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Q8VC19 (HEM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-aminolevulinate synthase, nonspecific, mitochondrial
Short name=ALAS-H
EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase 1
Delta-ALA synthase 1
Delta-aminolevulinate synthase 1
Gene names
Name:Alas1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

nucleus

Inferred from electronic annotation. Source: Compara

   Molecular_function5-aminolevulinate synthase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Mitochondrion By similarity
Chain57 – 6425865-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000001231

Sites

Active site4471 By similarity
Binding site2191Substrate By similarity
Binding site3361Substrate By similarity
Binding site3551Substrate By similarity
Binding site3881Pyridoxal phosphate By similarity
Binding site4161Pyridoxal phosphate By similarity
Binding site4441Pyridoxal phosphate By similarity
Binding site4761Pyridoxal phosphate By similarity
Binding site4771Pyridoxal phosphate By similarity
Binding site5641Substrate By similarity

Amino acid modifications

Modified residue4471N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict1921L → S in AAA91867. Ref.2
Sequence conflict3911Missing in AAH22110. Ref.1
Sequence conflict4631I → T in AAA91867. Ref.2
Sequence conflict5011A → P in AAA91867. Ref.2
Sequence conflict6021E → V in AAA91867. Ref.2
Sequence conflict6251E → V in AAA91867. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8VC19 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 34E0CBEB8599CFE5

FASTA64271,018
        10         20         30         40         50         60 
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTLST SAVHCQQVKE 

        70         80         90        100        110        120 
TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPSGHPSP ATSQGSGSKC PFLAAQLSQT 

       130        140        150        160        170        180 
GSSVFRKASL ELQEDVQEMH AVRKEAAQSP VPPSLVNVKT DGEDPSRLLK NFQDIMRKQR 

       190        200        210        220        230        240 
PERVSHLLQD NLPKSVSTFQ YDHFFEKKID EKKNDHTYRV FKTVNRRAQI FPMADDYTDS 

       250        260        270        280        290        300 
LITKKQVSVW CSNDYLGMSR HPRVCGAVME TVKQHGAGAG GTRNISGTSK FHVELEQALA 

       310        320        330        340        350        360 
DLHGKDAALL FSSCFVANDS TLFTLAKMMP GCEIYSDSGN HASMIQGIRN SRVPKYIFRH 

       370        380        390        400        410        420 
NDVNHLRELL QRSDPSVPKI VAFETVHSMD GAVCPLEELC DVAHEFGAIT FVDEVHAVGL 

       430        440        450        460        470        480 
YGARGGGIGD RDGVMPKMDI ISGTLGKAFG CVGGYIASTS LLIDTVRSYA AGFIFTTSLP 

       490        500        510        520        530        540 
PMLLAGALES VRILKSSEGR ALRRQHQRNV KLLRQMLMDA GLPVIHCPSH IIPVRVADAA 

       550        560        570        580        590        600 
KNTEICDELM TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFVE KLLVTWKRVG 

       610        620        630        640 
LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[2]Young E.G., Dierks P.M.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-642.
Strain: DBA/2.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC022110 mRNA. Translation: AAH22110.1.
M63245 mRNA. Translation: AAA91867.1.
IPIIPI00121287.
RefSeqNP_065584.2. NM_020559.2.
UniGeneMm.290578.

3D structure databases

ProteinModelPortalQ8VC19.
SMRQ8VC19. Positions 201-592.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000117014.

PTM databases

PhosphoSiteQ8VC19.

Proteomic databases

PaxDbQ8VC19.
PRIDEQ8VC19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074082; ENSMUSP00000073725; ENSMUSG00000032786.
ENSMUST00000112524; ENSMUSP00000108143; ENSMUSG00000032786.
ENSMUST00000141118; ENSMUSP00000117014; ENSMUSG00000032786.
GeneID11655.
KEGGmmu:11655.

Organism-specific databases

CTD211.
MGIMGI:87989. Alas1.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00530000063111.
HOGENOMHOG000221020.
HOVERGENHBG005954.
InParanoidQ8VC19.
KOK00643.
OMAALPGCHI.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Gene expression databases

ArrayExpressQ8VC19.
BgeeQ8VC19.
CleanExMM_ALAS1.
GenevestigatorQ8VC19.
GermOnlineENSMUSG00000032786. Mus musculus.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 2 hits.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALAS1. mouse.
NextBio279265.
SOURCESearch...

Entry information

Entry nameHEM1_MOUSE
AccessionPrimary (citable) accession number: Q8VC19
Secondary accession number(s): Q64453
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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