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Q9ZMR8 (HEM2_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. 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:jhp_0150
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length323 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
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 – 323323Delta-aminolevulinic acid dehydratase
PRO_0000140503

Sites

Active site1931Schiff-base intermediate with substrate By similarity
Active site2461Schiff-base intermediate with substrate By similarity
Metal binding1181Zinc; catalytic By similarity
Metal binding1201Zinc; catalytic By similarity
Metal binding1281Zinc; catalytic By similarity
Metal binding2311Magnesium By similarity
Binding site2031Substrate 1 By similarity
Binding site2151Substrate 1 By similarity
Binding site2721Substrate 2 By similarity
Binding site3111Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZMR8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 06938C45FE367F12

FASTA32336,251
        10         20         30         40         50         60 
MFKRLRRLRS SENLRAMVRE TRLNINDFIA PLFVIESDSG IKNEISSMPG VYQMSIEPLL 

        70         80         90        100        110        120 
KECEELVGLG IKAVLLFGIP KHKDATGSHA LNKDHIVAKA TREIKKRFKD LIVIADLCFC 

       130        140        150        160        170        180 
EYTDHGHCGI LENASVSNDK TLKILNLQGL ILAESGVDIL APSNMMDGNV LSLRKALDKA 

       190        200        210        220        230        240 
GYFHTPIMSY STKFASSYYG PFRDVANSPP SFGDRKSYQM DYANQKEALL ESLEDEKQGA 

       250        260        270        280        290        300 
DILMVKPALA YLDIVKEIRD HTLLPLALYN VSGEYAMLKL AQKHNLINYE SVLLETMTCF 

       310        320 
KRAGADMIIS YHAKEVANLL QRN 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD05731.1.
PIRH71968.
RefSeqNP_222871.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZMR8.
SMRQ9ZMR8. Positions 1-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp0150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD05731; AAD05731; jhp_0150.
GeneID889168.
KEGGhpj:jhp0150.
PATRIC20604918. VBIHelPyl98156_0171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMAQMNPANR.
OrthoDBEOG6VXFCB.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-157-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZMR8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 89 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