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Q02253 (MMSA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

Short name=MMSDH
Short name=Malonate-semialdehyde dehydrogenase [acylating]
EC=1.2.1.18
EC=1.2.1.27
Alternative name(s):
Aldehyde dehydrogenase family 6 member A1
Gene names
Name:Aldh6a1
Synonyms:Mmsdh
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.

Catalytic activity

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH.

3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion.

Tissue specificity

Expressed in the head and flagellum of epididymal sperm but not in testicular sperm (at protein level). Kidney > liver > heart > muscle > brain. Ref.5

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Mass spectrometry

Molecular mass is 57770.57 Da from positions 1 - 535. Determined by MALDI. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Ref.1 Ref.2 Ref.3
Chain33 – 535503Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
PRO_0000007190

Regions

Nucleotide binding209 – 2135NAD Potential
Nucleotide binding261 – 2666NAD Potential

Sites

Active site3171Nucleophile By similarity
Binding site4171NAD Potential

Amino acid modifications

Modified residue471N6-acetyllysine; alternate By similarity
Modified residue471N6-succinyllysine; alternate By similarity
Modified residue521N6-acetyllysine; alternate By similarity
Modified residue521N6-succinyllysine; alternate By similarity
Modified residue551N6-acetyllysine; alternate By similarity
Modified residue551N6-succinyllysine; alternate By similarity
Modified residue761N6-acetyllysine; alternate By similarity
Modified residue761N6-succinyllysine; alternate By similarity
Modified residue871N6-acetyllysine By similarity
Modified residue1171N6-acetyllysine; alternate By similarity
Modified residue1171N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue2981N6-acetyllysine By similarity
Modified residue3301N6-acetyllysine By similarity
Modified residue3311N6-acetyllysine By similarity
Modified residue3641N6-acetyllysine; alternate By similarity
Modified residue3641N6-succinyllysine; alternate By similarity
Modified residue3761N6-acetyllysine; alternate By similarity
Modified residue3761N6-succinyllysine; alternate By similarity
Modified residue3911N6-succinyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue5171N6-succinyllysine By similarity

Experimental info

Sequence conflict451D → N AA sequence Ref.1
Sequence conflict501E → Q AA sequence Ref.1
Sequence conflict1661D → N AA sequence Ref.1
Sequence conflict1681D → N AA sequence Ref.1
Sequence conflict1841P → T AA sequence Ref.1
Sequence conflict1901M → G AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q02253 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D914CE0311AA466A

FASTA53557,808
        10         20         30         40         50         60 
MAAAVAAAAA VRSRILQVSS KVNSTWYPAS SFSSSSVPTV KLFIDGKFVE SKSDKWIDIH 

        70         80         90        100        110        120 
NPATNEVVGR VPQSTKAEME AAVAACKRAF PAWADTSILS RQQVLLRYQQ LIKENLKEIA 

       130        140        150        160        170        180 
RLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMLGETM PSITKDMDLY SYRLPLGVCA 

       190        200        210        220        230        240 
GIAPFNFPAM IPLWMFPMAM VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG 

       250        260        270        280        290        300 
QHEAVNFICD HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN 

       310        320        330        340        350        360 
TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVERA KNLRVNAGDQ PGADLGPLIT 

       370        380        390        400        410        420 
PQAKERVCNL IDSGAKEGAS ILLDGRKIKV KGYENGNFVG PTIISNVKPS MTCYKEEIFG 

       430        440        450        460        470        480 
PVLVVLETET LDEAIKIVND NPYGNGTAIF TTNGAIARKY AHMVDVGQVG VNVPIPVPLP 

       490        500        510        520        530 
MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR 

« Hide

References

[1]"CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution."
Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A.
J. Biol. Chem. 267:19724-19729(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-50 AND 166-190.
Tissue: Liver.
[2]"Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase."
Goodwin G.W., Rougraff P.M., Davis E.J., Harris R.A.
J. Biol. Chem. 264:14965-14971(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-50, CHARACTERIZATION.
[3]"The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase."
Kedishvili N.Y., Popov K.M., Harris R.A.
Arch. Biochem. Biophys. 290:21-26(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
[4]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 56-70, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[5]"Differential proteomics leads to identification of domain specific epididymal sperm proteins."
Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.
J. Androl. 32:240-259(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, MASS SPECTROMETRY.
Strain: Holtzman.
Tissue: Sperm.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93401 mRNA. Translation: AAA41638.1.
PIRA44097.
RefSeqNP_112319.2. NM_031057.2.
UniGeneRn.2098.

3D structure databases

ProteinModelPortalQ02253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ02253. 1 interaction.
STRING10116.ENSRNOP00000015545.

Proteomic databases

PaxDbQ02253.
PRIDEQ02253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81708.
KEGGrno:81708.
UCSCRGD:621556. rat.

Organism-specific databases

CTD4329.
RGD621556. Aldh6a1.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271507.
HOVERGENHBG105023.
InParanoidQ02253.
KOK00140.
PhylomeDBQ02253.

Enzyme and pathway databases

SABIO-RKQ02253.

Gene expression databases

GenevestigatorQ02253.

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.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
PANTHERPTHR11699:SF27. PTHR11699:SF27. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615332.
PROQ02253.

Entry information

Entry nameMMSA_RAT
AccessionPrimary (citable) accession number: Q02253
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 11, 2014
This is version 122 of the entry and version 1 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