P46723 (HEM2_MYCLE) 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:	ML2419
ORF Names:	B2168_C3_264

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	329 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
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 – 329	329	Delta-aminolevulinic acid dehydratase		PRO_0000140504
Sites
	Active site	202	1	Schiff-base intermediate with substrate By similarity
	Active site	254	1	Schiff-base intermediate with substrate By similarity
	Metal binding	239	1	Magnesium By similarity
	Binding site	212	1	Substrate 1 By similarity
	Binding site	223	1	Substrate 1 By similarity
	Binding site	280	1	Substrate 2 By similarity
	Binding site	319	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46723 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 1E0EBA9498B8609C	FASTA	329	34,775
	10 20 30 40 50 60 MSVSGYPRHR PRRLRSTPAM RRLVAQTSLE PRNLVLPMFV ADGIDELRPI ASMPGVVQHT 70 80 90 100 110 120 RDSLRRAAVA AVDAGVGGLN LFGVPRDQDK DATGSAGVDP DGILNVALRD LAEDLGDATV 130 140 150 160 170 180 LMADTCLDEF TDHGHCGVLD GQGRVDNDAT VARYVELAVA QAESGANVVG PSGMMDGQIG 190 200 210 220 230 240 ALRDGLDSAG YADVAILAYA AKFSSAFYGP FREAVSCSLS GDRRTYQQEP GNAREALREI 250 260 270 280 290 300 KLDLDEGADI IMIKPASGYL DVVATAAGVS PVPVAAYQVS GEYAMICAAA ANNWIDERAA 310 320 VLESLTSIRR AGADIVFTYW AADVACWLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00018 Genomic DNA. Translation: AAA17246.1. AL583925 Genomic DNA. Translation: CAC31935.1.
PIR	S72910.
RefSeq	NP_302564.1. NC_002677.1.
3D structure databases
ProteinModelPortal	P46723.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000029189; EBMYCP00000028795; EBMYCG00000029184.
GeneID	908581.
GenomeReviews	Gene locus ML2419 in contig AL450380_GR.
KEGG	mle:ML2419.
NMPDR	fig|272631.1.peg.1436.
PATRIC	18059483. VBIMycLep78757_4656.
Organism-specific databases
Leproma	ML2419.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016458.
HOGENOM	HBG285270.
OMA	ADLCFCE.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	MLEP272631:ML2419-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_MYCLE

Accession

Primary (citable) accession number: P46723

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
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