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Protein

Alcohol dehydrogenase [NADP(+)] A

Gene

akr1a1a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).By similarity

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton donorBy similarity
Sitei79 – 791Lowers pKa of active site TyrBy similarity
Binding sitei112 – 1121SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 27263NADPBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase [NADP(+)] A (EC:1.1.1.2)
Alternative name(s):
Aldehyde reductase-A
Aldo-keto reductase family 1 member A1-A
Gene namesi
Name:akr1a1a
ORF Names:si:ch211-113n10.1, zgc:100940
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 5

Organism-specific databases

ZFINiZDB-GENE-040808-44. akr1a1a.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Alcohol dehydrogenase [NADP(+)] APRO_0000384152Add
BLAST

Proteomic databases

PaxDbiQ6AZW2.
PRIDEiQ6AZW2.

Expressioni

Gene expression databases

BgeeiQ6AZW2.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000051081.

Structurei

3D structure databases

ProteinModelPortaliQ6AZW2.
SMRiQ6AZW2. Positions 3-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
InParanoidiQ6AZW2.
KOiK00002.
OMAiGDRPWAS.
OrthoDBiEOG70KGQF.
PhylomeDBiQ6AZW2.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AZW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATITLSTG QRMPTVGLGT WKSAPGQVKQ AVLAALDCGY RHIDCAAAYS
60 70 80 90 100
NEREVGEALT ERLGPGKSLR RDDIFVTSKL WNTKHHPDDV EEACRRSLSD
110 120 130 140 150
LRLSYLDLYL IHWPMAFGRG DELIPRHPDG TIQYDDTHYR DTWAAMEKLV
160 170 180 190 200
DQGLAKAIGL SNFNAKQIDD ILSIAKHKPV VNQVECHPYL VQAELVSHCW
210 220 230 240 250
SRNLTVTAYS PLGSPDRPWV TPGEALLLDD PRVVGIAKSY NKTPAQVIIR
260 270 280 290 300
WHIQRGVVCI PKSVTPSRIK QNIEVFDFKL SDEDMRLIES FNRNERFIIP
310 320
TVIKDGQKIW RDAKHPHFPF IEPY
Length:324
Mass (Da):36,762
Last modified:September 22, 2009 - v2
Checksum:i74BAFFE5775EE624
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961V → A in AAH77140 (Ref. 2) Curated
Sequence conflicti309 – 3091I → V in AAH77140 (Ref. 2) Curated
Sequence conflicti314 – 3141K → N in AAH77140 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR318632, CR753867 Genomic DNA. Translation: CAM13142.1.
CR753867, CR318632 Genomic DNA. Translation: CAN88791.1.
BC077140 mRNA. Translation: AAH77140.1.
RefSeqiNP_001003783.1. NM_001003783.2.
UniGeneiDr.91252.

Genome annotation databases

EnsembliENSDART00000051082; ENSDARP00000051081; ENSDARG00000035257.
ENSDART00000163905; ENSDARP00000135248; ENSDARG00000035257.
GeneIDi445326.
KEGGidre:445326.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR318632, CR753867 Genomic DNA. Translation: CAM13142.1.
CR753867, CR318632 Genomic DNA. Translation: CAN88791.1.
BC077140 mRNA. Translation: AAH77140.1.
RefSeqiNP_001003783.1. NM_001003783.2.
UniGeneiDr.91252.

3D structure databases

ProteinModelPortaliQ6AZW2.
SMRiQ6AZW2. Positions 3-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000051081.

Proteomic databases

PaxDbiQ6AZW2.
PRIDEiQ6AZW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000051082; ENSDARP00000051081; ENSDARG00000035257.
ENSDART00000163905; ENSDARP00000135248; ENSDARG00000035257.
GeneIDi445326.
KEGGidre:445326.

Organism-specific databases

CTDi445326.
ZFINiZDB-GENE-040808-44. akr1a1a.

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
InParanoidiQ6AZW2.
KOiK00002.
OMAiGDRPWAS.
OrthoDBiEOG70KGQF.
PhylomeDBiQ6AZW2.
TreeFamiTF106492.

Miscellaneous databases

PROiQ6AZW2.

Gene expression databases

BgeeiQ6AZW2.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiA1A1A_DANRE
AccessioniPrimary (citable) accession number: Q6AZW2
Secondary accession number(s): A2CE54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.