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P45622 (HEM2_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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:blr5037
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Required for nodule development. Ref.1

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.1

Cofactor

Magnesium. Ref.1

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.

Sequence caution

The sequence BAC50302.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   LigandMagnesium
Metal-binding
   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 – 353353Delta-aminolevulinic acid dehydratase
PRO_0000140494

Sites

Active site2211Schiff-base intermediate with substrate By similarity
Active site2751Schiff-base intermediate with substrate By similarity
Metal binding2601Magnesium By similarity
Binding site2311Substrate 1 By similarity
Binding site2441Substrate 1 By similarity
Binding site3011Substrate 2 By similarity
Binding site3401Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P45622 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F143FA4892ACF1F8

FASTA35338,582
        10         20         30         40         50         60 
MAIKYGRPIE LREVSRRDGA AASPALDLAI RPRRNRKAEW ARRMVRENVL TTDDLIWPLF 

        70         80         90        100        110        120 
LIDGNNKREQ IASMPGVERL SVDQAVREAE RAMKLTIPCI ALFPYTDPSL RDEEGSEACN 

       130        140        150        160        170        180 
PNNLVCQAVR AIKKEFPEIG VLCDVALDPF TSHGHDGLIA DGAILNDETV AVLVRQALVQ 

       190        200        210        220        230        240 
AEAGCDIIAP SDMMDGRVAA IREGLDQAGL IDVQIMAYAA KYASAFYGPF RDAIGSAKTL 

       250        260        270        280        290        300 
TGDKRTYQMD SANTDEALRE VELDISEGAD MVMVKPGMPY LDVVRRVKDT FAMPTFAYQV 

       310        320        330        340        350 
SGEYAMIAAA AGNGWLDGDR AMMESLLAFK RAGADGVLSY FAPKAAEKLR TQG 

« Hide

References

« Hide 'large scale' references
[1]"Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain."
Chauhan S., O'Brian M.R.
J. Bacteriol. 175:7222-7227(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
Strain: I110.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24386 Genomic DNA. Translation: AAA89067.1.
BA000040 Genomic DNA. Translation: BAC50302.1. Different initiation.
PIRA49925.
RefSeqNP_771677.2. NC_004463.1.

3D structure databases

ProteinModelPortalP45622.
SMRP45622. Positions 31-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr5037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC50302; BAC50302; BAC50302.
GeneID1051848.
KEGGbja:blr5037.
PATRIC21193740. VBIBraJap65052_5115.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OrthoDBEOG6VXFCB.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-5074-MONOMER.
RETL1328306-WGS:GSTH-1519-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_BRADU
AccessionPrimary (citable) accession number: P45622
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 87 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