P43087 (HEM2_SYNE7) 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:	Synpcc7942_1792

Organism

Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]

Taxonomic identifier

1140 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus › Synechococcus elongatus

Protein attributes

Sequence length	326 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 – 326	326	Delta-aminolevulinic acid dehydratase		PRO_0000140520
Sites
	Active site	198	1	Schiff-base intermediate with substrate By similarity
	Active site	251	1	Schiff-base intermediate with substrate By similarity
	Metal binding	119	1	Zinc; catalytic By similarity
	Metal binding	121	1	Zinc; catalytic By similarity
	Metal binding	129	1	Zinc; catalytic By similarity
	Metal binding	236	1	Magnesium By similarity
	Binding site	208	1	Substrate 1 By similarity
	Binding site	220	1	Substrate 1 By similarity
	Binding site	277	1	Substrate 2 By similarity
	Binding site	316	1	Substrate 2 By similarity
Experimental info
	Sequence conflict	287	1	A → R in CAA49892. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P43087 [UniParc]. Last modified April 18, 2006. Version 2. Checksum: 0C4F44658CEB37BF	FASTA	326	35,574
	10 20 30 40 50 60 MFPTHRPRRL RSSETLRRMV RETTLTSADF IYPLFAVPGE GVAKEVTSMP GVYQLSIDKI 70 80 90 100 110 120 VEEAKEVYDL GIPSIILFGI PTDKDNDATG AWHDCGIVQK AATAVKEAVP ELIVAADTCL 130 140 150 160 170 180 CEYTPHGHCG YLEVGDLSGR VLNDPTLELL RKTAVSQAKA GADIIAPSGM MDGFVATIRD 190 200 210 220 230 240 ALDEAGFSDT PIMAYSAKYA SAYYGPFRDA AESTPQFGDR RTYQMDPGNS REALKEVELD 250 260 270 280 290 300 VAEGADIVMV KPALSYMDII CRIKETTDLP VAAYNVSGEY SMVKAAALNG WIDEERVVLE 310 320 TLTSFKRAGA DLILTYHAKD AARWLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterisation of genes for tetrapyrrole biosynthesis from the cyanobacterium Anacystis nidulans R2." Jones M.C., Jenkins J.M., Smith A.G., Howe C.J. Plant Mol. Biol. 24:435-448(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7942.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70434 Genomic DNA. Translation: CAA49892.1. CP000100 Genomic DNA. Translation: ABB57822.1.
RefSeq	YP_400809.1. NC_007604.1.
3D structure databases
ProteinModelPortal	P43087.
SMR	P43087. Positions 5-326.
ModBase	Search...
Protein-protein interaction databases
STRING	1140.Synpcc7942_1792.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB57822; ABB57822; Synpcc7942_1792.
GeneID	3774367.
KEGG	syf:Synpcc7942_1792.
PATRIC	23789009. VBISynElo51371_2028.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0113.
HOGENOM	HOG000020323.
KO	K01698.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	SELO1140:GJWQ-1820-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_SYNE7

Accession

Primary (citable) accession number: P43087
Secondary accession number(s): Q31M97

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 18, 2006
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program