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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC), Porphobilinogen deaminase (hemC)
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi118 – 1181Zinc; catalyticBy similarity
Metal bindingi120 – 1201Zinc; catalyticBy similarity
Metal bindingi128 – 1281Zinc; catalyticBy similarity
Active sitei195 – 1951Schiff-base intermediate with substrateBy similarity
Binding sitei205 – 2051Substrate 1By similarity
Binding sitei217 – 2171Substrate 1By similarity
Metal bindingi233 – 2331MagnesiumBy similarity
Active sitei248 – 2481Schiff-base intermediate with substrateBy similarity
Binding sitei274 – 2741Substrate 2By similarity
Binding sitei313 – 3131Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Delta-aminolevulinic acid dehydratasePRO_0000140516Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi93062.SACOL1715.

Structurei

3D structure databases

ProteinModelPortaliP0C1R9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C1R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG
60 70 80 90 100
VYQISLNLLE SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA
110 120 130 140 150
TRIAKKMYDD LLIVADTCLC EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT
160 170 180 190 200
AISQVEAGAD IIAPSNMMDG FVAEIRRGLD EAGYYNIPIM SYGVKYASSF
210 220 230 240 250
FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE GCDMMIVKPA
260 270 280 290 300
LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV
310 320
SMKRAGADMI ITYCKDICRY LDN
Length:323
Mass (Da):36,454
Last modified:July 25, 2006 - v1
Checksum:iA17C437EAD77D47E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S72488 Genomic DNA. Translation: AAB32123.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S72488 Genomic DNA. Translation: AAB32123.2.

3D structure databases

ProteinModelPortaliP0C1R9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0113.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of the hemB gene of Staphylococcus aureus."
    Kafala B., Sasarman A.
    Can. J. Microbiol. 40:651-657(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SA1959.

Entry informationi

Entry nameiHEM2_STAAU
AccessioniPrimary (citable) accession number: P0C1R9
Secondary accession number(s): P50915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 22, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.