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A6QLI6 (HEM1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length647 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-containing compound 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 By similarity.

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

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_function5-aminolevulinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-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 – 6475915-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000352676

Sites

Active site4521 By similarity
Binding site2241Substrate By similarity
Binding site3411Substrate By similarity
Binding site3601Substrate By similarity
Binding site3931Pyridoxal phosphate By similarity
Binding site4211Pyridoxal phosphate By similarity
Binding site4491Pyridoxal phosphate By similarity
Binding site4811Pyridoxal phosphate By similarity
Binding site4821Pyridoxal phosphate By similarity
Binding site5691Substrate By similarity

Amino acid modifications

Modified residue4521N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QLI6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: DF0A4622352C9401

FASTA64771,062
        10         20         30         40         50         60 
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEIG AKPAPRALST SAVLCQQVTE 

        70         80         90        100        110        120 
TPPANEKDKA AKAEVQQAPD GSQQAPDGSQ QTADGTQLPS GHPSLASSQG TGSKCPFLAA 

       130        140        150        160        170        180 
EMSQGGSSVF RKASLALQED VQEMHAVREE VAQTSVNPSV INVKTEGGEL NGLLKNFQDI 

       190        200        210        220        230        240 
MRKQRPERVS HLLQDNLPKS VCTFQYDRFF EKKIDEKKND HSYRVFKTVN RKAQCFPMAD 

       250        260        270        280        290        300 
DYSDSLISKK QVSVWCSNDY LGMSRHPRVC GAVIDTLKQH GTGAGGTRNI SGTSKFHVDL 

       310        320        330        340        350        360 
EQELADLHGK DAALLFSSCF VANDSTLFTL AKMMPGCEIY SDAGNHASMI QGIRNSGVPK 

       370        380        390        400        410        420 
YIFRHNDVSH LRELLQRSDP AVPKIVAFET VHSMDGAVCP LEELCDVAHE FGAITFVDEV 

       430        440        450        460        470        480 
HAVGLYGLQG GGIGDRDGVM PKMDIISGTL GKAIGCVGGY IASTSSLIDT VRSYAAGFIF 

       490        500        510        520        530        540 
TTSLPPMLLA GALESVRILR STEGRTLRRQ HQRNVKLMRQ MLMDAGLPVV HCPSHIIPVR 

       550        560        570        580        590        600 
VADAAKNTEV CDELMTRHNI YVQAINYPTV PRGEELLRIA PTPHHTPQMM SYFVDNLLAT 

       610        620        630        640 
WKRVGLELKP HSSAECNFCR RPLHFEMMSE REKSYFSGMS KLVSAQA 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC147978 mRNA. Translation: AAI47979.1.
RefSeqNP_001094624.1. NM_001101154.1.
UniGeneBt.15857.

3D structure databases

ProteinModelPortalA6QLI6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000005380.

Proteomic databases

PRIDEA6QLI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005380; ENSBTAP00000005380; ENSBTAG00000004118.
GeneID534286.
KEGGbta:534286.

Organism-specific databases

CTD211.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00530000063111.
HOGENOMHOG000221020.
HOVERGENHBG005954.
InParanoidA6QLI6.
KOK00643.
OMAPQMMSYF.
OrthoDBEOG7TQV0F.
TreeFamTF300724.

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

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

NextBio20876339.

Entry information

Entry nameHEM1_BOVIN
AccessionPrimary (citable) accession number: A6QLI6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 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