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Reviewed, UniProtKB/Swiss-Prot Q02250 (HEM2_METSC)

Last modified June 16, 2009. Version 49. 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
Synonyms: alaDH
OrganismMethanothermus sociabilis
Taxonomic identifier2181 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Zinc.

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 processPorphyrin biosynthesis
   LigandZinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological processporphyrin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionporphobilinogen synthase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Delta-aminolevulinic acid dehydratase
PRO_0000140524

Regions

Region116 – 13419Zinc-binding By similarity

Sites

Active site2471 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02250-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 16F13425105F38D0

FASTA32035,925
        10         20         30         40         50         60 
MKFPYTRMRR LRKNSKIRSL VKETTLSKDD LIYPVFVKEG IKTKEKIPKM PGQYRYSVDE 

        70         80         90        100        110        120 
LIDEAKKLEE KGLKAILVFG IPKKKDKYGS SAYDPNGIVQ KSVKLLKEET DLVVITDVCL 

       130        140        150        160        170        180 
CQYTEHGHCG IVKNKKIVND ETLKYLSKVA LSHAEAGADV VAPSDMMDGR VKAIREELEK 

       190        200        210        220        230        240 
NGFDDVIIMS YSAKYASSFY EPFRSAVYSS PAFGDRSTYQ MDPPNSLEAL REVKLDIDEG 

       250        260        270        280        290        300 
ADIVMVKPAL PYLDIIRLVK DTFGVPTAAY NVSGEYSMIK AAIDANYLSN KVIIETLLSI 

       310        320 
KRAGADLIIT HFAPEIVEEI 

« Hide

References

[1]"Sequence of the 5-aminolevulinic acid dehydratase-encoding gene from the hyperthermophilic methanogen, Methanothermus sociabilis."
Broeckl G., Berchtold M., Behr M., Koenig H.
Gene 119:151-152(1992) [PubMed: 1398086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

M90083 Genomic DNA. Translation: AAA73226.1.
PIRJC1286.

3D structure databases

HSSPHSSP built from PDB template 1E51 based on UniProtKB P13716.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.2.1.24. 2716.

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_METSC
AccessionPrimary (citable) accession number: Q02250
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 49 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