P64334 (HEM2_STAAN) 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:	SA1492

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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_0000140512
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)
	P64334 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: BF24378E01E7C93E	FASTA	324	36,583
	10 20 30 40 50 60 MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG VYQISLNLLE 70 80 90 100 110 120 SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA TRIAKKMYDD LLIVADTCLC 130 140 150 160 170 180 EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT AISQVEAGAD IIAPSNMMDG FVAEIRRGLD 190 200 210 220 230 240 EAGYYNIPIM SYGVKYASSF FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE 250 260 270 280 290 300 GCDMMIVKPA LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV 310 320 SMKRAGADMI ITYFAKDICR YLDK

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.

[2]

"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42759.1.
PIR	B89950.
RefSeq	NP_374780.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P64334.
SMR	P64334. Positions 5-318.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA1492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB42759; BAB42759; BAB42759.
GeneID	1124337.
KEGG	sau:SA1492.
PATRIC	19575284. VBIStaAur116463_1612.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0113.
HOGENOM	HOG000020323.
KO	K01698.
OMA	MIISYHA.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-1565-MONOMER.
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_STAAN

Accession

Primary (citable) accession number: P64334
Secondary accession number(s): Q99TJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program