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P78698 (HEM1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. 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:KLLA0C15059g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length570 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.

Pathway

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

Subcellular location

Mitochondrion matrix.

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
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
Chain? – 5705-aminolevulinate synthase, mitochondrialPRO_0000001241

Sites

Active site3591 By similarity
Binding site1191Substrate By similarity
Binding site2321Substrate By similarity
Binding site2511Substrate By similarity
Binding site2841Pyridoxal phosphate By similarity
Binding site3121Pyridoxal phosphate By similarity
Binding site3561Pyridoxal phosphate By similarity
Binding site3881Pyridoxal phosphate By similarity
Binding site3891Pyridoxal phosphate By similarity
Binding site4741Substrate By similarity

Amino acid modifications

Modified residue3591N6-(pyridoxal phosphate)lysine Probable

Experimental info

Sequence conflict3321A → R in CAA63497. Ref.1
Sequence conflict4871T → S in CAA63497. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78698 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: CD9151C4A529AA89

FASTA57062,139
        10         20         30         40         50         60 
MESVIRSSAK ICPFMHSATG SMQSVKALKN ANLPAIAQQC PFMGKAMEQR RGYASSASGA 

        70         80         90        100        110        120 
SAAAAATATA STSASNSNSS VEASASADVV DHATKEASFD YQGLFDSDLA KKRMDKSYRF 

       130        140        150        160        170        180 
FNNINRLAKE FPMAHRKLED DKVTVWCSND YLALSKNQEV IEVMKKTLDK YGAGAGGTRN 

       190        200        210        220        230        240 
IAGHNKHALQ LEAELATLHK KEGALVFSSC FVANDAVISL LGQKIKDLVI FSDELNHASM 

       250        260        270        280        290        300 
IVGIKHASTK KHIFKHNNLD QLEELLAMYP KSTPKLIAFE SVYSMSGSVA DIDKICDLAE 

       310        320        330        340        350        360 
KYGALTFLDE VHAVGLYGPH GAGVAEHCNF DAHRKAGIAS PEFRTVMDRV DMITGTLGKS 

       370        380        390        400        410        420 
FGTVGGYVAG SLQLIDWVRS YAPGFIFTTT LPPAVMAGAA EAIRYQRSHL DLRQDQQRHT 

       430        440        450        460        470        480 
TYVKDGLADL GIPVMPNPSH IVPVLVGNPH LAKQASDILM DKHRIYVQAI NFPTVARGTE 

       490        500        510        520        530        540 
RLRITPTPGH TNDLSDILMD ALEDVWSTLQ LPRVRDWEAQ GGLLGVGDPN HVPQPNLWTK 

       550        560        570 
DQLTLTNNDL HPNVKQPIIE QLEVSSGIRY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92944 Genomic DNA. Translation: CAA63497.1.
CR382123 Genomic DNA. Translation: CAH01726.1.
RefSeqXP_452875.1. XM_452875.1.

3D structure databases

ProteinModelPortalP78698.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.P78698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2892616.
KEGGkla:KLLA0C15059g.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMAHYLQSIN.
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_KLULA
AccessionPrimary (citable) accession number: P78698
Secondary accession number(s): Q6CT64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2004
Last modified: May 14, 2014
This is version 99 of the entry and version 2 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