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O42768 (HEM2_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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:CAGL0D06138g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

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_0000140532

Sites

Active site2101Schiff-base intermediate with substrate By similarity
Active site2631Schiff-base intermediate with substrate By similarity
Metal binding1331Zinc; catalytic By similarity
Metal binding1351Zinc; catalytic By similarity
Metal binding1431Zinc; catalytic By similarity
Binding site2201Substrate 1 By similarity
Binding site2321Substrate 1 By similarity
Binding site2901Substrate 2 By similarity
Binding site3291Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O42768 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E5819CE183FF83E5

FASTA34037,425
        10         20         30         40         50         60 
MHTADFLDIE PTEISSILSG GYNHPLLREW QSERQLKKNM LIFPLFISDI PDEATPIDSL 

        70         80         90        100        110        120 
PNIKRFGINK LVDYVKPLVE KGLRSVILFG VPLKEGTKDP VGTAADDPEG PVIQAIKLLR 

       130        140        150        160        170        180 
KEFPELYIIC DVCLCEYTSH GHCGVLYDDG TINRERSVSR IAAVAVNYAK AGAHCVAPSD 

       190        200        210        220        230        240 
MIDGRIKDIK KGLISAGLAH KTFVLSYAAK FSGNLYGPFR DAACSSPSNG DRKCYQLPQA 

       250        260        270        280        290        300 
GRGLARRALA RDKNEGADGI IVKPSTFYLD IMRDASEICE DLPICAYHVS GEYAMLHAAA 

       310        320        330        340 
EKGIVDLKSI AFESHEGFLR AGARLIISYF TPEFLDWLSN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038566 Genomic DNA. Translation: AAB94926.1.
CR380950 Genomic DNA. Translation: CAG58584.1.
RefSeqXP_445673.1. XM_445673.1.

3D structure databases

ProteinModelPortalO42768.
SMRO42768. Positions 1-338.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2887248.
KEGGcgr:CAGL0D06138g.

Phylogenomic databases

HOGENOMHOG000020323.
KOK01698.
OMAVSRAMSY.
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_CANGA
AccessionPrimary (citable) accession number: O42768
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: May 14, 2014
This is version 91 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