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Q802W2

- A9A1B_DANRE

UniProt

Q802W2 - A9A1B_DANRE

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Protein
Aldehyde dehydrogenase family 9 member A1-B
Gene
aldh9a1b, aldh9a1, si:ch211-284b7.5
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei278 – 2781 Reviewed prediction
Active sitei312 – 3121 Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi256 – 2616NAD By similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 9 member A1-B (EC:1.2.1.3)
Gene namesi
Name:aldh9a1b
Synonyms:aldh9a1
ORF Names:si:ch211-284b7.5
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Chromosome 2

Organism-specific databases

ZFINiZDB-GENE-040120-5. aldh9a1b.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Aldehyde dehydrogenase family 9 member A1-B
PRO_0000300625Add
BLAST

Proteomic databases

PRIDEiQ802W2.

Expressioni

Gene expression databases

BgeeiQ802W2.

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ802W2.
SMRiQ802W2. Positions 24-518.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00720000108597.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ802W2.
KOiK00149.
OMAiIREMATP.
OrthoDBiEOG7327P4.
PhylomeDBiQ802W2.
TreeFamiTF314257.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q802W2-1 [UniParc]FASTAAdd to Basket

« Hide

MALMRCLLPP GFYRTLYHPW TRCASSGTLQ IKDPLNFWCG ARVDLKDVKT    50
KSEPVFEPAT GRVLCRLQTC GSAEVDAAVR NASAAFKVWR KLSGMERARV 100
MLEAARLIEK RREEIAEMEV INNGKSITEA RLDVDSARLS IEYFAGQATT 150
LSGQHVQLPG GSFAYTRREP FGVCVGIGAW NYPFQIAAWK SAPAIACGNS 200
MVFKPSPLTP VTAVLLAEIY RQAGAPEGLF NVVQGGQETG SLLCLHPSVE 250
KVSFTGSVPT GKKIMEMASR GVKAVTLELG GKSPLIIFED TDLENAVRGA 300
LMANFLSQGQ VCSNGTRVFV QSSIVPQFLK EVVRRTKAIS IGDPLLDETR 350
MGALVSKAHL DKVLRYVEQA KNEGAQVLCG GEPFSPADPK LKDGYYMTPC 400
VLDSCTDDMT CVKEEIFGPV MSVLTFDTED EVLRRANDSD LGLAAGVFTK 450
DVKRAHRVIE NLQAGSCFIN NYNITPVEVP FGGFKASGIG RENGQVTIEF 500
YSQLKTVVVE MGDVDSLF 518
Length:518
Mass (Da):56,438
Last modified:October 23, 2007 - v2
Checksum:i105AB1667E4199FF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 203HPW → NPG in AAH47176. 1 Publication
Sequence conflicti84 – 841A → V in AAH47176. 1 Publication
Sequence conflicti87 – 871K → T in AAH47176. 1 Publication
Sequence conflicti102 – 1021L → M in AAH47176. 1 Publication
Sequence conflicti140 – 1401S → C in AAH47176. 1 Publication
Sequence conflicti167 – 1671R → H in AAH47176. 1 Publication
Sequence conflicti227 – 2271E → D in AAH47176. 1 Publication
Sequence conflicti342 – 3421G → R in AAH47176. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954171 Genomic DNA. Translation: CAM14219.1.
BC047176 mRNA. Translation: AAH47176.1.
RefSeqiNP_958916.1. NM_201508.1.
XP_005163288.1. XM_005163231.1.
UniGeneiDr.23802.

Genome annotation databases

EnsembliENSDART00000053868; ENSDARP00000053867; ENSDARG00000037061.
GeneIDi399481.
KEGGidre:399481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954171 Genomic DNA. Translation: CAM14219.1 .
BC047176 mRNA. Translation: AAH47176.1 .
RefSeqi NP_958916.1. NM_201508.1.
XP_005163288.1. XM_005163231.1.
UniGenei Dr.23802.

3D structure databases

ProteinModelPortali Q802W2.
SMRi Q802W2. Positions 24-518.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q802W2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000053868 ; ENSDARP00000053867 ; ENSDARG00000037061 .
GeneIDi 399481.
KEGGi dre:399481.

Organism-specific databases

CTDi 399481.
ZFINi ZDB-GENE-040120-5. aldh9a1b.

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00720000108597.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
InParanoidi Q802W2.
KOi K00149.
OMAi IREMATP.
OrthoDBi EOG7327P4.
PhylomeDBi Q802W2.
TreeFami TF314257.

Miscellaneous databases

NextBioi 20816591.

Gene expression databases

Bgeei Q802W2.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. 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 ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.

Entry informationi

Entry nameiA9A1B_DANRE
AccessioniPrimary (citable) accession number: Q802W2
Secondary accession number(s): A2AWD6
Entry historyi
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 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

External Data

Dasty 3

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