Q8CNZ0 (HEM2_STAES) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-aminolevulinic acid dehydratase
Short name=ALAD
Short name=ALADH
EC=4.2.1.24

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	hemB
Ordered Locus Names:	SE_1343

Organism

Staphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]

Taxonomic identifier

176280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus epidermidis

Protein attributes

Sequence length	324 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	Magnesium Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 324	324	Delta-aminolevulinic acid dehydratase		PRO_0000140517
Sites
	Active site	195	1	Schiff-base intermediate with substrate By similarity
	Active site	248	1	Schiff-base intermediate with substrate By similarity
	Metal binding	118	1	Zinc; catalytic By similarity
	Metal binding	120	1	Zinc; catalytic By similarity
	Metal binding	128	1	Zinc; catalytic By similarity
	Metal binding	233	1	Magnesium By similarity
	Binding site	205	1	Substrate 1 By similarity
	Binding site	217	1	Substrate 1 By similarity
	Binding site	274	1	Substrate 2 By similarity
	Binding site	313	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CNZ0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 31685329B5943A51	FASTA	324	36,570
	10 20 30 40 50 60 MKFDRHRRLR SSKTMRDLVR ETHVRKEDLI YPIFVVEQDD IKSEIKSLPG IYQISLNLLH 70 80 90 100 110 120 EEIKEAYDLG IRAIMFFGVP NDKDDIGSGA YDHNGVVQEA TRISKNLYKD LLIVADTCLC 130 140 150 160 170 180 EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT AISQVEAGAD IIAPSNMMDG FVAEIREGLD 190 200 210 220 230 240 QAGYQNIPIM SYGIKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE 250 260 270 280 290 300 GCDMMIVKPS LSYLDIIRDV KNNTNVPVVA YNVSGEYSMT KAAALNGWID EEKIVMEQMI 310 320 SMKRAGADLI ITYFAKDICR YLDK

References

[1]

"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015929 Genomic DNA. Translation: AAO04942.1.
RefSeq	NP_764898.1. NC_004461.1.
3D structure databases
ProteinModelPortal	Q8CNZ0.
ModBase	Search...
Protein-protein interaction databases
STRING	176280.SE1343.
Proteomic databases
PRIDE	Q8CNZ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO04942; AAO04942; SE_1343.
GeneID	1056288.
KEGG	sep:SE1343.
PATRIC	19608478. VBIStaEpi113981_1312.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0113.
KO	K01698.
OMA	MIISYHA.
ProtClustDB	PRK09283.
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_STAES

Accession

Primary (citable) accession number: Q8CNZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program