P56074 (HEM2_HELPY) 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:	HP_0163

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	323 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 Reference 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 – 323	323	Delta-aminolevulinic acid dehydratase		PRO_0000140502
Sites
	Active site	193	1	Schiff-base intermediate with substrate By similarity
	Active site	246	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	231	1	Magnesium By similarity
	Binding site	203	1	Substrate 1 By similarity
	Binding site	215	1	Substrate 1 By similarity
	Binding site	272	1	Substrate 2 By similarity
	Binding site	311	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56074 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: ADB784A450856CA2	FASTA	323	36,203
	10 20 30 40 50 60 MFKRLRRLRS SENLRAMLRE TRLNIDDFIA PLFVIESDSC IKNEISSMPG VYQMSMEPLL 70 80 90 100 110 120 KECEELVGLG VKAVLLFGIP KHKDATGSHA LNKDHIVAKA AKEIKKRFKD LIVIADLCFC 130 140 150 160 170 180 EYTDHGHCGI LENASVSNDK TLEILNLQGL ILAESGVDIL APSNMMDGNV LSLRKTLDNA 190 200 210 220 230 240 GYTHTPIMSY STKFASSYYG PFRDVANSAP SFGDRKSYQM DYANQKEALL ESLEDEKQGA 250 260 270 280 290 300 DILMVKPALA YLDIVKEIRD HTLLPLALYN VSGEYAMLKL AQKHNLINYE SVLLETMTCF 310 320 KRAGADMIIS YHAKEVANLL QRN

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD07232.1.
PIR	C64540.
RefSeq	NP_206962.1. NC_000915.1. YP_006934086.1. NC_018939.1.
3D structure databases
ProteinModelPortal	P56074.
SMR	P56074. Positions 1-318.
ModBase	Search...
Protein-protein interaction databases
STRING	85962.HP0163.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD07232; AAD07232; HP_0163.
GeneID	13869342. 899142.
KEGG	heo:C694_00810. hpy:HP0163.
PATRIC	20591547. VBIHelPyl33062_0173.
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_HELPY

Accession

Primary (citable) accession number: P56074

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program