDA	1.1.1.21. 424.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALRA_DICDI

Accession

Primary (citable) accession number: Q6IMN8
Secondary accession number(s): Q54B70

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)