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P0ACB2 (HEM2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Synonyms:ncf
Ordered Locus Names:b0369, JW0361
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Binds 1 zinc ion per monomer. Ref.9 Ref.10 Ref.11 Ref.12

Enzyme regulation

Allosteric enzyme. Stimulated by magnesium ions. Ref.9

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer. Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the ALADH family.

Sequence caution

The sequence AAB18092.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA12842.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 324323Delta-aminolevulinic acid dehydratase
PRO_0000140501

Sites

Active site1951Schiff-base intermediate with substrate Ref.11 Ref.12
Active site2471Schiff-base intermediate with substrate Ref.11 Ref.12
Metal binding1201Zinc; catalytic
Metal binding1221Zinc; catalytic
Metal binding1301Zinc; catalytic
Metal binding2321Magnesium
Binding site2051Substrate 1
Binding site2161Substrate 1
Binding site2731Substrate 2
Binding site3121Substrate 2

Experimental info

Mutagenesis1271H → A: No significant effect on activity; when associated with A-129. Ref.9
Mutagenesis1291H → A: No significant effect on activity; when associated with A-127. Ref.9
Sequence conflict18 – 192RA → PR in AAA62629. Ref.1
Sequence conflict19 – 4224AMFEE…EEEID → VCLKRQHLSLTTWCCRSLLK KKLT in CAA35467. Ref.2
Sequence conflict90 – 912SD → ER in AAA62629. Ref.1
Sequence conflict1041R → P in AAA62629. Ref.1
Sequence conflict2261R → P in CAA35467. Ref.2
Sequence conflict2271R → A in AAA62629. Ref.1
Sequence conflict2291A → G in AAA62629. Ref.1
Sequence conflict2311R → A in AAA62629. Ref.1
Sequence conflict2331S → Y in AAA62629. Ref.1
Sequence conflict2411A → P in AAA62629. Ref.1
Sequence conflict2541D → N in AAA62629. Ref.1

Secondary structure

............................................................... 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ACB2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CE814E5705BFD255

FASTA32435,625
        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 

« Hide

References

« Hide 'large scale' references
[1]"The structure of the Escherichia coli hemB gene."
Li J.-M., Russell C.S., Cosloy S.D.
Gene 75:177-184(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence of the hemB gene of Escherichia coli K12."
Echelard Y., Dymetryszyn J., Drolet M., Sasarman A.
Mol. Gen. Genet. 214:503-508(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]Sigurdsson E., Backman V.M., Eggertsson G.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]Nashimoto H., Saito N.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[5]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain."
Spencer P., Jordan P.M.
Biochem. J. 290:279-287(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 2-6; 96-135 AND 238-254.
[9]"The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis."
Mitchell L.W., Volin M., Jaffe E.K.
J. Biol. Chem. 270:24054-24059(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-127 AND HIS-129.
[10]"X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0-A resolution."
Erskine P.T., Norton E., Cooper J.B., Lambert R., Coker A., Lewis G., Spencer P., Sarwar M., Wood S.P., Warren M.J., Shoolingin-Jordan P.M.
Biochemistry 38:4266-4276(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH LEVULINIC ACID AND ZINC IONS, SUBUNIT, COFACTOR.
[11]"Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity."
Kervinen J., Jaffe E.K., Stauffer F., Neier R., Wlodawer A., Zdanov A.
Biochemistry 40:8227-8236(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH 4,7-DIOXOSEBACIC ACID; ZINC AND MAGNESIUM, ACTIVE SITE, SUBUNIT, COFACTOR.
[12]"Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid."
Jaffe E.K., Kervinen J., Martins J., Stauffer F., Neier R., Wlodawer A., Zdanov A.
J. Biol. Chem. 277:19792-19799(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH 4-OXOSEBACIC ACID; ZINC AND MAGNESIUM, ACTIVE SITE, SUBUNIT, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24488 Genomic DNA. Translation: AAA62629.1.
X17417 Genomic DNA. Translation: CAA35467.1.
L44595 Genomic DNA. Translation: AAB52499.1.
D85613 Genomic DNA. Translation: BAA12842.1. Different initiation.
U73857 Genomic DNA. Translation: AAB18092.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73472.2.
AP009048 Genomic DNA. Translation: BAE76150.1.
PIRSYECPF. A64765.
RefSeqNP_414903.4. NC_000913.3.
YP_488662.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4EX-ray2.00A2-324[»]
1I8JX-ray1.90A/B2-324[»]
1L6SX-ray1.70A/B2-324[»]
1L6YX-ray1.90A/B2-324[»]
ProteinModelPortalP0ACB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36209N.
IntActP0ACB2. 6 interactions.
MINTMINT-6765615.
STRING511145.b0369.

Chemistry

BindingDBP0ACB2.

2D gel databases

SWISS-2DPAGEP0ACB2.

Proteomic databases

PaxDbP0ACB2.
PRIDEP0ACB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73472; AAC73472; b0369.
BAE76150; BAE76150; BAE76150.
GeneID12932508.
945017.
KEGGecj:Y75_p0358.
eco:b0369.
PATRIC32115877. VBIEscCol129921_0380.

Organism-specific databases

EchoBASEEB0423.
EcoGeneEG10428. hemB.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAQMNPANR.
OrthoDBEOG6VXFCB.
PhylomeDBP0ACB2.

Enzyme and pathway databases

BioCycEcoCyc:PORPHOBILSYNTH-MONOMER.
ECOL316407:JW0361-MONOMER.
MetaCyc:PORPHOBILSYNTH-MONOMER.
UniPathwayUPA00251; UER00318.

Gene expression databases

GenevestigatorP0ACB2.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ACB2.
PROP0ACB2.

Entry information

Entry nameHEM2_ECOLI
AccessionPrimary (citable) accession number: P0ACB2
Secondary accession number(s): P15002, P78247, Q2MC56
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene