Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O26839 (HEM2_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. 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:MTH_744
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length326 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 – 326326Delta-aminolevulinic acid dehydratase
PRO_0000140525

Sites

Active site2001Schiff-base intermediate with substrate By similarity
Active site2531Schiff-base intermediate with substrate By similarity
Metal binding1251Zinc; catalytic By similarity
Metal binding1271Zinc; catalytic By similarity
Metal binding1351Zinc; catalytic By similarity
Metal binding2381Magnesium By similarity
Binding site2101Substrate 1 By similarity
Binding site2221Substrate 1 By similarity
Binding site2791Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O26839 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 29EDC9060F39A170

FASTA32635,841
        10         20         30         40         50         60 
MSDNMEFPTK RMRRLRKSPQ IRNILRETRL HPSDLIYPMF VSEKLGRGDV EAIDTMPGQF 

        70         80         90        100        110        120 
RYSVDDAVSE ASRLEDEGLS SVLIFGMPSA KDELASAAHD PHGVVQRTVR RLKEETDLVV 

       130        140        150        160        170        180 
MTDVCLCQYT SHGHCGIVVD GEIVNDETLE VLSRIALSHA EAGADVVAPS DMMDGRVAAI 

       190        200        210        220        230        240 
RRSLDDAGFQ DTLIMSYAVK YASAFYAPFR GAVSSAPAFG DRRSYQMDPA NIDEALIEAE 

       250        260        270        280        290        300 
LDLREGADIL MVKPALAYLD VIGKVRERFS VPLAAYNVSG EYSMLKAAIK SGYLTDEAIY 

       310        320 
ESILSIKRAG ADLIISHFAP DLLGVI 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85248.1.
PIRE69199.
RefSeqNP_275887.1. NC_000916.1.

3D structure databases

ProteinModelPortalO26839.
SMRO26839. Positions 10-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH744.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85248; AAB85248; MTH_744.
GeneID1471152.
KEGGmth:MTH744.

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMAGEYAMVE.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-746-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_METTH
AccessionPrimary (citable) accession number: O26839
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: October 16, 2013
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