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Q5HNN5 (HEM2_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:SERP1232
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [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_0000140518

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
Q5HNN5 [UniParc].

Last modified February 15, 2005. 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]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54583.1.
RefSeqYP_188806.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HNN5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP1232.

Proteomic databases

PRIDEQ5HNN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54583; AAW54583; SERP1232.
GeneID3241030.
KEGGser:SERP1232.
PATRIC19613313. VBIStaEpi130894_1199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMADMILTYF.
OrthoDBEOG6VXFCB.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-1259-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_STAEQ
AccessionPrimary (citable) accession number: Q5HNN5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 63 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