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Q59295 (HEM2_CLOJO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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
OrganismClostridium josui
Taxonomic identifier1499 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length205 AA.
Sequence statusFragment.
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
   LigandMetal-binding
Zinc
   Molecular functionLyase
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 – ›205›205Delta-aminolevulinic acid dehydratase
PRO_0000140500

Sites

Active site1921Schiff-base intermediate with substrate By similarity
Metal binding1171Zinc; catalytic By similarity
Metal binding1191Zinc; catalytic By similarity
Metal binding1271Zinc; catalytic By similarity
Binding site2021Substrate By similarity

Experimental info

Non-terminal residue2051

Sequences

Sequence LengthMass (Da)Tools
Q59295 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 886F9DAEFDB1144E

FASTA20523,172
        10         20         30         40         50         60 
MIKRPRRLRT NEVLRKAVRE TRLSTDSLIW PLFIVEGKNI KKEISSLPGQ YHFSPDMVGK 

        70         80         90        100        110        120 
AIEAALKADV KSVLLFGLPK HKDEKGSEAY NENGVLQQGI REIKQRYPQM QVITDICMCE 

       130        140        150        160        170        180 
YTSHGHCGIL EGERVDNDRT LPYLEKIALS HVMAGADMIA PSDMMDGRIY ALRSTLDKNG 

       190        200 
FTDIPIMSYA VKYASSFYGP FREAA 

« Hide

References

[1]"Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FERM P-9684.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28503 Genomic DNA. Translation: BAA05863.1.
PIRI40812.

3D structure databases

ProteinModelPortalQ59295.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ59295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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]
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_CLOJO
AccessionPrimary (citable) accession number: Q59295
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 64 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