HEM2 porphobilinogen synthase HEM2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: HEM2
Gene description: porphobilinogen synthase HEM2
Primary source: FungiDB:YGL040C
Locus tag: YGL040C
See related: SGD:S000003008; AllianceGenome:SGD:S000003008; VEuPathDB:YGL040C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: OLE4; SLU1
Summary: Enables porphobilinogen synthase activity and zinc ion binding activity. Involved in heme biosynthetic process. Located in cytoplasm and nucleus. Human ortholog(s) of this gene implicated in porphyria cutanea tarda and sickle cell anemia. Orthologous to human ALAD (aminolevulinate dehydratase). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See HEM2 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (419527..420555, complement)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables porphobilinogen synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables porphobilinogen synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables porphobilinogen synthase activity	IEA Inferred from Electronic Annotation more info
enables porphobilinogen synthase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables zinc ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in heme biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in heme biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in heme biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protoporphyrinogen IX biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in tetrapyrrole biosynthetic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	HDA more info	PubMed

General protein information

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Preferred Names: porphobilinogen synthase HEM2

NP_011475.1

EC 4.2.1.24

Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001139.9 Reference assembly

Range

419527..420555 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180905.1 → NP_011475.1 TPA: porphobilinogen synthase HEM2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011475.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VU99, P05373

UniProtKB/TrEMBL

A0A6A5PVL1, A6ZUV5, B3LIQ1, C7GS20, C8Z8K3, G2WE55, N1P5J0

Conserved Domains (1) summary

cd04824
Location:20 → 338

eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...