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UniProtKB/Swiss-Prot entry Q02252

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

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Entry information
Entry name MMSA_HUMAN
Primary accession number Q02252
Secondary accession number Q9UKM8
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 24, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 88)
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
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MMSDH DEFICIENCY ARG-446.
TISSUE=Liver, and Lymphocyte;
DOI=10.1023/A:1005616315087; PubMed=10947204 [NCBI, ExPASy, EBI, Israel, Japan]
Chambliss K.L., Gray R.G.F., Rylance G., Pollitt R.J., Gibson K.M.;
"Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency.";
J. Inherit. Metab. Dis. 23:497-504(2000).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
Ding J.H., Yang B.Z., Wilkinson J., Roe C.R.;
"Molecular basis of human MMSDH deficiency: gene organization and mutation analysis.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ding J.H., Yang B.Z., Wilkinson J.K., Roe C.R.;
"The structure and organization of the methylmalonic semialdehyde dehydrogenase (MMSDH) gene.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 106-535.
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).
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.
  • CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.
  • SUBUNIT: Homotetramer.
  • SUBCELLULAR LOCATION: Mitochondrion.
  • DISEASE: Defects in ALDH6A1 are the cause of methylmalonate semialdehyde dehydrogenase deficiency (MMSDH deficiency) [MIM:603178]. This is characterized by elevated beta-alanine, 3-hydroxypropionic acid, and both isomers of 3-amino and 3-hydroxyisobutyric acids in urine organic acids.
  • SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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
AJ249994; CAB76468.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF159889; AAF80380.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF148505; AAF04489.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF148855; AAG29581.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004909; AAH04909.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032371; AAH32371.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M93405; AAA36328.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_005580.1; -.
UniGene Hs.293970
3D structure databases
HSSP Q28399; 1O9J. [HSSP ENTRY / PDB]
ModBase Q02252.
PTM databases
PhosphoSite Q02252; -.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
2D gel databases
REPRODUCTION-2DPAGE IPI00024990; -.
Organism-specific databases
H-InvDB HIX0011806; -.
HGNC HGNC:7179; ALDH6A1.
GenAtlas ALDH6A1.
MIM 603178; gene+phenotype. [NCBI / EBI]
PharmGKB PA24703; -.
GeneCards Q02252.
Gene expression databases
ArrayExpress Q02252; -.
CleanEx HS_ALDH6A1; -.
GermOnline ENSG00000119711; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (non-traceable author statement from UniProtKB).
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 sequence or structural similarity from UniProtKB).
GO:0004491; Molecular function: methylmalonate-semialdehyde dehydrogenase (acylating) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019859; Biological process: thymine metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006573; Biological process: valine metabolic process (inferred from sequence or structural similarity 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.
ProtoNet Q02252.
Proteomic databases
PeptideAtlas Q02252; -.
Genome annotation databases
Ensembl ENSG00000119711; Homo sapiens. [Contig view]
GeneID 4329; -.
KEGG hsa:4329; -.
NMPDR fig|9606.3.peg.9864; -.
Phylogenomic databases
HOGENOM Q02252; -.
HOVERGEN Q02252; -.
Other
DrugBank DB00157; NADH.
LinkHub Q02252; -.
NextBio 17035; -.
SOURCE ALDH6A1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Disease mutation; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    33  33     Mitochondrion (By similarity). 
CHAIN   34   535  502     Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial. PRO_0000007189
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). 
VARIANT   446   446  1     G -> R (in MMSDH deficiency). VAR_010244 
Sequence information
Length: 535 AA [This is the length of the unprocessed precursor] Molecular weight: 57840 Da [This is the MW of the unprocessed precursor] CRC64: 0786AF63897E7962 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAALLAAAAV RARILQVSSK VKSSPTWYSA SSFSSSVPTV KLFIGGKFVE SKSDKWIDIH 

        70         80         90        100        110        120 
NPATNEVIGR VPQATKAEMD AAIASCKRAF PAWADTSVLS RQQVLLRYQQ LIKENLKEIA 

       130        140        150        160        170        180 
KLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMMGETM PSITKDMDLY SYRLPLGVCA 

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

       250        260        270        280        290        300 
QHEAVNFICD HPDIKAISFV GSNKAGEYIF ERGSRHGKRV QANMGAKNHG VVMPDANKEN 

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

       370        380        390        400        410        420 
PQAKERVCNL IDSGTKEGAS ILLDGRKIKV KGYENGNFVG PTIISNVKPN MTCYKEEIFG 

       430        440        450        460        470        480 
PVLVVLETET LDEAIQIVNN NPYGNGTAIF TTNGATARKY AHLVDVGQVG VNVPIPVPLP 

       490        500        510        520        530 
MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR
Q02252 in FASTA format

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