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P26505 (HEM1_RHIRD) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. 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

EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene names
Name:hemA
OrganismRhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Taxonomic identifier358 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
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.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 4054055-aminolevulinate synthase
PRO_0000163824

Sites

Active site2481 By similarity
Binding site211Substrate By similarity
Binding site1371Substrate By similarity
Binding site1891Pyridoxal phosphate By similarity
Binding site2171Pyridoxal phosphate By similarity
Binding site2451Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate By similarity
Binding site2781Pyridoxal phosphate By similarity
Binding site3631Substrate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
P26505 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: F173AC1B13CAACDA

FASTA40544,412
        10         20         30         40         50         60 
MDFEAFFTTE LQSLHSEGRY RVFADIERQQ GNFPRATRYN ANGQRKDVTV WCSNDYLGMG 

        70         80         90        100        110        120 
QNPKVIEAMK AAIDHCGAGA GGTRNISGTN HYHVLLEQEL ADLHGKESAL IFTSGYVSNW 

       130        140        150        160        170        180 
ATLGTLGQKI PGLIIFSDAL NHASMIEGIR YGRCERVIWK HNDLEDLEAK LKAADPNAPK 

       190        200        210        220        230        240 
LIAFESVYSM DGDIAPIKEI CDLADRYGAM TYLDEVHAVG MYGPRGGGIA EREGLMDRLT 

       250        260        270        280        290        300 
IIEGTLGKAF GVMGGYITGS TAVCDFIRSF ASGFIFTTAL PPSLAAGAIA SIQHLKASPF 

       310        320        330        340        350        360 
ERARHQDRVR KLRGLLDARG IPHMDNPSHI VPVMVGDAAK CKWISDILLD SHGVYVQPIN 

       370        380        390        400 
YPTVPRKTER LRITPTPLHS DADIEHLVGA LHQLWSHCAL ARAVA 

« Hide

References

[1]"Cloning and nucleotide sequence of the hemA gene of Agrobacterium radiobacter."
Drolet M., Sasarman A.
Mol. Gen. Genet. 226:250-256(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 4718 / JCM 20199 / IAM 1526 / LMG 139 / NBRC 12664 / CIP 104326.

Cross-references

Sequence databases

PIRS15996.

3D structure databases

ProteinModelPortalP26505.
SMRP26505. Positions 2-395.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_RHIRD
AccessionPrimary (citable) accession number: P26505
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 16, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways