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

Q60178 (HEM2_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MJ0643
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length335 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 – 335335Delta-aminolevulinic acid dehydratase
PRO_0000140523

Sites

Active site2041Schiff-base intermediate with substrate By similarity
Active site2571Schiff-base intermediate with substrate By similarity
Metal binding1291Zinc; catalytic By similarity
Metal binding1311Zinc; catalytic By similarity
Metal binding1391Zinc; catalytic By similarity
Metal binding2421Magnesium By similarity
Binding site2141Substrate 1 By similarity
Binding site2261Substrate 1 By similarity
Binding site2831Substrate 2 By similarity
Binding site3221Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60178 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4D097DAB45F3705D

FASTA33537,396
        10         20         30         40         50         60 
MFKINLGDFM LIRPRRLRKN QKIRDLVRET ILTKNDLIMP IFVDENLKGN EKKEISSMPN 

        70         80         90        100        110        120 
QYRFSVEGAI EEAKEIADLG IPAVILFGIP KHKDEIASSA YDKNGVVQRT IRGIKEELGD 

       130        140        150        160        170        180 
ELLVIADCCL CEYTSHGHCG IVKDGKILND ATLPILAKIA LSYADAGVDI VAPSDMMDGR 

       190        200        210        220        230        240 
VRAIREILEE NGYDDVAIMS YSAKYASSFY GPFREAAESA PKFGDRKSYQ MDIGNAREAL 

       250        260        270        280        290        300 
KEIALDIEEG ADLILVKPAL PYLDIIRMAK DRFDVPIGGY CVSGEYAMVE AAARNGWLDR 

       310        320        330 
EKVIYEILLS IKRAGADFII TYWAKEVAEI GLSQE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98637.1.
PIRC64380.
RefSeqNP_247627.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ60178.
SMRQ60178. Positions 11-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0643.

Proteomic databases

PRIDEQ60178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98637; AAB98637; MJ_0643.
GeneID1451509.
KEGGmja:MJ_0643.

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMAGEYAMVE.
ProtClustDBPRK09283.

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]
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_METJA
AccessionPrimary (citable) accession number: Q60178
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 16, 2013
This is version 86 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names