GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ARATH:SSDH

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Arabidopsis thaliana (Mouse-ear cress). (3702)
Gene Name(s) ALDH5F1 (synonyms: SSADH1)
Protein Name(s) Succinate-semialdehyde dehydrogenase, mitochondrial

At-SSADH1 Aldehyde dehydrogenase family 5 member F1 NAD(+)-dependent succinic semialdehyde dehydrogenase

External Links
UniProt Q9SAK4
EMBL AF117335
AC007202
CP002684
AF428367
AY056147
PIR E96825
RefSeq NP_178062.1
UniGene At.11884
ProteinModelPortal Q9SAK4
SMR Q9SAK4
STRING 3702.AT1G79440.1-P
PaxDb Q9SAK4
PRIDE Q9SAK4
EnsemblPlants AT1G79440.1
GeneID 844282
KEGG ath:AT1G79440
GeneFarm 4340
TAIR AT1G79440
eggNOG COG1012
HOGENOM HOG000271509
InParanoid Q9SAK4
KO K17761
OMA IKYICMS
PhylomeDB Q9SAK4
BioCyc ARA:AT1G79440-MONOMER
Reactome REACT_190919
UniPathway UPA00733
PRO PR:Q9SAK4
Proteomes UP000006548
Genevestigator Q9SAK4
GO GO:0009507
GO:0009570
GO:0005759
GO:0005739
GO:0005507
GO:0051287
GO:0004777
GO:0009013
GO:0009450
GO:0006540
GO:0072593
GO:0009408
GO:0009416
Gene3D 3.40.309.10
3.40.605.10
InterPro IPR016161
IPR016163
IPR016160
IPR029510
IPR016162
IPR015590
IPR010102
Pfam PF00171
SUPFAM SSF53720
TIGRFAMs TIGR01780
PROSITE PS00070
PS00687

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

UniProtKB:P76149


F

Figure 1

complete
CACAO 10494

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

UniProtKB:P51649


F

Figure 1

complete
CACAO 10495

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

UniProtKB:P51650


F

Figure 1

complete
CACAO 10496

involved_in

GO:0010492

maintenance of shoot apical meristem identity

PMID:21690177[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1902074

response to salt

PMID:20122158[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0048825

cotyledon development

PMID:21690177[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0048366

leaf development

PMID:21690177[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009943

adaxial/abaxial axis specification

PMID:21690177[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009409

response to cold

PMID:17461790[4]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009416

response to light stimulus

PMID:15642352[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

sequence alignment evidence used in manual assertion

UniProtKB:P51650

F

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

sequence alignment evidence used in manual assertion

UniProtKB:P51649

F

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000247

sequence alignment evidence used in manual assertion

UniProtKB:P76149

F

Seeded From UniProt

complete

involved_in

GO:0072593

reactive oxygen species metabolic process

PMID:15642352[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

PMID:10955999[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009570

chloroplast stroma

PMID:20061580[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:18431481[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009450

gamma-aminobutyric acid catabolic process

PMID:10517851[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009416

response to light stimulus

PMID:12740438[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:12740438[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006540

glutamate decarboxylation to succinate

PMID:15642352[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006540

glutamate decarboxylation to succinate

PMID:10517851[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

PMID:10517851[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14671022[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:11743115[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005507

copper ion binding

PMID:20018591[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:10517851[1]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

enables

GO:0009013

succinate-semialdehyde dehydrogenase [NAD(P)+] activity

PMID:21873635[13]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11329
PANTHER:PTN000192580
SGD:S000000210

F

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

PMID:21873635[13]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11329
FB:FBgn0039349
PANTHER:PTN000192580
RGD:621422
TAIR:locus:2206405
UniProtKB:P51649

F

Seeded From UniProt

complete

enables

GO:0009013

succinate-semialdehyde dehydrogenase [NAD(P)+] activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010102

F

Seeded From UniProt

complete

involved_in

GO:0009450

gamma-aminobutyric acid catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010102

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR029510

F

Seeded From UniProt

complete

enables

GO:0016620

oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016163

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010102
InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR029510

P

Seeded From UniProt

complete

enables

GO:0004777

succinate-semialdehyde dehydrogenase (NAD+) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.1.24

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0170

C

Seeded From UniProt

complete

involved_in

GO:0009450

gamma-aminobutyric acid catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00733

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 Busch, KB & Fromm, H (1999) Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides. Plant Physiol. 121 589-97 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Toyokura, K et al. (2011) Succinic semialdehyde dehydrogenase is involved in the robust patterning of Arabidopsis leaves along the adaxial-abaxial axis. Plant Cell Physiol. 52 1340-53 PubMed GONUTS page
  3. Renault, H et al. (2010) The Arabidopsis pop2-1 mutant reveals the involvement of GABA transaminase in salt stress tolerance. BMC Plant Biol. 10 20 PubMed GONUTS page
  4. Kaplan, F et al. (2007) Transcript and metabolite profiling during cold acclimation of Arabidopsis reveals an intricate relationship of cold-regulated gene expression with modifications in metabolite content. Plant J. 50 967-81 PubMed GONUTS page
  5. 5.0 5.1 5.2 Fait, A et al. (2005) GABA shunt deficiencies and accumulation of reactive oxygen intermediates: insight from Arabidopsis mutants. FEBS Lett. 579 415-20 PubMed GONUTS page
  6. Busch, K et al. (2000) Plant succinic semialdehyde dehydrogenase: dissection of nucleotide binding by surface plasmon resonance and fluorescence spectroscopy. Biochemistry 39 10110-7 PubMed GONUTS page
  7. Ferro, M et al. (2010) AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell Proteomics 9 1063-84 PubMed GONUTS page
  8. Zybailov, B et al. (2008) Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3 e1994 PubMed GONUTS page
  9. 9.0 9.1 Bouché, N et al. (2003) Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants. Proc. Natl. Acad. Sci. U.S.A. 100 6843-8 PubMed GONUTS page
  10. Heazlewood, JL et al. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16 241-56 PubMed GONUTS page
  11. Millar, AH et al. (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol. 127 1711-27 PubMed GONUTS page
  12. Tan, YF et al. (2010) Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function. Plant Physiol. 152 747-61 PubMed GONUTS page
  13. 13.0 13.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page