P54919 (HEM2_STRCO) 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:	SCO3311
ORF Names:	SCE68.09c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	330 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.
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
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 – 330	330	Delta-aminolevulinic acid dehydratase		PRO_0000140519
Sites
	Active site	203	1	Schiff-base intermediate with substrate By similarity
	Active site	255	1	Schiff-base intermediate with substrate By similarity
	Metal binding	240	1	Magnesium By similarity
	Binding site	213	1	Substrate 1 By similarity
	Binding site	224	1	Substrate 1 By similarity
	Binding site	281	1	Substrate 2 By similarity
	Binding site	320	1	Substrate 2 By similarity
Experimental info
	Sequence conflict	100	1	D → V in AAA61398. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54919 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: D2AF1F8B971F30F5	FASTA	330	35,453
	10 20 30 40 50 60 MTTYGSFPGA RPRRLRTTPV MRRMVAETRL HPADFILPAF VREGVSEPVP IAAMPGVVQH 70 80 90 100 110 120 TRDTLKKAAA EAVEAGVSGI MLFGVPEDGK KDAAGTAGTD PDGILQVALR DVRAEVGDEL 130 140 150 160 170 180 LVMSDLCLDE FTDHGHCGVL DGQGRVDNDA TLERYAEMAQ VQADAGAHVV GPSGMMDGQI 190 200 210 220 230 240 GVIRDALDQI GREDVAILAY TAKYASAFYG PFREAVGSSL KGDRKTYQQD SANARESLRE 250 260 270 280 290 300 LALDLEEGAD MVMVKPAGPY LDILAKVAEA SDVPVAAYQI SGEYSMIEAA AEKGWIDRDR 310 320 330 AILESLTGIK RAGARNILTY WATEVARTLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterisation of the genes that encode enzymes for first steps of tetrapyrrole biosynthesis in Streptomyces coelicolor A3(2)." Petricek M. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A3(2) / NRRL B-16638.
[2]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19249 Genomic DNA. Translation: AAA61398.1. AL939116 Genomic DNA. Translation: CAB45345.1.
PIR	T36259.
RefSeq	NP_627521.1. NC_003888.3.
3D structure databases
ProteinModelPortal	P54919.
ModBase	Search...
Protein-protein interaction databases
STRING	100226.SCO3311.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB45345; CAB45345; CAB45345.
GeneID	1098745.
KEGG	sco:SCO3311.
PATRIC	23736366. VBIStrCoe124346_3371.
Phylogenomic databases
eggNOG	COG0113.
HOGENOM	HOG000020323.
KO	K01698.
OMA	DVAIMSY.
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_STRCO

Accession

Primary (citable) accession number: P54919
Secondary accession number(s): Q9S2E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program