Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6CCW0 (HEM1_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:YALI0C06083g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length563 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? – 5635-aminolevulinate synthase, mitochondrialPRO_0000001244

Sites

Active site3761 By similarity
Binding site1371Substrate By similarity
Binding site2511Substrate By similarity
Binding site2701Substrate By similarity
Binding site3031Pyridoxal phosphate By similarity
Binding site3311Pyridoxal phosphate By similarity
Binding site3731Pyridoxal phosphate By similarity
Binding site4051Pyridoxal phosphate By similarity
Binding site4061Pyridoxal phosphate By similarity
Binding site4911Substrate By similarity

Amino acid modifications

Modified residue3761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CCW0 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: FC7BBC2F382C0170

FASTA56361,237
        10         20         30         40         50         60 
MESLVRQSKK LCPYIGRTSA SSLKQLGNGR LTQKAGQCPI MGKAMGVRGF KSDAGSNAES 

        70         80         90        100        110        120 
ATVDVHAAVD TSKGTCPHAA QYSPVYPSSR LDNYPFGMTQ RGLGKVPTQD AHNATTFNYE 

       130        140        150        160        170        180 
SFYENKINAK HQDKSYRYFN NINRLAAEFP RAHRGSIEED KVTVWCANDY LGMGRNPVVV 

       190        200        210        220        230        240 
DAMHETLDKY GAGAGGTRNI AGHNRHAVEL EAAIADLHKK EAALVFSSCY VANDSTLSLL 

       250        260        270        280        290        300 
GQALPNCVYF SDASNHASMI HGIRHGGSEK VVWKHNDLAD LEAKLARYPK STPKVIAFES 

       310        320        330        340        350        360 
VYSMCGSIGP IEEICDLADK YGAITFLDEV HAVGMYGPTG AGVAEHLDFE HYHSGAQTQR 

       370        380        390        400        410        420 
QPIMDRVDIF TGTLGKAYGC VGGYIAGSAK FVDMVRSYAP GFIFTTTLPP ATMAGARAAI 

       430        440        450        460        470        480 
NYQKATMKDR VAQQTHTRYV KDKLANRGIP VVPNPSHIVP VLVGDAQKAK AASDLLLTKH 

       490        500        510        520        530        540 
QIYVQAINFP TVPIGQERLR VTPTPGHHEG LCDELVAALE DVWQELDLKR VEDWTAEGGL 

       550        560 
CGVGEGVEVE PLWSEEQLSY GRD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382129 Genomic DNA. Translation: CAG81803.1.
RefSeqXP_501502.1. XM_501502.1.

3D structure databases

ProteinModelPortalQ6CCW0.
SMRQ6CCW0. Positions 118-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.Q6CCW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAG81803; CAG81803; YALI0_C06083g.
GeneID2909236.
KEGGyli:YALI0C06083g.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMAERESASC.
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_YARLI
AccessionPrimary (citable) accession number: Q6CCW0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: August 16, 2004
Last modified: May 14, 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