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O28305 (HEM2_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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:AF_1974
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length322 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 – 322322Delta-aminolevulinic acid dehydratase
PRO_0000140522

Sites

Active site1951Schiff-base intermediate with substrate By similarity
Active site2481Schiff-base intermediate with substrate By similarity
Metal binding1201Zinc; catalytic By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1301Zinc; catalytic By similarity
Metal binding2331Magnesium By similarity
Binding site2051Substrate 1 By similarity
Binding site2171Substrate 1 By similarity
Binding site2741Substrate 2 By similarity
Binding site3121Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O28305 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5FE684E6B394B509

FASTA32236,398
        10         20         30         40         50         60 
MAEFPKVRMR RLRKANLRWM FREARLSPEN LITPIFVDEN IKEKKPIESM PDYFRIPLEM 

        70         80         90        100        110        120 
VDKEVEECLE KDLRSFILFG IPSYKDETGS SAYDQNGVIQ KAVRRIKAEF PDAVIVTDVC 

       130        140        150        160        170        180 
LCEYTTHGHC GVVKDGEIVN DETLPIIGKT AVSHAESGAD IVAPSGMMDG MVKAIREALD 

       190        200        210        220        230        240 
AAGFESTPIM SYSAKYASNF YSPFRDAAES GFKFGDRRGY QMDIHNAREA MREIELDVKE 

       250        260        270        280        290        300 
GADIIMVKPA LPYLDIIRMV RERFDLPLAA YNVSGEYSMI KAAIKNGWLS EEAIYEVLIS 

       310        320 
IKRAGADLII TYHSKEIAEK LQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89292.1.
PIRE69496.
RefSeqNP_070798.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28305.
SMRO28305. Positions 6-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF1974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89292; AAB89292; AF_1974.
GeneID1485196.
KEGGafu:AF1974.

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMADMILTYF.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-2011-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_ARCFU
AccessionPrimary (citable) accession number: O28305
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 86 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