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Q75DX7 (HEM1_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. 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, mitochondrial

EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene names
Name:HEM1
Ordered Locus Names:ABL104C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Subcellular location

Mitochondrion matrix 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

   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 – ?Mitochondrion Potential
Chain? – 5565-aminolevulinate synthase, mitochondrialPRO_0000001236

Sites

Active site3451 By similarity
Binding site1051Substrate By similarity
Binding site2181Substrate By similarity
Binding site2371Substrate By similarity
Binding site2701Pyridoxal phosphate By similarity
Binding site2981Pyridoxal phosphate By similarity
Binding site3421Pyridoxal phosphate By similarity
Binding site3741Pyridoxal phosphate By similarity
Binding site3751Pyridoxal phosphate By similarity
Binding site4601Substrate By similarity

Amino acid modifications

Modified residue3451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q75DX7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: DABDD7E6FEB4E764

FASTA55661,222
        10         20         30         40         50         60 
MDSLARQSAK ICPFVSRVTS SMQQVQVLHK TNMSAMAQQC PVMRRAMAAR GYVTASPPAG 

        70         80         90        100        110        120 
AAAADVGEAR PITPVLERGT QERTFDYDGL FETELQKKRL DSSYRFFNNI NRLAKEYPMA 

       130        140        150        160        170        180 
HRLEEEDKVT VWCSNDYLTY SRNEKVMETM KRTIDKYGAG AGGTRNIAGH NRHAMRLEAE 

       190        200        210        220        230        240 
LAALHKKEGA LVFSSCFVAN DAVLSLLGQK MPNMVIFSDE MNHASMIMGI KHANVQKHIF 

       250        260        270        280        290        300 
RHNDLQHLEE LLAMYPKSQP KLIAFESVYS MSGSVADIRK ICDLAEKYGA LTFLDEVHSV 

       310        320        330        340        350        360 
GLYGPHGAGV AEHLDFEAHR KAGLASPAQT TVLDRVDMIT ATLGKSFGSV GGYLAASEKL 

       370        380        390        400        410        420 
VDFVRSYAPG FIFTSSLPPA VMAGSAAAVF DQRSSLHLRQ LQQKHTSYVK TGLGDLGIPV 

       430        440        450        460        470        480 
QPNPSHIVPV LVGNPDLAKR ASDILMEKHR IYVQAINFPT VPRGTERLRI TPTPGHTNDL 

       490        500        510        520        530        540 
SDVLLDAMDD VWKTLQLPRV SDWAAHGGLL GVGEPDYVPE ANLWTEEQMS LTNDDLHPSV 

       550 
FSPVEKFLEV SSGIKA 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016815 Genomic DNA. Translation: AAS50667.1.
RefSeqNP_982843.1. NM_208196.1.

3D structure databases

ProteinModelPortalQ75DX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_ABL104C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS50667; AAS50667; AGOS_ABL104C.
GeneID4618923.
KEGGago:AGOS_ABL104C.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMAKLAQYPK.
OrthoDBEOG7HHX1P.

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.
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.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_ASHGO
AccessionPrimary (citable) accession number: Q75DX7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways