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Q9ZCB8 (HEM1_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. 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:RP841
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus 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
Reference 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_0000163831

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
Q9ZCB8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 9763C4E1966A2822

FASTA41446,516
        10         20         30         40         50         60 
MSYYDTIFNK HIDKIKSEGR YREFKSLKRQ ADNFPFAEYE DKQIVMWCIN DYLGMSKHVK 

        70         80         90        100        110        120 
VMQASIDALL KYGVGSGGTR NIGGNNISIL ELEKELADLH SKETALVFTS GFVANDTTLA 

       130        140        150        160        170        180 
SLAKIIPDIV FFSDELNHAS IIAGIKSSRA EKYVYRHLDV QHLEKLLQSV DINKPKIIVF 

       190        200        210        220        230        240 
ESAYSMDGFF SPIKDIINLA KKYNALTFID EVHTVGLYGK QGGGISELLD CSNQIDIIQG 

       250        260        270        280        290        300 
TLAKAYGTIG GYITSNYNLI DAIRLTAPGF IFTTSLPPVI STAATHSIRH LKESNEERIK 

       310        320        330        340        350        360 
HQEVVTKLKN SFEHFNIPYL KNESHIIPII IGDPIKATKV SNMLLNEYGI YVQHINFPTV 

       370        380        390        400        410 
PRGTERLRII PTPAHTDKMI NDLSTALVHI FDELDIELSS AKELNKEVRL HLIA 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235273 Genomic DNA. Translation: CAA15265.1.
PIRA71646.
RefSeqNP_221189.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZCB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP841.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15265; CAA15265; CAA15265.
GeneID883292.
KEGGrpr:RP841.
PATRIC17902558. VBIRicPro72556_0879.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMARAEKYIY.
OrthoDBEOG6Q8HZD.
ProtClustDBPRK09064.

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_RICPR
AccessionPrimary (citable) accession number: Q9ZCB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 13, 2013
This is version 88 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 prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways