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Q802W2 (A9A1B_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase family 9 member A1-B

EC=1.2.1.3
Gene names
Name:aldh9a1b
Synonyms:aldh9a1
ORF Names:si:ch211-284b7.5
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Aldehyde dehydrogenase family 9 member A1-B
PRO_0000300625

Regions

Nucleotide binding256 – 2616NAD By similarity

Sites

Active site2781 Potential
Active site3121 Potential

Experimental info

Sequence conflict18 – 203HPW → NPG in AAH47176. Ref.2
Sequence conflict841A → V in AAH47176. Ref.2
Sequence conflict871K → T in AAH47176. Ref.2
Sequence conflict1021L → M in AAH47176. Ref.2
Sequence conflict1401S → C in AAH47176. Ref.2
Sequence conflict1671R → H in AAH47176. Ref.2
Sequence conflict2271E → D in AAH47176. Ref.2
Sequence conflict3421G → R in AAH47176. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q802W2 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 105AB1667E4199FF

FASTA51856,438
        10         20         30         40         50         60 
MALMRCLLPP GFYRTLYHPW TRCASSGTLQ IKDPLNFWCG ARVDLKDVKT KSEPVFEPAT 

        70         80         90        100        110        120 
GRVLCRLQTC GSAEVDAAVR NASAAFKVWR KLSGMERARV MLEAARLIEK RREEIAEMEV 

       130        140        150        160        170        180 
INNGKSITEA RLDVDSARLS IEYFAGQATT LSGQHVQLPG GSFAYTRREP FGVCVGIGAW 

       190        200        210        220        230        240 
NYPFQIAAWK SAPAIACGNS MVFKPSPLTP VTAVLLAEIY RQAGAPEGLF NVVQGGQETG 

       250        260        270        280        290        300 
SLLCLHPSVE KVSFTGSVPT GKKIMEMASR GVKAVTLELG GKSPLIIFED TDLENAVRGA 

       310        320        330        340        350        360 
LMANFLSQGQ VCSNGTRVFV QSSIVPQFLK EVVRRTKAIS IGDPLLDETR MGALVSKAHL 

       370        380        390        400        410        420 
DKVLRYVEQA KNEGAQVLCG GEPFSPADPK LKDGYYMTPC VLDSCTDDMT CVKEEIFGPV 

       430        440        450        460        470        480 
MSVLTFDTED EVLRRANDSD LGLAAGVFTK DVKRAHRVIE NLQAGSCFIN NYNITPVEVP 

       490        500        510 
FGGFKASGIG RENGQVTIEF YSQLKTVVVE MGDVDSLF 

« Hide

References

[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. expand/collapse author list , 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 (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: AB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954171 Genomic DNA. Translation: CAM14219.1.
BC047176 mRNA. Translation: AAH47176.1.
RefSeqNP_958916.1. NM_201508.1.
XP_005163288.1. XM_005163231.1.
UniGeneDr.23802.

3D structure databases

ProteinModelPortalQ802W2.
SMRQ802W2. Positions 24-518.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ802W2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000053868; ENSDARP00000053867; ENSDARG00000037061.
GeneID399481.
KEGGdre:399481.

Organism-specific databases

CTD399481.
ZFINZDB-GENE-040120-5. aldh9a1b.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00720000108597.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidQ802W2.
KOK00149.
OMAIREMATP.
OrthoDBEOG7327P4.
PhylomeDBQ802W2.
TreeFamTF314257.

Gene expression databases

BgeeQ802W2.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816591.

Entry information

Entry nameA9A1B_DANRE
AccessionPrimary (citable) accession number: Q802W2
Secondary accession number(s): A2AWD6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 23, 2007
Last modified: June 11, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families