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UniProtKB/Swiss-Prot entry Q02253

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMSA_RAT
Primary accession number Q02253
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 78)
Name and origin of the protein
Protein name Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial [Precursor]
Synonyms MMSDH
Malonate-semialdehyde dehydrogenase [acylating]
EC 1.2.1.27
EC 1.2.1.18
Aldehyde dehydrogenase family 6 member A1
Gene name
Name: Aldh6a1
Synonyms: Mmsdh
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-50 AND 166-190.
TISSUE=Liver;
PubMed=1527093 [NCBI, ExPASy, EBI, Israel, Japan]
Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A.;
"CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution.";
J. Biol. Chem. 267:19724-19729(1992).
[2]
 PROTEIN SEQUENCE OF 33-50, AND CHARACTERIZATION.
PubMed=2768248 [NCBI, ExPASy, EBI, Israel, Japan]
Goodwin G.W., Rougraff P.M., Davis E.J., Harris R.A.;
"Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase.";
J. Biol. Chem. 264:14965-14971(1989).
[3]
 PROTEIN SEQUENCE OF N-TERMINUS.
DOI=10.1016/0003-9861(91)90586-8; PubMed=1898092 [NCBI, ExPASy, EBI, Israel, Japan]
Kedishvili N.Y., Popov K.M., Harris R.A.;
"The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase.";
Arch. Biochem. Biophys. 290:21-26(1991).
[4]
 PROTEIN SEQUENCE OF 56-70, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M93401; AAA41638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A44097; A44097.
RefSeq NP_112319.2; -.
UniGene Rn.2098
3D structure databases
HSSP Q28399; 1O9J. [HSSP ENTRY / PDB]
ModBase Q02253.
Organism-specific databases
RGD 621556; Aldh6a1.
Gene expression databases
ArrayExpress Q02253; -.
GermOnline ENSRNOG00000011419; Rattus norvegicus.
Ontologies
GO
GO:0000062; Molecular function: acyl-CoA binding (inferred from sequence or structural similarity from UniProtKB).
GO:0018478; Molecular function: malonate-semialdehyde dehydrogenase (acetylating) activity (inferred from direct assay from UniProtKB).
GO:0004491; Molecular function: methylmalonate-semialdehyde dehydrogenase (acylating) activity (inferred from direct assay from UniProtKB).
GO:0019859; Biological process: thymine metabolic process (inferred from direct assay from UniProtKB).
GO:0006573; Biological process: valine metabolic process (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR010061; MeMal-semiAld_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF27; MMSDH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01722; MMSDH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
BLOCKS Q02253.
ProtoNet Q02253.
Genome annotation databases
Ensembl ENSRNOG00000011419; Rattus norvegicus. [Contig view]
GeneID 81708; -.
KEGG rno:81708; -.
Phylogenomic databases
HOVERGEN Q02253; -.
Other
NextBio 615332; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    32  32     Mitochondrion. 
CHAIN   33   535  503     Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial. PRO_0000007190
NP_BIND   209   213  5     NAD (Potential). 
NP_BIND   261   266  6     NAD (Potential). 
ACT_SITE   317   317        Nucleophile (By similarity). 
BINDING   417   417        NAD (Potential). 
MOD_RES   55    55        N6-acetyllysine (By similarity). 
MOD_RES   117   117        N6-acetyllysine (By similarity). 
MOD_RES   331   331        N6-acetyllysine (By similarity). 
CONFLICT   45    45        D -> N (in Ref. 1; AA sequence). 
CONFLICT   50    50        E -> Q (in Ref. 1; AA sequence). 
CONFLICT   166   166        D -> N (in Ref. 1; AA sequence). 
CONFLICT   168   168        D -> N (in Ref. 1; AA sequence). 
CONFLICT   184   184        P -> T (in Ref. 1; AA sequence). 
CONFLICT   190   190        M -> G (in Ref. 1; AA sequence). 
Sequence information
Length: 535 AA [This is the length of the unprocessed precursor] Molecular weight: 57808 Da [This is the MW of the unprocessed precursor] CRC64: D914CE0311AA466A [This is a checksum on the sequence] 
        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
Q02253 in FASTA format

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