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Q2FXR3 (HEM2_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SAOUHSC_01772
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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
Reference 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Delta-aminolevulinic acid dehydratase
PRO_0000247939

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

Experimental info

Sequence conflict314 – 3152FA → C in AAC45835. Ref.1
Sequence conflict3241K → N in AAC45835. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2FXR3 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: BF24378E01E7C93E

FASTA32436,583
        10         20         30         40         50         60 
MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG VYQISLNLLE 

        70         80         90        100        110        120 
SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA TRIAKKMYDD LLIVADTCLC 

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

       190        200        210        220        230        240 
EAGYYNIPIM SYGVKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE 

       250        260        270        280        290        300 
GCDMMIVKPA LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV 

       310        320 
SMKRAGADMI ITYFAKDICR YLDK

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for early steps in heme biosynthesis."
Kafala B., Sasarman A.
Gene 199:231-239(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U89396 Genomic DNA. Translation: AAC45835.1.
CP000253 Genomic DNA. Translation: ABD30841.1.
RefSeqYP_500277.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2FXR3.
SMRQ2FXR3. Positions 5-318.
ModBaseSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_01772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30841; ABD30841; SAOUHSC_01772.
GeneID3919690.
KEGGsao:SAOUHSC_01772.
PATRIC19580911. VBIStaAur99865_1616.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAMIISYHA.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-1691-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_STAA8
AccessionPrimary (citable) accession number: Q2FXR3
Secondary accession number(s): P50915
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 21, 2006
Last modified: May 29, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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