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

Q6BX71 (HEM1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. 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:DEHA2B05478g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length575 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? – 5755-aminolevulinate synthase, mitochondrialPRO_0000001239

Sites

Active site3641 By similarity
Binding site1241Substrate By similarity
Binding site2371Substrate By similarity
Binding site2561Substrate By similarity
Binding site2891Pyridoxal phosphate By similarity
Binding site3171Pyridoxal phosphate By similarity
Binding site3611Pyridoxal phosphate By similarity
Binding site3931Pyridoxal phosphate By similarity
Binding site3941Pyridoxal phosphate By similarity
Binding site4791Substrate By similarity

Amino acid modifications

Modified residue3641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6BX71 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 05107F73EB488A2C

FASTA57562,652
        10         20         30         40         50         60 
MESITRVSMS VCPFVKSSSA QALRQLSKNS ALTSQARQCP FMGAALNAKE STRSYSSATK 

        70         80         90        100        110        120 
PVRATASSLA SNPPSTMQSK YSFKAEELVG NKDAINLESK ENTFDFKGYL NSELSKKRTD 

       130        140        150        160        170        180 
KSYRFFNNIN RLANEFPKAH RSEENDKVTV WCSNDYLGMG KNENTINEMK RVLTKYGSGA 

       190        200        210        220        230        240 
GGTRNIAGHN IHALKLESEL AALHKHEAAL VFSSCFVAND AVLSLFGQKI KDLVIFSDEL 

       250        260        270        280        290        300 
NHASMIQGIR NSRAKKQVFK HNDLADLEEK LAQYPKSTPK LIAFESVYSM CGSIAPIEAI 

       310        320        330        340        350        360 
CDLAEKYGAL TFLDEVHAVG MYGPHGAGVA EHLDFDAHLK SGIASPQTQT VMNRVDMVTG 

       370        380        390        400        410        420 
TLGKAYGTVG GYITGKANLI DWFRSFAPGF IFTTTLPPSI MAGSSASIRY QRSTLQDRIA 

       430        440        450        460        470        480 
QQTNTRYVKN NLTDIGIPVI PNPSHIVPVL VGNALDAKKA SDLLLDKYNI YVQAINFPTV 

       490        500        510        520        530        540 
PIGQERLRIT PTPGHGPELS NQLIGALDSV FNELSLSRIG DWEGKGGLCG VGEPDIEPIE 

       550        560        570 
HIWTSEQLAL TDADINPNVI DPVIQPIGVS SGVRD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382134 Genomic DNA. Translation: CAG85193.1.
RefSeqXP_457198.1. XM_457198.1.

3D structure databases

ProteinModelPortalQ6BX71.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.Q6BX71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2913002.
KEGGdha:DEHA2B05478g.

Phylogenomic databases

eggNOGCOG0156.
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_DEBHA
AccessionPrimary (citable) accession number: Q6BX71
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: August 16, 2004
Last modified: November 13, 2013
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