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Q1RIV2 (HEM1_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:RBE_0631
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
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.

Sequence similarities

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

Ontologies

Keywords
   Biological processHeme biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
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 – 4144145-aminolevulinate synthase
PRO_0000280896

Sites

Active site2441 By similarity
Binding site221Substrate By similarity
Binding site1331Substrate By similarity
Binding site1521Substrate By similarity
Binding site1851Pyridoxal phosphate By similarity
Binding site2131Pyridoxal phosphate By similarity
Binding site2411Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site2741Pyridoxal phosphate By similarity
Binding site3591Substrate By similarity

Amino acid modifications

Modified residue2441N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
Q1RIV2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 7D110EE50478F213

FASTA41445,964
        10         20         30         40         50         60 
MSYYDTIFSD HIDKIKSEGR YREFKALKRQ ADNFPFAMCD DKQIVMWCIN DYLGMSKHPK 

        70         80         90        100        110        120 
VVQASIDAVL KYGVGSGGTR NIGGNNVAIL ELEQELASLH NKEASLVFTS GFVANDTTLA 

       130        140        150        160        170        180 
TLAKIMPNIV FFSDELNHAS IIAGITGSKA EKHIYRHLDV KHLEELLQSV DINRPKIIVF 

       190        200        210        220        230        240 
ESAYSMDGFF SPVKDIINLA KKYNALTFID EVHTVGLYGK TGAGIAELLD CSDEIDIIQG 

       250        260        270        280        290        300 
TLAKAYGTIG GYITANHSLI DAIRLSASGF IFTTSLPPVI STAATHSIRH LKESNQERKT 

       310        320        330        340        350        360 
HQQVVSKLKS SFDRFNIPYL KNESHIVPII IGDPIKASKA SNMLLNEYSI YVQHINFPTV 

       370        380        390        400        410 
PRGTERLRII PTPAHTDEMI NDLSIALVQI FAALNIELSS TKELNDEIYL NLIA 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04712.1.
RefSeqYP_537801.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RIV2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04712; ABE04712; RBE_0631.
GeneID3995921.
KEGGrbe:RBE_0631.
PATRIC17882712. VBIRicBel102610_0723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMAHYLQSIN.
OrthoDBEOG6Q8HZD.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-650-MONOMER.
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_RICBR
AccessionPrimary (citable) accession number: Q1RIV2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 57 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

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways