Q9ZMR8 (HEM2_HELPJ) 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:	jhp_0150

Organism

Helicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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_0000140503
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)
	Q9ZMR8 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 06938C45FE367F12	FASTA	323	36,251
	10 20 30 40 50 60 MFKRLRRLRS SENLRAMVRE TRLNINDFIA PLFVIESDSG IKNEISSMPG VYQMSIEPLL 70 80 90 100 110 120 KECEELVGLG IKAVLLFGIP KHKDATGSHA LNKDHIVAKA TREIKKRFKD LIVIADLCFC 130 140 150 160 170 180 EYTDHGHCGI LENASVSNDK TLKILNLQGL ILAESGVDIL APSNMMDGNV LSLRKALDKA 190 200 210 220 230 240 GYFHTPIMSY STKFASSYYG PFRDVANSPP SFGDRKSYQM DYANQKEALL ESLEDEKQGA 250 260 270 280 290 300 DILMVKPALA YLDIVKEIRD HTLLPLALYN VSGEYAMLKL AQKHNLINYE SVLLETMTCF 310 320 KRAGADMIIS YHAKEVANLL QRN

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J99.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001439 Genomic DNA. Translation: AAD05731.1.
PIR	H71968.
RefSeq	NP_222871.1. NC_000921.1.
3D structure databases
ProteinModelPortal	Q9ZMR8.
SMR	Q9ZMR8. Positions 1-318.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ZMR8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	889168.
GenomeReviews	Gene locus jhp_0150 in contig AE001439_GR.
KEGG	hpj:jhp0150.
NMPDR	fig|85963.1.peg.149.
PATRIC	20604918. VBIHelPyl98156_0171.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0113.
HOGENOM	HBG285270.
OMA	ADLCFCE.
PhylomeDB	Q9ZMR8.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	HPYL85963:JHP0150-MONOMER.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
PANTHER	PTHR11458. AlaD_dehydratase. 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_HELPJ

Accession

Primary (citable) accession number: Q9ZMR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program