P45622 (HEM2_BRAJA) 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:	blr5037

Organism

Bradyrhizobium japonicum (strain USDA 110) [Reference proteome] [HAMAP]

Taxonomic identifier

224911 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium › Bradyrhizobium japonicum

Protein attributes

Sequence length	353 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. Required for nodule development. Ref.1
Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.1
Cofactor	Magnesium. Ref.1
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.
Sequence caution	The sequence BAC50302.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Ligand	Magnesium Metal-binding
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 – 353	353	Delta-aminolevulinic acid dehydratase		PRO_0000140494
Sites
	Active site	221	1	Schiff-base intermediate with substrate By similarity
	Active site	275	1	Schiff-base intermediate with substrate By similarity
	Metal binding	260	1	Magnesium By similarity
	Binding site	231	1	Substrate 1 By similarity
	Binding site	244	1	Substrate 1 By similarity
	Binding site	301	1	Substrate 2 By similarity
	Binding site	340	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45622 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: F143FA4892ACF1F8	FASTA	353	38,582
	10 20 30 40 50 60 MAIKYGRPIE LREVSRRDGA AASPALDLAI RPRRNRKAEW ARRMVRENVL TTDDLIWPLF 70 80 90 100 110 120 LIDGNNKREQ IASMPGVERL SVDQAVREAE RAMKLTIPCI ALFPYTDPSL RDEEGSEACN 130 140 150 160 170 180 PNNLVCQAVR AIKKEFPEIG VLCDVALDPF TSHGHDGLIA DGAILNDETV AVLVRQALVQ 190 200 210 220 230 240 AEAGCDIIAP SDMMDGRVAA IREGLDQAGL IDVQIMAYAA KYASAFYGPF RDAIGSAKTL 250 260 270 280 290 300 TGDKRTYQMD SANTDEALRE VELDISEGAD MVMVKPGMPY LDVVRRVKDT FAMPTFAYQV 310 320 330 340 350 SGEYAMIAAA AGNGWLDGDR AMMESLLAFK RAGADGVLSY FAPKAAEKLR TQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain." Chauhan S., O'Brian M.R. J. Bacteriol. 175:7222-7227(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR. Strain: I110.
[2]	"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L24386 Genomic DNA. Translation: AAA89067.1. BA000040 Genomic DNA. Translation: BAC50302.1. Different initiation.
PIR	A49925.
RefSeq	NP_771677.2. NC_004463.1.
3D structure databases
ProteinModelPortal	P45622.
SMR	P45622. Positions 31-350.
ModBase	Search...
Protein-protein interaction databases
STRING	224911.blr5037.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC50302; BAC50302; BAC50302.
GeneID	1051848.
KEGG	bja:blr5037.
PATRIC	21193740. VBIBraJap65052_5115.
Phylogenomic databases
eggNOG	COG0113.
HOGENOM	HOG000020323.
KO	K01698.
OMA	DVAIMSY.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	BJAP224911:GJEJ-5074-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_BRAJA

Accession

Primary (citable) accession number: P45622

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program