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P13195 (HEM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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

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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Pathway

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

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

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_processcellular response to insulin stimulus

Inferred from expression pattern PubMed 11716532. Source: RGD

cellular response to organic cyclic compound

Inferred from expression pattern PubMed 11368315. Source: RGD

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to cAMP

Inferred from expression pattern PubMed 17761694. Source: RGD

response to cobalt ion

Inferred from expression pattern PubMed 6688350PubMed 818637. Source: RGD

response to drug

Inferred from expression pattern PubMed 818637. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 18472004. Source: RGD

response to gonadotropin

Inferred from expression pattern PubMed 19467246. Source: RGD

response to herbicide

Inferred from expression pattern PubMed 12180188. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 9849899. Source: RGD

response to nickel cation

Inferred from expression pattern PubMed 925603. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 17537461. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18657588. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 17761694. Source: RGD

response to platinum ion

Inferred from expression pattern PubMed 925603. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 17761694. Source: RGD

   Molecular_function5-aminolevulinate synthase activity

Inferred from direct assay PubMed 16125296Ref.2. Source: RGD

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
Chain57 – 6425865-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000001232

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 conflict118 – 13619SQTGS…LQEDV → ARRAAASSARPVWSFRRTW in AAA40790. Ref.1
Sequence conflict1441K → T in AAA40790. Ref.1
Sequence conflict1951S → V in AAA40790. Ref.1
Sequence conflict244 – 2452KK → NN in AAA40790. Ref.1
Sequence conflict2511C → S in AAA40790. Ref.1
Sequence conflict3771V → L in AAA40724. Ref.2
Sequence conflict5871F → Y in AAA40790. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13195 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: B28FC05D5F834886

FASTA64271,021
        10         20         30         40         50         60 
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTVST SAAQCQQVKE 

        70         80         90        100        110        120 
TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPPGHPSP STSQSSGSKC PFLAAQLSQT 

       130        140        150        160        170        180 
GSSVFRKASL ELQEDVQEMH AVRKEVAQSP VLPSLVNAKR DGEGPSPLLK NFQDIMRKQR 

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

       250        260        270        280        290        300 
LITKKQVSVW CSNDYLGMSR HPRVCGAVIE TVKQHGAGAG GTRNISGTSK FHVELEQELA 

       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 
YGASGGGIGD RDGVMPKMDI ISGTLGKAFG CVGGYIASTS LLIDTVRSYA AGFIFTTSLP 

       490        500        510        520        530        540 
PMLLAGALES VRILKSNEGR ALRRQHQRNV KLMRQMLMDA GLPVIHCPSH IIPVRVADAA 

       550        560        570        580        590        600 
KNTEICDELM TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFLE KLLLTWKRVG 

       610        620        630        640 
LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of 5-aminolevulinate synthase mRNA in different rat tissues."
Srivastava G., Borthwick I.A., Maguire D.J., Elferink C.J., Bawden M.J., Mercer J.F.B., May B.K.
J. Biol. Chem. 263:5202-5209(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Structure, turnover, and heme-mediated suppression of the level of mRNA encoding rat liver delta-aminolevulinate synthase."
Yamamoto M., Kure S., Engel J.D., Hiraga K.
J. Biol. Chem. 263:15973-15979(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03190 mRNA. Translation: AAA40790.1.
J04044 mRNA. Translation: AAA40724.1.
BC061793 mRNA. Translation: AAH61793.1.
PIRSYRTAL. A28191.
RefSeqNP_077810.2. NM_024484.2.
UniGeneRn.97126.

3D structure databases

ProteinModelPortalP13195.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP13195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65155.
KEGGrno:65155.

Organism-specific databases

CTD211.
RGD68392. Alas1.

Phylogenomic databases

HOVERGENHBG005954.
KOK00643.
PhylomeDBP13195.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Gene expression databases

GenevestigatorP13195.

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. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614001.
PROP13195.

Entry information

Entry nameHEM1_RAT
AccessionPrimary (citable) accession number: P13195
Secondary accession number(s): Q6P782
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: September 27, 2004
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways