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Reviewed, UniProtKB/Swiss-Prot Q9EQ20 (MMSA_MOUSE)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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=1.2.1.27
    EC=1.2.1.18
Alternative name(s):
    Aldehyde dehydrogenase family 6 member A1
Gene names
Name: Aldh6a1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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General annotation (Comments)

Function

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

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 By similarity.

Subcellular location

Mitochondrion By similarity.

Post-translational modification

Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion By similarity
Chain33 – 535503Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
PRO_0000320299

Regions

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

Sites

Active site3171Nucleophile By similarity
Binding site4171NAD Potential

Amino acid modifications

Modified residue551N6-acetyllysine Ref.4
Modified residue1171N6-acetyllysine Ref.4
Modified residue3311N6-acetyllysine Ref.4

Experimental info

Sequence conflict551K → R in BAE41702. Ref.2
Sequence conflict1411G → C in AAH33440. Ref.3
Sequence conflict2111S → P in BAE41702. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9EQ20-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 1EF4ED4C4FE2284D

FASTA53557,916
        10         20         30         40         50         60 
MAAAVAAAAA MRSRILQVSS KVNATWYPAS SFSSSSVPTV KLFIDGKFVE SKSDKWIDIH 

        70         80         90        100        110        120 
NPATNEVVGR VPQSTKAEMD AAVESCKRAF 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 
QHDAVNFICD HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN 

       310        320        330        340        350        360 
TLNQLVGAAF GAAGQRCMAL STAILVGEAK KWLPELVDRA KNLRVNAGDQ PGADLGPLIT 

       370        380        390        400        410        420 
PQAKERVCNL IDSGTKEGAS ILLDGRRIKV KGYENGNFVG PTIISNVKPS MTCYKEEIFG 

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

       490        500        510        520        530 
MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR

« Hide

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References

« Hide 'large scale' references
[1]"Mouse methylmalonate-semialdehyde dehydrogenase (MMSDH) cDNA and gene map."
Yang B.-Z., Zhang L.-F., Roe C.R., Ding J.-H.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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 and NOD.
Tissue: Cecum, Kidney and Spleen.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-117 AND LYS-331, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF297860 mRNA. Translation: AAG44988.1.
AK033587 mRNA. Translation: BAC28375.1.
AK147146 mRNA. Translation: BAE27715.1.
AK155814 mRNA. Translation: BAE33445.1.
AK169915 mRNA. Translation: BAE41455.1.
AK170305 mRNA. Translation: BAE41702.1.
AK171581 mRNA. Translation: BAE42539.1.
AK171896 mRNA. Translation: BAE42726.1.
BC033440 mRNA. Translation: AAH33440.1.
IPIIPI00461964.
RefSeqNP_598803.1.
UniGeneMm.247510

3D structure databases

HSSPHSSP built from PDB template 1O9J based on UniProtKB Q28399.
ModBaseSearch...

PTM databases

PhosphoSiteQ9EQ20.

Proteomic databases

PRIDEQ9EQ20.

Genome annotation databases

EnsemblENSMUSG00000021238. Mus musculus. [Contig view]
GeneID104776.
KEGGmmu:104776.

Organism-specific databases

MGIMGI:1915077. Aldh6a1.

Phylogenomic databases

HOVERGENQ9EQ20.
OMAQ9EQ20. IISNVKP.

Enzyme and pathway databases

BRENDA1.2.1.18. 244.
1.2.1.27. 244.

Gene expression databases

ArrayExpressQ9EQ20.
BgeeQ9EQ20.
CleanExMM_ALDH6A1.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PTHR11699:SF27. MMSDH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio357280.
SOURCESearch...

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Entry information

Entry nameMMSA_MOUSE
AccessionPrimary (citable) accession number: Q9EQ20
Secondary accession number(s): Q3TDA2, Q8CIB4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents