Skip Header

Contribute Send feedback
Read comments (?) or add your own

P52713 (MMSA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
Short name=MMSDH
Short name=Malonate-semialdehyde dehydrogenase [acylating]
EC=1.2.1.18
EC=1.2.1.27
Gene names
Name:alh-8
ORF Names:F13D12.4
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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

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.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion By similarity
Chain23 – 523501Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
PRO_0000007191

Regions

Nucleotide binding199 – 2035NAD Potential
Nucleotide binding251 – 2566NAD Potential

Sites

Active site3071Nucleophile By similarity
Binding site4071NAD Potential

Sequences

Sequence LengthMass (Da)Tools
P52713 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2871499FE3267A29

FASTA52356,462
        10         20         30         40         50         60 
MLSRLARVQP KCQQLAHFST SKSAAAAPTV KLWIDGQAVE SKTTDFVELT NPATNEVIAM 

        70         80         90        100        110        120 
VPNATQAEMQ AAVDSAKNAF NTWKNTSPLT RQQCMFKLQA LIKRDMKKLA ESITIEQGKT 

       130        140        150        160        170        180 
LPDAEGDVSR GLQVVEHACS VPSLMMGETL PNVSRDMDTH SYRIPLGVTA GICPFNFPAM 

       190        200        210        220        230        240 
IPLWMFPVAL ATGNTMVIKP SEQDPGAAQL LVELAKEAGV PDGCVNIIHG QHSAVNFICD 

       250        260        270        280        290        300 
NPDIKAISFV GGDAAGKHIY ERGAKNGKRV QSNMGAKNHG VIMADANKEQ TLNQLTAAAF 

       310        320        330        340        350        360 
GAAGQRCMAL TTAVLVGEAR AWLPELVEKA KNLKVNAGWK PDTDIGPLIS KQSKARVLRL 

       370        380        390        400        410        420 
IESAKKEGAQ VPLDGSNITV PGFENGNFVG PTILAGVKPN MTCYREEIFG PVLVVMEAEN 

       430        440        450        460        470        480 
LNEAIEIINN NPYGNGTAIF TSNGATARKF TNEVDVGQIG INVPIPVPLP MFSFTGSRGS 

       490        500        510        520 
FLGDLNFYGK AGIQFYTQWK TVTQYWNESL TELKPQMSFP QLK

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z49127 Genomic DNA. Translation: CAA88946.1.
PIRT20828.
RefSeqNP_001022078.1. NM_001026907.2.

3D structure databases

ProteinModelPortalP52713.
SMRP52713. Positions 28-506.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-25038N.
MINTMINT-1076511.
STRING6239.F13D12.4a.2.

2D gel databases

World-2DPAGE0011:P52713.
0020:P52713.

Proteomic databases

PaxDbP52713.
PRIDEP52713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF13D12.4a.1; F13D12.4a.1; F13D12.4.
F13D12.4a.2; F13D12.4a.2; F13D12.4.
F13D12.4a.3; F13D12.4a.3; F13D12.4.
GeneID174800.
KEGGcel:CELE_F13D12.4.
UCSCF13D12.4a.2. c. elegans.

Organism-specific databases

CTD174800.
WormBaseF13D12.4a; CE02183; WBGene00000114; alh-8.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00560000077032.
HOGENOMHOG000271507.
InParanoidP52713.
KOK00140.
OMAVANQSEF.

Gene expression databases

ArrayExpressP52713.

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.
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. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio885562.

Entry information

Entry nameMMSA_CAEEL
AccessionPrimary (citable) accession number: P52713
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

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