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Reviewed, UniProtKB/Swiss-Prot P45622 (HEM2_BRAJA)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
      Short name=ALAD
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase
Gene names
Name: hemB
Ordered Locus Names: blr5037
OrganismBradyrhizobium japonicum [Complete proteome] [HAMAP]
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Required for nodule development.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Magnesium.

Pathway

Porphyrin 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
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processheme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmagnesium 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 – 353353Delta-aminolevulinic acid dehydratase
PRO_0000140494

Regions

Region143 – 16119Magnesium-binding By similarity

Sites

Active site2751 By similarity

Sequences

Sequence LengthMass (Da)Tools
P45622-1 [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: 8226669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.
+Additional computationally mapped references.

Cross-references

Sequence databases

L24386 Genomic DNA. Translation: AAA89067.1.
BA000040 Genomic DNA. Translation: BAC50302.1. Different initiation.
PIRA49925.
RefSeqNP_771677.2.

3D structure databases

HSSPHSSP built from PDB template 1GZG based on UniProtKB Q59643.
ModBaseSearch...

Genome annotation databases

GeneID1051848.
GenomeReviewsGene locus blr5037 in contig BA000040_GR.
KEGGbja:blr5037.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP45622.

Enzyme and pathway databases

BioCycBJAP224911:BLR5037-MON.
BRENDA4.2.1.24. 280.

Family and domain databases

InterProIPR001731. 4pyrrol_synth_porphobiln_synth.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11458. AlaD_dehydratase. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
ProDomPD002304. AlaD_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_BRAJA
AccessionPrimary (citable) accession number: P45622
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents