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O42768

- HEM2_CANGA

UniProt

O42768 - HEM2_CANGA

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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: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Zinc; catalyticBy similarity
Metal bindingi135 – 1351Zinc; catalyticBy similarity
Metal bindingi143 – 1431Zinc; catalyticBy similarity
Active sitei210 – 2101Schiff-base intermediate with substrateBy similarity
Binding sitei220 – 2201Substrate 1By similarity
Binding sitei232 – 2321Substrate 1By similarity
Active sitei263 – 2631Schiff-base intermediate with substrateBy similarity
Binding sitei290 – 2901Substrate 2By similarity
Binding sitei329 – 3291Substrate 2By similarity

GO - Molecular functioni

  1. lead ion binding Source: UniProtKB
  2. porphobilinogen synthase activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. heme biosynthetic process Source: UniProtKB
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
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
ProteomesiUP000002428: Chromosome D

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Delta-aminolevulinic acid dehydratasePRO_0000140532Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO42768.
SMRiO42768. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

HOGENOMiHOG000020323.
InParanoidiO42768.
KOiK01698.
OMAiVSRAMSY.
OrthoDBiEOG779P7W.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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

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 .
RefSeqi XP_445673.1. XM_445673.1.

3D structure databases

ProteinModelPortali O42768.
SMRi O42768. Positions 1-338.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2887248.
KEGGi cgr:CAGL0D06138g.

Phylogenomic databases

HOGENOMi HOG000020323.
InParanoidi O42768.
KOi K01698.
OMAi VSRAMSY.
OrthoDBi EOG779P7W.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 2001-L5.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

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: November 26, 2014
This is version 94 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

External Data

Dasty 3