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Q8BWF0 (SSDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processacetate metabolic process

Inferred from mutant phenotype. Source: MGI

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

galactosylceramide metabolic process

Inferred from mutant phenotype. Source: MGI

gamma-aminobutyric acid catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glucose metabolic process

Inferred from mutant phenotype. Source: MGI

glucosylceramide metabolic process

Inferred from mutant phenotype. Source: MGI

glutamate metabolic process

Inferred from mutant phenotype. Source: MGI

glutamine metabolic process

Inferred from mutant phenotype. Source: MGI

glutathione metabolic process

Inferred from mutant phenotype. Source: MGI

glycerophospholipid metabolic process

Inferred from mutant phenotype. Source: MGI

neurotransmitter catabolic process

Inferred from mutant phenotype. Source: MGI

post-embryonic development

Inferred from mutant phenotype. Source: MGI

respiratory electron transport chain

Inferred from mutant phenotype. Source: MGI

short-chain fatty acid metabolic process

Inferred from mutant phenotype. Source: MGI

succinate metabolic process

Inferred from mutant phenotype. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: UniProtKB

   Molecular functionsuccinate-semialdehyde dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 523488Succinate-semialdehyde dehydrogenase, mitochondrial
PRO_0000007185

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 residue671Phosphotyrosine Ref.4
Modified residue1141N6-acetyllysine By similarity
Disulfide bond328 ↔ 330In inhibited form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BWF0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E0CF82E4F4FAE9D0

FASTA52355,968
        10         20         30         40         50         60 
MATCFLLRSF WAARPALPPP GRFRPEPAGT PRRSYASGPG GLHADLLRGD SFVGGRWLPA 

        70         80         90        100        110        120 
PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFNSW KGVSVKERSL LLRKWYDLMI 

       130        140        150        160        170        180 
QNKDDLAKII TAESGKPLKE AQGEILYSAL FLEWFSEEAR RIYGDIIYTS AKDKRGLVLK 

       190        200        210        220        230        240 
QPVGVAAIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPAG 

       250        260        270        280        290        300 
VYNVIPCSRN 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 EKQVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM 

       430        440        450        460        470        480 
LCITEETFGP LAPVIKFDKE EEAVAIANAA EVGLAGYFYS QDPAQIWRVA EQLEVGMVGV 

       490        500        510        520 
NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 57-87; 115-123; 129-160; 162-172; 181-201; 254-289; 291-320; 323-333; 339-347; 358-375; 401-436; 469-496 AND 507-516, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[4]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK052703 mRNA. Translation: BAC35105.1.
AK144030 mRNA. Translation: BAE25663.1.
AL589699 Genomic DNA. Translation: CAI26086.1.
IPIIPI00273164.
RefSeqNP_766120.1. NM_172532.3.
UniGeneMm.393311.

3D structure databases

ProteinModelPortalQ8BWF0.
SMRQ8BWF0. Positions 44-523.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8BWF0. 1 interaction.
STRINGQ8BWF0.

PTM databases

PhosphoSiteQ8BWF0.

Proteomic databases

PRIDEQ8BWF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037615; ENSMUSP00000040591; ENSMUSG00000035936.
GeneID214579.
KEGGmmu:214579.
NMPDRfig|10090.3.peg.27594.

Organism-specific databases

CTD7915.
MGIMGI:2441982. Aldh5a1.

Phylogenomic databases

eggNOGroNOG15833.
GeneTreeENSGT00550000075018.
HOGENOMHBG752218.
HOVERGENHBG108515.
InParanoidQ8BWF0.
OMAMIQNKDD.
OrthoDBEOG4255SZ.
PhylomeDBQ8BWF0.

Gene expression databases

ArrayExpressQ8BWF0.
BgeeQ8BWF0.
CleanExMM_ALDH5A1.
GenevestigatorQ8BWF0.
GermOnlineENSMUSG00000035936. Mus musculus.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010102. Succ_semiAld_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK00139.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR01780. SSADH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374368.
SOURCESearch...

Entry information

Entry nameSSDH_MOUSE
AccessionPrimary (citable) accession number: Q8BWF0
Secondary accession number(s): Q5SZW1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

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