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Q6FXE3 (HEM1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:CAGL0B02607g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length530 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
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? – 5305-aminolevulinate synthase, mitochondrialPRO_0000001238

Sites

Active site3191 By similarity
Binding site731Substrate By similarity
Binding site1861Substrate By similarity
Binding site2051Substrate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2661Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity
Binding site3481Pyridoxal phosphate By similarity
Binding site3491Pyridoxal phosphate By similarity
Binding site4341Substrate By similarity

Amino acid modifications

Modified residue3191N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FXE3 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 0C5F159D8408A5D2

FASTA53058,385
        10         20         30         40         50         60 
MFRPVLKVRP SFSYPYSIVS SRSVRLASTA TANANTAAAT STVAAHGTQE TPFDFEGHFE 

        70         80         90        100        110        120 
SELAKKRLDK SYRYFNNINR LAKEFPLAHR QLEDDKVTVW CSNDYLALSK NPQVLDAMRK 

       130        140        150        160        170        180 
TIDKYGAGAG GTRNIAGHNI PTMRLEAELA ALHKKEGALV FSSCYVANDA VISLLGQKVK 

       190        200        210        220        230        240 
DLVIFSDELN HASMIVGIKH ANRPKHIFRH NDLAQLEEML QMYPKSTPKL IAFESVYSMA 

       250        260        270        280        290        300 
GSVADINKIC DLAEKYGALT FLDEVHAVGL YGPHGAGVAE HCDFEAHRVA GIATPPQGDN 

       310        320        330        340        350        360 
GRLRTVMDRV DMITGTLGKS FGTVGGYVAA SSKLIDWVRS YAPGFIFTTT LPPAVMAGAA 

       370        380        390        400        410        420 
EAIRFQRSHL NLRQDQQRHT AYVKKGLHDL GIPVIPNPSH IVPVLIGNPD LAKQASDILM 

       430        440        450        460        470        480 
EKHRIYVQAI NFPTVSRGTE RLRITPTPGH TNDLSDILIA AVDDVFNELQ LPRIRDWEMQ 

       490        500        510        520        530 
GGLLGVGDKN FVPEPNLWTE EQLSFSNEDL NSNVFEPVID QLEVSSGVKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380948 Genomic DNA. Translation: CAG57984.1.
RefSeqXP_445084.1. XM_445084.1.

3D structure databases

ProteinModelPortalQ6FXE3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2886690.
KEGGcgr:CAGL0B02607g.

Phylogenomic databases

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_CANGA
AccessionPrimary (citable) accession number: Q6FXE3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 72 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