Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51650 (SSDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate-semialdehyde dehydrogenase, mitochondrial

EC=1.2.1.24
Alternative name(s):
Aldehyde dehydrogenase family 5 member A1
NAD(+)-dependent succinic semialdehyde dehydrogenase
Gene names
Name:Aldh5a1
Synonyms:Ssadh
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) By similarity.

Catalytic activity

Succinate semialdehyde + NAD+ + H2O = succinate + NADH.

Enzyme regulation

Redox-regulated. Inhibited under oxydizing conditions By similarity.

Pathway

Amino-acid degradation; 4-aminobutanoate degradation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Brain, pancreas, heart, liver, skeletal muscle, kidney. Lower in spleen, lung, kidney and testis.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P51650-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P51650-2)

The sequence of this isoform differs from the canonical sequence as follows:
     107-134: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion Ref.2 Ref.3
Chain36 – 523488Succinate-semialdehyde dehydrogenase, mitochondrial
PRO_0000056567

Regions

Nucleotide binding216 – 2194NAD By similarity
Nucleotide binding272 – 2776NAD By similarity

Sites

Active site2941Proton acceptor By similarity
Active site3281Nucleophile By similarity
Binding site2011NAD By similarity
Binding site2011Substrate By similarity
Binding site3221Substrate By similarity
Binding site4861Substrate By similarity
Site1931Transition state stabilizer By similarity

Amino acid modifications

Modified residue1141N6-acetyllysine; alternate By similarity
Modified residue1141N6-succinyllysine; alternate By similarity
Modified residue1231N6-succinyllysine By similarity
Modified residue1721N6-succinyllysine By similarity
Modified residue2531N6-acetyllysine; alternate By similarity
Modified residue2531N6-succinyllysine; alternate By similarity
Modified residue3531N6-acetyllysine By similarity
Modified residue3901N6-succinyllysine By similarity
Modified residue3991N6-acetyllysine By similarity
Disulfide bond328 ↔ 330In inhibited form By similarity

Natural variations

Alternative sequence107 – 13428Missing in isoform Short.
VSP_001284

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 4CA521139C9FA98F

FASTA52356,131
        10         20         30         40         50         60 
MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD SFVGGRWLPT 

        70         80         90        100        110        120 
PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW KEISVKERSS LLRKWYDLMI 

       130        140        150        160        170        180 
QNKDELAKII TAESGKPLKE AQGEILYSAF FLEWFSEEAR RVYGDIIYTS AKDKRGLVLK 

       190        200        210        220        230        240 
QPVGVASIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPPG 

       250        260        270        280        290        300 
VYNVIPCSRT KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP 

       310        320        330        340        350        360 
FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN 

       370        380        390        400        410        420 
GFEEGTTQGP LINEKAVEKV EKHVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM 

       430        440        450        460        470        480 
LCITEETFGP VAPVIKFDKE EEAVAIANAA DVGLAGYFYS QDPAQIWRVA EQLEVGMVGV 

       490        500        510        520 
NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL 

« Hide

Isoform Short [UniParc].

Checksum: FC69A1D9215CEF5F
Show »

FASTA49552,798

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression."
Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., Gibson K.M.
J. Biol. Chem. 270:461-467(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND 503-526.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03105019 Genomic DNA. No translation available.
L34821 mRNA. Translation: AAA67058.1.
PIRI61704.
UniGeneRn.10070.

3D structure databases

ProteinModelPortalP51650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000035601.

PTM databases

PhosphoSiteP51650.

2D gel databases

World-2DPAGE0004:P51650.

Proteomic databases

PaxDbP51650.
PRIDEP51650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621422. rat. [P51650-1]

Organism-specific databases

RGD621422. Aldh5a1.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271509.
HOVERGENHBG108515.
InParanoidP51650.
PhylomeDBP51650.

Enzyme and pathway databases

SABIO-RKP51650.
UniPathwayUPA00733.

Gene expression databases

GenevestigatorP51650.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010102. Succ_semiAld_DH.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01780. SSADH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP51650.

Entry information

Entry nameSSDH_RAT
AccessionPrimary (citable) accession number: P51650
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways