Reviewed, UniProtKB/Swiss-Prot P0ACB3 (HEM2_SHIFL)

Names and origin

Protein names

Recommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
      Short name=ALAD
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase

Gene names

Name:	hemB
Ordered Locus Names:	SF0249, S0270

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O.
Cofactor	Binds 1 magnesium ion per monomer By similarity. 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	Porphyrin biosynthesis
Ligand	Magnesium Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 324	323	Delta-aminolevulinic acid dehydratase		PRO_0000140509
Sites
	Active site	195	1	By similarity
	Active site	247	1	By similarity
	Metal binding	120	1	Zinc; catalytic By similarity
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	130	1	Zinc; catalytic By similarity
	Metal binding	232	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0ACB3-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CE814E5705BFD255	FASTA	324	35,625
	10 20 30 40 50 60 MTDLIQRPRR LRKSPALRAM FEETTLSLND LVLPIFVEEE IDDYKAVEAM PGVMRIPEKH 70 80 90 100 110 120 LAREIERIAN AGIRSVMTFG ISHHTDETGS DAWREDGLVA RMSRICKQTV PEMIVMSDTC 130 140 150 160 170 180 FCEYTSHGHC GVLCEHGVDN DATLENLGKQ AVVAAAAGAD FIAPSAAMDG QVQAIRQALD 190 200 210 220 230 240 AAGFKDTAIM SYSTKFASSF YGPFREAAGS ALKGDRKSYQ MNPMNRREAI RESLLDEAQG 250 260 270 280 290 300 ADCLMVKPAG AYLDIVRELR ERTELPIGAY QVSGEYAMIK FAALAGAIDE EKVVLESLGS 310 320 IKRAGADLIF SYFALDLAEK KILR

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005674 Genomic DNA. Translation: AAN41910.1. Different initiation. AE014073 Genomic DNA. Translation: AAP15794.1. Different initiation.
RefSeq	NP_706203.1. NP_835989.1.
3D structure databases
SMR	P0ACB3. Positions 2-324.
ModBase	Search...
Genome annotation databases
GeneID	1024339. 1076701.
GenomeReviews	Gene locus SF0249 in contig AE005674_GR. Gene locus S0270 in contig AE014073_GR.
KEGG	sfl:SF0249. sfx:S0270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0ACB3.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN41910.1-MON.
BRENDA	4.2.1.24. 189495.
Family and domain databases
InterPro	IPR001731. 4pyrrol_synth_porphobiln_synth. IPR013785. Aldolase_TIM. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
ProDom	PD002304. AlaD_dehydratase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_SHIFL

Accession

Primary (citable) accession number: P0ACB3
Secondary accession number(s): P15002, P78247

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)