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Protein

Aldehyde dehydrogenase family 9 member A1-B

Gene

aldh9a1b

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: 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 – 2781Sequence Analysis
Active sitei312 – 3121Sequence Analysis

Regions

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

GO - Molecular functioni

  1. 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: GO_Central
  2. aminobutyraldehyde dehydrogenase activity Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_260713. Carnitine synthesis.

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-BPRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ802W2.
KOiK00149.
OMAiEPIANIH.
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

        10         20         30         40         50
MALMRCLLPP GFYRTLYHPW TRCASSGTLQ IKDPLNFWCG ARVDLKDVKT
60 70 80 90 100
KSEPVFEPAT GRVLCRLQTC GSAEVDAAVR NASAAFKVWR KLSGMERARV
110 120 130 140 150
MLEAARLIEK RREEIAEMEV INNGKSITEA RLDVDSARLS IEYFAGQATT
160 170 180 190 200
LSGQHVQLPG GSFAYTRREP FGVCVGIGAW NYPFQIAAWK SAPAIACGNS
210 220 230 240 250
MVFKPSPLTP VTAVLLAEIY RQAGAPEGLF NVVQGGQETG SLLCLHPSVE
260 270 280 290 300
KVSFTGSVPT GKKIMEMASR GVKAVTLELG GKSPLIIFED TDLENAVRGA
310 320 330 340 350
LMANFLSQGQ VCSNGTRVFV QSSIVPQFLK EVVRRTKAIS IGDPLLDETR
360 370 380 390 400
MGALVSKAHL DKVLRYVEQA KNEGAQVLCG GEPFSPADPK LKDGYYMTPC
410 420 430 440 450
VLDSCTDDMT CVKEEIFGPV MSVLTFDTED EVLRRANDSD LGLAAGVFTK
460 470 480 490 500
DVKRAHRVIE NLQAGSCFIN NYNITPVEVP FGGFKASGIG RENGQVTIEF
510
YSQLKTVVVE MGDVDSLF
Length:518
Mass (Da):56,438
Last modified:October 23, 2007 - v2
Checksum:i105AB1667E4199FF
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954171 Genomic DNA. Translation: CAM14219.1.
BC047176 mRNA. Translation: AAH47176.1.
RefSeqiNP_958916.1. NM_201508.1.
XP_005163288.1. XM_005163231.2.
UniGeneiDr.23802.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954171 Genomic DNA. Translation: CAM14219.1.
BC047176 mRNA. Translation: AAH47176.1.
RefSeqiNP_958916.1. NM_201508.1.
XP_005163288.1. XM_005163231.2.
UniGeneiDr.23802.

3D structure databases

ProteinModelPortaliQ802W2.
SMRiQ802W2. Positions 24-518.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ802W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi399481.
ZFINiZDB-GENE-040120-5. aldh9a1b.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ802W2.
KOiK00149.
OMAiEPIANIH.
OrthoDBiEOG7327P4.
PhylomeDBiQ802W2.
TreeFamiTF314257.

Enzyme and pathway databases

ReactomeiREACT_260713. Carnitine synthesis.

Miscellaneous databases

NextBioi20816591.

Gene expression databases

BgeeiQ802W2.

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]
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 (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: February 4, 2015
This is version 82 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

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 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.