Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Delta-aminolevulinic acid dehydratase

Gene

HEM2

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (HEM2)
  2. Porphobilinogen deaminase (HEM3)
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (CAGL0H08371g)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi133Zinc; catalyticBy similarity1
Metal bindingi135Zinc; catalyticBy similarity1
Metal bindingi143Zinc; catalyticBy similarity1
Active sitei210Schiff-base intermediate with substrateBy similarity1
Binding sitei220Substrate 1By similarity1
Binding sitei232Substrate 1By similarity1
Active sitei263Schiff-base intermediate with substrateBy similarity1
Binding sitei290Substrate 2By similarity1
Binding sitei329Substrate 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEM2
Ordered Locus Names:CAGL0D06138g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome D

Organism-specific databases

CGDiCAL0128021. HEM2.
EuPathDBiFungiDB:CAGL0D06138g.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001405321 – 340Delta-aminolevulinic acid dehydrataseAdd BLAST340

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi284593.XP_445673.1.

Structurei

3D structure databases

ProteinModelPortaliO42768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiKOG2794. Eukaryota.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiO42768.
KOiK01698.
OMAiQFLDWLD.
OrthoDBiEOG092C32OH.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42768-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHTADFLDIE PTEISSILSG GYNHPLLREW QSERQLKKNM LIFPLFISDI
60 70 80 90 100
PDEATPIDSL PNIKRFGINK LVDYVKPLVE KGLRSVILFG VPLKEGTKDP
110 120 130 140 150
VGTAADDPEG PVIQAIKLLR KEFPELYIIC DVCLCEYTSH GHCGVLYDDG
160 170 180 190 200
TINRERSVSR IAAVAVNYAK AGAHCVAPSD MIDGRIKDIK KGLISAGLAH
210 220 230 240 250
KTFVLSYAAK FSGNLYGPFR DAACSSPSNG DRKCYQLPQA GRGLARRALA
260 270 280 290 300
RDKNEGADGI IVKPSTFYLD IMRDASEICE DLPICAYHVS GEYAMLHAAA
310 320 330 340
EKGIVDLKSI AFESHEGFLR AGARLIISYF TPEFLDWLSN
Length:340
Mass (Da):37,425
Last modified:June 1, 1998 - v1
Checksum:iE5819CE183FF83E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038566 Genomic DNA. Translation: AAB94926.1.
CR380950 Genomic DNA. Translation: CAG58584.1.
RefSeqiXP_445673.1. XM_445673.1.

Genome annotation databases

EnsemblFungiiCAG58584; CAG58584; CAGL0D06138g.
GeneIDi2887248.
KEGGicgr:CAGL0D06138g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038566 Genomic DNA. Translation: AAB94926.1.
CR380950 Genomic DNA. Translation: CAG58584.1.
RefSeqiXP_445673.1. XM_445673.1.

3D structure databases

ProteinModelPortaliO42768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284593.XP_445673.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG58584; CAG58584; CAGL0D06138g.
GeneIDi2887248.
KEGGicgr:CAGL0D06138g.

Organism-specific databases

CGDiCAL0128021. HEM2.
EuPathDBiFungiDB:CAGL0D06138g.

Phylogenomic databases

eggNOGiKOG2794. Eukaryota.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiO42768.
KOiK01698.
OMAiQFLDWLD.
OrthoDBiEOG092C32OH.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM2_CANGA
AccessioniPrimary (citable) accession number: O42768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: October 5, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.