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O67876 (HEM2_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. 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:aq_2109
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length330 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Delta-aminolevulinic acid dehydratase
PRO_0000140491

Sites

Active site1981Schiff-base intermediate with substrate By similarity
Active site2511Schiff-base intermediate with substrate By similarity
Metal binding1231Zinc; catalytic By similarity
Metal binding1251Zinc; catalytic By similarity
Metal binding1331Zinc; catalytic By similarity
Metal binding2361Magnesium By similarity
Binding site2081Substrate 1 By similarity
Binding site2201Substrate 1 By similarity
Binding site2771Substrate 2 By similarity
Binding site3161Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O67876 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: AC70D2063D9C7457

FASTA33037,091
        10         20         30         40         50         60 
MIVGRFPSSR PRRLRRNENI RRLVRETHLT LDDLIYPIFV RWGENVVEEV PSMPGVYRYS 

        70         80         90        100        110        120 
VDKVVDAVKE VRDLGIPAII LFGIPEHKDE VGSDTWSEEG IIQRALRKIK KEVPDIYVIT 

       130        140        150        160        170        180 
DVCFCEYTTH GHCGVLHDHD VENDLTLENL KKQVVSHAEN GADMVAPSGM MDGMVKVIRE 

       190        200        210        220        230        240 
ALDEAGFKHI PIMAYSAKFA SAYYGPFREA AESAPAFGDR RTYQMDPANS REALKEVLMD 

       250        260        270        280        290        300 
VEEGADVVMV KPALAYLDII AKVKENVLVP VCAYNVSGEY SLIKAAGKLG WIDEKKVMWE 

       310        320        330 
TLLSIKRAGA DMIITYFAKD AARMIIEGEV 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07837.1.
PIRH70480.
RefSeqNP_214445.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67876.
SMRO67876. Positions 9-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_2109.

Proteomic databases

PRIDEO67876.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07837; AAC07837; aq_2109.
GeneID1193865.
KEGGaae:aq_2109.
PATRIC20961068. VBIAquAeo85532_1627.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAGEYAMVE.
OrthoDBEOG6VXFCB.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1508-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_AQUAE
AccessionPrimary (citable) accession number: O67876
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 83 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