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Q8S528 (AL2B7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 2 member B7, mitochondrial
Short name=ALDH2b
EC=1.2.1.3
Gene names
Name:ALDH2B7
Synonyms:ALDH3
Ordered Locus Names:At1g23800
ORF Names:F5O8.33, F5O8.35
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Possesses activity on acetaldehyde and glycolaldehyde in vitro. Ref.1

Catalytic activity

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix Potential.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAC98035.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAL99612.1 differs from that shown. Reason: Frameshift at positions 303 and 309.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Potential
Chain22 – 534513Aldehyde dehydrogenase family 2 member B7, mitochondrial
PRO_0000256057

Regions

Nucleotide binding278 – 2836NAD By similarity

Sites

Active site3011Proton acceptor By similarity
Active site3351Nucleophile By similarity
Site2021Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8S528 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: C709B0E539E52C31

FASTA53458,153
        10         20         30         40         50         60 
MASRRVSSLL SRSFMSSSRS IFSLRGMNRG AQRYSNLAAA VENTITPPVK VEHTQLLIGG 

        70         80         90        100        110        120 
RFVDAVSGKT FPTLDPRNGE VIAQVSEGDA EDVNRAVAAA RKAFDEGPWP KMTAYERSKI 

       130        140        150        160        170        180 
LFRFADLIEK HNDEIAALET WDNGKPYEQS AQIEVPMLAR VFRYYAGWAD KIHGMTMPGD 

       190        200        210        220        230        240 
GPHHVQTLHE PIGVAGQIIP WNFPLLMLSW KLGPALACGN TVVLKTAEQT PLSALLVGKL 

       250        260        270        280        290        300 
LHEAGLPDGV VNIVSGFGAT AGAAIASHMD VDKVAFTGST DVGKIILELA SKSNLKAVTL 

       310        320        330        340        350        360 
ELGGKSPFIV CEDADVDQAV ELAHFALFFN QGQCCCAGSR TFVHERVYDE FVEKAKARAL 

       370        380        390        400        410        420 
KRNVGDPFKS GIEQGPQVDS EQFNKILKYI KHGVEAGATL QAGGDRLGSK GYYIQPTVFS 

       430        440        450        460        470        480 
DVKDDMLIAT DEIFGPVQTI LKFKDLDEVI ARANNSRYGL AAGVFTQNLD TAHRLMRALR 

       490        500        510        520        530 
VGTVWINCFD VLDASIPFGG YKMSGIGREK GIYSLNNYLQ VKAVVTSLKN PAWL

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF348416 mRNA. Translation: AAL99612.1. Frameshift.
AC005990 Genomic DNA. Translation: AAC98035.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30433.1.
AY035139 mRNA. Translation: AAK59643.1.
AY113912 mRNA. Translation: AAM44960.1.
IPIIPI00533796.
PIRC86372.
RefSeqNP_564204.1. NM_102228.3.
UniGeneAt.22317.

3D structure databases

ProteinModelPortalQ8S528.
SMRQ8S528. Positions 55-518.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G23800.1-P.

Proteomic databases

PaxDbQ8S528.
PRIDEQ8S528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G23800.1; AT1G23800.1; AT1G23800.
GeneID838991.
KEGGath:AT1G23800.

Organism-specific databases

GeneFarm4318.
TAIRAt1g23800.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
InParanoidQ8S528.
KOK00128.
OMAGTDTGKK.
PhylomeDBQ8S528.
ProtClustDBPLN02466.

Gene expression databases

ArrayExpressQ8S528.
GenevestigatorQ8S528.

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.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL2B7_ARATH
AccessionPrimary (citable) accession number: Q8S528
Secondary accession number(s): Q94C67, Q9ZUB6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 29, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents