Delta-aminolevulinic acid dehydratase - Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)

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O42768 (HEM2_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Inferred 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 metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer By similarity.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	heme biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	lead ion binding Inferred from sequence or structural similarity. Source: UniProtKB porphobilinogen synthase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 340

340

Delta-aminolevulinic acid dehydratase

PRO_0000140532

Sites

Active site

210

Schiff-base intermediate with substrate By similarity

Active site

263

Schiff-base intermediate with substrate By similarity

Metal binding

133

Zinc; catalytic By similarity

Metal binding

135

Zinc; catalytic By similarity

Metal binding

143

Zinc; catalytic By similarity

Binding site

220

Substrate 1 By similarity

Binding site

232

Substrate 1 By similarity

Binding site

290

Substrate 2 By similarity

Binding site

329

Substrate 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O42768 [UniParc].

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

340

37,425

        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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A role for HEM2 in cadmium tolerance." Hunter T.C., Mehra R.K. J. Inorg. Biochem. 69:293-303(1998) [PubMed] [Europe PMC] [Abstract] 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. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF038566 Genomic DNA. Translation: AAB94926.1. CR380950 Genomic DNA. Translation: CAG58584.1.
RefSeq	XP_445673.1. XM_445673.1.
3D structure databases
ProteinModelPortal	O42768.
SMR	O42768. Positions 1-338.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2887248.
KEGG	cgr:CAGL0D06138g.
Phylogenomic databases
HOGENOM	HOG000020323.
KO	K01698.
OMA	AVMEAMT.
OrthoDB	EOG454D75.
Enzyme and pathway databases
UniPathway	UPA00251; UER00318.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
PANTHER	PTHR11458. PTHR11458. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_CANGA

Accession

Primary (citable) accession number: O42768

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents