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Q92G23 (HEM1_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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:RC1303
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever 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.

Sequence caution

The sequence AAL03841.1 differs from that shown. Reason: Erroneous initiation.

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_0000280897

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
Q92G23 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: D6E5838194CE8504

FASTA41446,238
        10         20         30         40         50         60 
MSYYDIIFSK HIDKIKSEGR YREFKALKRQ ADNFPFAEHA NKQIVMWCIN DYLGMSKHAK 

        70         80         90        100        110        120 
VMHASIDALL KYGVGSGGTR NIGGNNIAIL ELEKELANLH KKQAALVFTS GFVANDTTLA 

       130        140        150        160        170        180 
SLAKIMPDIV FFSDELNHAS IIAGITSSRA EKYIYRHLDV KHLEELLQSV DINRPKIVVF 

       190        200        210        220        230        240 
ESAYSMDGFF SPIKDIINLA KKYNALTFID EVHTVGLYGK QGGGIAELLN CSDQIDIIQG 

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

       310        320        330        340        350        360 
HQEVVTKLKN SFERFNIPYL KNESHIVPII IGDPIKTAKA SNMLLNEYGI YVQHINFPTV 

       370        380        390        400        410 
PRGTERLRII PTPAHTDKMI NDLSVALVQI FAELDIELSS AKELNEEVRL NLIA 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03841.1. Different initiation.
PIRG97862.
RefSeqNP_360940.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92G23.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC1303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03841; AAL03841; RC1303.
GeneID928451.
KEGGrco:RC1303.
PATRIC17890133. VBIRicCon45613_1495.

Organism-specific databases

CMRSearch...

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_RICCN
AccessionPrimary (citable) accession number: Q92G23
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: November 13, 2013
This is version 76 of the entry and version 2 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 conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways