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Protein

Aldehyde dehydrogenase family 2 member B4, mitochondrial

Gene

ALDH2B4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses activity on acetaldehyde and glycolaldehyde in vitro.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei206 – 2061Transition state stabilizerBy similarity
Active sitei305 – 3051Proton acceptorPROSITE-ProRule annotation
Active sitei339 – 3391NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi282 – 2876NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: GO_Central
  2. ATP binding Source: TAIR

GO - Biological processi

  1. response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciARA:AT3G48000-MONOMER.
ReactomeiREACT_243795. Ethanol oxidation.
REACT_257757. Metabolism of serotonin.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 2 member B4, mitochondrial (EC:1.2.1.3)
Short name:
ALDH2a
Gene namesi
Name:ALDH2B4
Synonyms:ALDH2
Ordered Locus Names:At3g48000
ORF Names:T17F15.130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G48000.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121MitochondrionSequence AnalysisAdd
BLAST
Chaini22 – 538517Aldehyde dehydrogenase family 2 member B4, mitochondrialPRO_0000256056Add
BLAST

Proteomic databases

PaxDbiQ9SU63.
PRIDEiQ9SU63.

Expressioni

Gene expression databases

GenevestigatoriQ9SU63.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi9274. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9SU63.
SMRiQ9SU63. Positions 54-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiQ9SU63.
KOiK00128.
OMAiTIWIALE.
PhylomeDBiQ9SU63.

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.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SU63-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAARRVSSLL SRSFSASSPL LFRSQGRNCY NGGILRRFGT SSAAAEEIIN
60 70 80 90 100
PSVQVSHTQL LINGNFVDSA SGKTFPTLDP RTGEVIAHVA EGDAEDINRA
110 120 130 140 150
VKAARTAFDE GPWPKMSAYE RSRVLLRFAD LVEKHSEELA SLETWDNGKP
160 170 180 190 200
YQQSLTAEIP MFARLFRYYA GWADKIHGLT IPADGNYQVH TLHEPIGVAG
210 220 230 240 250
QIIPWNFPLL MFAWKVGPAL ACGNTIVLKT AEQTPLTAFY AGKLFLEAGL
260 270 280 290 300
PPGVLNIVSG FGATAGAALA SHMDVDKLAF TGSTDTGKVI LGLAANSNLK
310 320 330 340 350
PVTLELGGKS PFIVFEDADI DKAVELAHFA LFFNQGQCCC AGSRTFVHEK
360 370 380 390 400
VYDEFVEKSK ARALKRVVGD PFRKGIEQGP QIDLKQFEKV MKYIKSGIES
410 420 430 440 450
NATLECGGDQ IGDKGYFIQP TVFSNVKDDM LIAQDEIFGP VQSILKFSDV
460 470 480 490 500
DEVIKRANET KYGLAAGVFT KNLDTANRVS RALKAGTVWV NCFDVFDAAI
510 520 530
PFGGYKMSGN GREKGIYSLN NYLQIKAVVT ALNKPAWI
Length:538
Mass (Da):58,589
Last modified:May 1, 2000 - v1
Checksum:iB7C054157659391C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251L → C in CAA81249. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030820 mRNA. Translation: BAA96792.1.
AF349447 mRNA. Translation: AAM27003.1.
AL049658 Genomic DNA. Translation: CAB41139.1.
CP002686 Genomic DNA. Translation: AEE78355.1.
AF327426 mRNA. Translation: AAG42016.1.
AF349522 mRNA. Translation: AAK15569.1.
AF372911 mRNA. Translation: AAK49627.1.
AY090443 mRNA. Translation: AAL91287.1.
BT000752 mRNA. Translation: AAN31892.1.
BT006371 mRNA. Translation: AAP21179.1.
Z26417 mRNA. Translation: CAA81249.1.
PIRiT06683.
RefSeqiNP_190383.1. NM_114669.3.
UniGeneiAt.22890.

Genome annotation databases

EnsemblPlantsiAT3G48000.1; AT3G48000.1; AT3G48000.
GeneIDi823955.
KEGGiath:AT3G48000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030820 mRNA. Translation: BAA96792.1.
AF349447 mRNA. Translation: AAM27003.1.
AL049658 Genomic DNA. Translation: CAB41139.1.
CP002686 Genomic DNA. Translation: AEE78355.1.
AF327426 mRNA. Translation: AAG42016.1.
AF349522 mRNA. Translation: AAK15569.1.
AF372911 mRNA. Translation: AAK49627.1.
AY090443 mRNA. Translation: AAL91287.1.
BT000752 mRNA. Translation: AAN31892.1.
BT006371 mRNA. Translation: AAP21179.1.
Z26417 mRNA. Translation: CAA81249.1.
PIRiT06683.
RefSeqiNP_190383.1. NM_114669.3.
UniGeneiAt.22890.

3D structure databases

ProteinModelPortaliQ9SU63.
SMRiQ9SU63. Positions 54-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9274. 2 interactions.

Proteomic databases

PaxDbiQ9SU63.
PRIDEiQ9SU63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G48000.1; AT3G48000.1; AT3G48000.
GeneIDi823955.
KEGGiath:AT3G48000.

Organism-specific databases

GeneFarmi4339.
TAIRiAT3G48000.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiQ9SU63.
KOiK00128.
OMAiTIWIALE.
PhylomeDBiQ9SU63.

Enzyme and pathway databases

BioCyciARA:AT3G48000-MONOMER.
ReactomeiREACT_243795. Ethanol oxidation.
REACT_257757. Metabolism of serotonin.

Gene expression databases

GenevestigatoriQ9SU63.

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.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
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

« Hide 'large scale' publications
  1. "Molecular and cellular characterizations of a cDNA clone encoding a novel isozyme of aldehyde dehydrogenase from rice."
    Li Y., Nakazono M., Tsutsumi N., Hirai A.
    Gene 249:67-74(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of the aldehyde dehydrogenase gene families of Zea mays and Arabidopsis."
    Skibbe D.S., Liu F., Wen T.-J., Yandeau M.D., Cui X., Cao J., Simmons C.R., Schnable P.S.
    Plant Mol. Biol. 48:751-764(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Philipps G., Gigot C.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-125.

Entry informationi

Entry nameiAL2B4_ARATH
AccessioniPrimary (citable) accession number: Q9SU63
Secondary accession number(s): Q42090
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.