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

Q8CNZ0 (HEM2_STAES) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 72. 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:
Delta-aminolevulinic acid dehydratase

Short name=ALAD
Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:hemB
Ordered Locus Names:SE_1343
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen By similarity.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Binds 1 zinc ion per monomer By similarity.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer By similarity.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

porphobilinogen synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Delta-aminolevulinic acid dehydratase
PRO_0000140517

Sites

Active site1951Schiff-base intermediate with substrate By similarity
Active site2481Schiff-base intermediate with substrate By similarity
Metal binding1181Zinc; catalytic By similarity
Metal binding1201Zinc; catalytic By similarity
Metal binding1281Zinc; catalytic By similarity
Metal binding2331Magnesium By similarity
Binding site2051Substrate 1 By similarity
Binding site2171Substrate 1 By similarity
Binding site2741Substrate 2 By similarity
Binding site3131Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CNZ0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 31685329B5943A51

FASTA32436,570
        10         20         30         40         50         60 
MKFDRHRRLR SSKTMRDLVR ETHVRKEDLI YPIFVVEQDD IKSEIKSLPG IYQISLNLLH 

        70         80         90        100        110        120 
EEIKEAYDLG IRAIMFFGVP NDKDDIGSGA YDHNGVVQEA TRISKNLYKD LLIVADTCLC 

       130        140        150        160        170        180 
EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT AISQVEAGAD IIAPSNMMDG FVAEIREGLD 

       190        200        210        220        230        240 
QAGYQNIPIM SYGIKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE 

       250        260        270        280        290        300 
GCDMMIVKPS LSYLDIIRDV KNNTNVPVVA YNVSGEYSMT KAAALNGWID EEKIVMEQMI 

       310        320 
SMKRAGADLI ITYFAKDICR YLDK 

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015929 Genomic DNA. Translation: AAO04942.1.
RefSeqNP_764898.1. NC_004461.1.

3D structure databases

ProteinModelPortalQ8CNZ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176280.SE1343.

Proteomic databases

PRIDEQ8CNZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO04942; AAO04942; SE_1343.
GeneID1056288.
KEGGsep:SE1343.
PATRIC19608478. VBIStaEpi113981_1312.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMAGEYAMVE.
OrthoDBEOG6VXFCB.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycSEPI176280:GCDG-1349-MONOMER.
UniPathwayUPA00251; UER00318.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_STAES
AccessionPrimary (citable) accession number: Q8CNZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: November 13, 2013
This is version 72 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