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

Q750E0 (HEM2_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. 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=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEM2
Ordered Locus Names:AGR015C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length340 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Delta-aminolevulinic acid dehydratase
PRO_0000140531

Sites

Active site2111Schiff-base intermediate with substrate By similarity
Active site2641Schiff-base intermediate with substrate By similarity
Metal binding1341Zinc; catalytic By similarity
Metal binding1361Zinc; catalytic By similarity
Metal binding1441Zinc; catalytic By similarity
Binding site2211Substrate 1 By similarity
Binding site2331Substrate 1 By similarity
Binding site2911Substrate 2 By similarity
Binding site3301Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q750E0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EA5FAB60A7562999

FASTA34037,331
        10         20         30         40         50         60 
MKHTAEFLDT HQTQISSILS GGYNHPLLRE WQNERQLAKN MFIFPLFVSD MPDEDQPIES 

        70         80         90        100        110        120 
LPNIRRFGVN KLAGYLKPLV AKGLRAVLLF GVPMKPNSKD EFGSAADDPE GPVIQAIKLL 

       130        140        150        160        170        180 
RAEFPELYIL CDVCLCEYTS HGHCGVLYDD GSINREQSVR RLAAVAVNYA KAGAHSVAPS 

       190        200        210        220        230        240 
DMIDGRIRDI KLGLLAAGLA HKTFVMSYAA KFSGNLYGPF RDAACSAPSQ GDRKCYQLPS 

       250        260        270        280        290        300 
GGRGLARRAL RRDLDEGADG IIVKPSTFYL DIMADASEIA KDVPICAYHV SGEYAMLHAA 

       310        320        330        340 
AKAGVVDFKS IAFESHQGFL RAGARLIISY MTPEFLDWLS 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54504.1.
RefSeqNP_986680.1. NM_211742.1.

3D structure databases

ProteinModelPortalQ750E0.
SMRQ750E0. Positions 3-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AGR015C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS54504; AAS54504; AGOS_AGR015C.
GeneID4622979.
KEGGago:AGOS_AGR015C.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMASGYFHPT.
OrthoDBEOG779P7W.

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_ASHGO
AccessionPrimary (citable) accession number: Q750E0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways