Reviewed, UniProtKB/Swiss-Prot O42768 (HEM2_CANGA)

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 (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O.
Cofactor	Zinc.
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 electronic annotation. Source: UniProtKB-KW
Molecular function	porphobilinogen synthase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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	263	1	By similarity
	Metal binding	133	1	Zinc; catalytic By similarity
	Metal binding	135	1	Zinc; catalytic By similarity
	Metal binding	143	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O42768-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E5819CE183FF83E5	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

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: 9654753] [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. , 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: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF038566 Genomic DNA. Translation: AAB94926.1. CR380950 Genomic DNA. Translation: CAG58584.1.
RefSeq	XP_445673.1.
3D structure databases
HSSP	HSSP built from PDB template 1QNV based on UniProtKB P05373.
SMR	O42768. Positions 1-338.
ModBase	Search...
Protein-protein interaction databases
STRING	O42768.
Genome annotation databases
GeneID	2887248.
GenomeReviews	Gene locus CAGL0D06138g in contig CR380950_GR.
KEGG	cgr:CAGL0D06138g.
Phylogenomic databases
HOGENOM	O42768.
OMA	AESTPQF.
Enzyme and pathway databases
BRENDA	4.2.1.24. 189220.
Family and domain databases
InterPro	IPR001731. 4pyrrol_synth_porphobiln_synth. IPR013785. Aldolase_TIM. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
ProDom	PD002304. AlaD_dehydratase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)