O33357 (HEM2_MYCTU) 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:	Rv0512, MT0533
ORF Names:	MTCY20G10.02

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

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 Reference 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_0000140505
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)
	O33357 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F3E59A9639AB544A	FASTA	329	34,871
	10 20 30 40 50 60 MSMSSYPRQR PRRLRSTVAM RRLVAQTSLE PRHLVLPMFV ADGIDEPRPI TSMPGVVQHT 70 80 90 100 110 120 RDSLRRAAAA AVAAGVGGLM LFGVPRDQDK DGVGSAGIDP DGILNVALRD LAKDLGEATV 130 140 150 160 170 180 LMADTCLDEF TDHGHCGVLD DRGRVDNDAT VARYVELAVA QAESGAHVVG PSGMMDGQVA 190 200 210 220 230 240 AIRDGLDAAG YIDVVILAYA AKFASAFYGP FREAVSSSLS GDRRTYQQEP GNAAEALREI 250 260 270 280 290 300 ELDLDEGADI VMVKPAMGYL DVVAAAADVS PVPVAAYQVS GEYAMIRAAA ANNWIDERAA 310 320 VLESLTGIRR AGADIVLTYW AVDAAGWLT

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842573 Genomic DNA. Translation: CAB10749.1. AE000516 Genomic DNA. Translation: AAK44756.1.
PIR	E70509.
RefSeq	NP_215026.1. NC_000962.2. NP_334942.1. NC_002755.2.
3D structure databases
ProteinModelPortal	O33357.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000001282; EBMYCP00000001282; EBMYCG00000001282. EBMYCT00000072421; EBMYCP00000070480; EBMYCG00000072416.
GeneID	887312. 924242.
GenomeReviews	Gene locus MT0533 in contig AE000516_GR. Gene locus Rv0512 in contig AL123456_GR.
KEGG	mtc:MT0533. mtu:Rv0512.
PATRIC	18122882. VBIMycTub22151_0575.
TIGR	MT0533.
Organism-specific databases
TubercuList	Rv0512.
Phylogenomic databases
GeneTree	EBGT00050000016458.
HOGENOM	HBG285270.
OMA	ADLCFCE.
PhylomeDB	O33357.
ProtClustDB	PRK09283.
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_MYCTU

Accession

Primary (citable) accession number: O33357

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program