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Protein

Aldehyde dehydrogenase family 7 member B4

Gene

ALDH7B4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 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
Sitei165 – 1651Transition state stabilizerBy similarity
Active sitei266 – 2661Proton acceptorPROSITE-ProRule annotation
Active sitei300 – 3001NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi244 – 2496NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular aldehyde metabolic process Source: UniProtKB
  • response to abscisic acid Source: TAIR
  • response to desiccation Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciARA:AT1G54100-MONOMER.
ARA:GQT-790-MONOMER.
ReactomeiREACT_310104. Lysine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 7 member B4 (EC:1.2.1.3)
Alternative name(s):
Antiquitin-1
Turgor-responsive ALDH
Gene namesi
Name:ALDH7B4
Ordered Locus Names:At1g54100
ORF Names:F15I1.19
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G54100.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 508507Aldehyde dehydrogenase family 7 member B4PRO_0000056495Add
BLAST

Proteomic databases

PaxDbiQ9SYG7.
PRIDEiQ9SYG7.

Expressioni

Inductioni

By abscisic acid (ABA) and dehydration in roots and plantlets, and by salt stress in plantlets.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi27074. 2 interactions.
STRINGi3702.AT1G54100.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SYG7.
SMRiQ9SYG7. Positions 7-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271511.
InParanoidiQ9SYG7.
KOiK14085.
OMAiNAIIVFE.
PhylomeDBiQ9SYG7.

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.
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.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9SYG7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSANNEYEF LSEIGLTSHN LGSYVAGKWQ ANGPLVSTLN PANNQPIAQV
60 70 80 90 100
VEASLEDYEQ GLKACEEAAK IWMQVTAPKR GDIVRQIGDA LRSKLDYLGR
110 120 130 140 150
LLSLEMGKIL AEGIGEVQEV IDMCDFAVGL SRQLNGSVIP SERPNHMMLE
160 170 180 190 200
MWNPLGIVGV ITAFNFPCAV LGWNACIALV CGNCVVWKGA PTTPLITIAM
210 220 230 240 250
TKLVAEVLEK NNLPGAIFTA MCGGAEIGEA IAKDTRIPLV SFTGSSRVGS
260 270 280 290 300
MVQQTVNARS GKTLLELSGN NAIIVMDDAD IQLAARSVLF AAVGTAGQRC
310 320 330 340 350
TTCRRLLLHE SVYDKVLEQL LTSYKQVKIG NPLEKGTLLG PLHTPESKKN
360 370 380 390 400
FEKGIEVIKS QGGKILTGGK AVEGEGNFVE PTIIEISADA AVVKEELFAP
410 420 430 440 450
VLYVLKFKSF GEAVAINNSV PQGLSSSIFT RNPENIFRWI GPLGSDCGIV
460 470 480 490 500
NVNIPTNGAE IGGAFGGEKA TGGGREAGSD SWKQYMRRST CTINYGNELP

LAQGINFG
Length:508
Mass (Da):54,208
Last modified:November 15, 2002 - v3
Checksum:i7690BB8D906B263A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ584645 mRNA. Translation: CAE48164.1.
AC006577 Genomic DNA. Translation: AAD25783.1.
CP002684 Genomic DNA. Translation: AEE33048.1.
CP002684 Genomic DNA. Translation: AEE33049.1.
AY048242 mRNA. Translation: AAK82504.1.
AF378873 mRNA. Translation: AAK55676.1.
AY091032 mRNA. Translation: AAM13853.1.
AY102145 mRNA. Translation: AAM26712.1.
AY117345 mRNA. Translation: AAM51420.1.
AK230363 mRNA. Translation: BAF02162.1.
PIRiH96581.
RefSeqiNP_175812.1. NM_104287.4.
NP_849807.1. NM_179476.2.
UniGeneiAt.20851.

Genome annotation databases

EnsemblPlantsiAT1G54100.1; AT1G54100.1; AT1G54100.
AT1G54100.2; AT1G54100.2; AT1G54100.
GeneIDi841849.
KEGGiath:AT1G54100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ584645 mRNA. Translation: CAE48164.1.
AC006577 Genomic DNA. Translation: AAD25783.1.
CP002684 Genomic DNA. Translation: AEE33048.1.
CP002684 Genomic DNA. Translation: AEE33049.1.
AY048242 mRNA. Translation: AAK82504.1.
AF378873 mRNA. Translation: AAK55676.1.
AY091032 mRNA. Translation: AAM13853.1.
AY102145 mRNA. Translation: AAM26712.1.
AY117345 mRNA. Translation: AAM51420.1.
AK230363 mRNA. Translation: BAF02162.1.
PIRiH96581.
RefSeqiNP_175812.1. NM_104287.4.
NP_849807.1. NM_179476.2.
UniGeneiAt.20851.

3D structure databases

ProteinModelPortaliQ9SYG7.
SMRiQ9SYG7. Positions 7-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27074. 2 interactions.
STRINGi3702.AT1G54100.1.

Proteomic databases

PaxDbiQ9SYG7.
PRIDEiQ9SYG7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G54100.1; AT1G54100.1; AT1G54100.
AT1G54100.2; AT1G54100.2; AT1G54100.
GeneIDi841849.
KEGGiath:AT1G54100.

Organism-specific databases

TAIRiAT1G54100.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271511.
InParanoidiQ9SYG7.
KOiK14085.
OMAiNAIIVFE.
PhylomeDBiQ9SYG7.

Enzyme and pathway databases

BioCyciARA:AT1G54100-MONOMER.
ARA:GQT-790-MONOMER.
ReactomeiREACT_310104. Lysine catabolism.

Miscellaneous databases

PROiQ9SYG7.

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.
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.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Detailed expression analysis of selected genes of the aldehyde dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana."
    Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.
    Plant Mol. Biol. 57:315-332(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  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.
    , 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.
    , 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.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: NOMENCLATURE.

Entry informationi

Entry nameiAL7B4_ARATH
AccessioniPrimary (citable) accession number: Q9SYG7
Secondary accession number(s): Q546B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: June 24, 2015
This is version 112 of the entry and version 3 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.