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P0ACB2

- HEM2_ECOLI

UniProt

P0ACB2 - HEM2_ECOLI

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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+4 PublicationsNote: Binds 1 zinc ion per monomer.4 Publications

Enzyme regulationi

Allosteric enzyme. Stimulated by magnesium ions.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Zinc; catalytic2 Publications
Metal bindingi122 – 1221Zinc; catalytic2 Publications
Metal bindingi130 – 1301Zinc; catalytic2 Publications
Active sitei195 – 1951Schiff-base intermediate with substrate
Binding sitei205 – 2051Substrate 1
Binding sitei216 – 2161Substrate 1
Metal bindingi232 – 2321Magnesium2 Publications
Active sitei247 – 2471Schiff-base intermediate with substrate
Binding sitei273 – 2731Substrate 2
Binding sitei312 – 3121Substrate 2

GO - Molecular functioni

  1. metal ion binding Source: EcoCyc
  2. porphobilinogen synthase activity Source: EcoCyc
  3. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. heme biosynthetic process Source: EcoliWiki
  2. protoporphyrinogen IX biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:PORPHOBILSYNTH-MONOMER.
ECOL316407:JW0361-MONOMER.
MetaCyc:PORPHOBILSYNTH-MONOMER.
UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
Synonyms:ncf
Ordered Locus Names:b0369, JW0361
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10428. hemB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271H → A: No significant effect on activity; when associated with A-129. 1 Publication
Mutagenesisi129 – 1291H → A: No significant effect on activity; when associated with A-127. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 324323Delta-aminolevulinic acid dehydratasePRO_0000140501Add
BLAST

Proteomic databases

PaxDbiP0ACB2.
PRIDEiP0ACB2.

2D gel databases

SWISS-2DPAGEP0ACB2.

Expressioni

Gene expression databases

GenevestigatoriP0ACB2.

Interactioni

Subunit structurei

Homooctamer.3 Publications

Protein-protein interaction databases

DIPiDIP-36209N.
IntActiP0ACB2. 6 interactions.
MINTiMINT-6765615.
STRINGi511145.b0369.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 125Combined sources
Helixi15 – 217Combined sources
Helixi28 – 303Combined sources
Beta strandi31 – 388Combined sources
Beta strandi48 – 503Combined sources
Beta strandi54 – 574Combined sources
Helixi58 – 603Combined sources
Helixi61 – 7010Combined sources
Beta strandi75 – 817Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 934Combined sources
Helixi98 – 10912Combined sources
Beta strandi113 – 1197Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi135 – 1384Combined sources
Helixi140 – 15718Combined sources
Beta strandi160 – 1645Combined sources
Helixi171 – 18111Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi194 – 1963Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 2087Combined sources
Turni217 – 2193Combined sources
Helixi226 – 23813Combined sources
Beta strandi242 – 2487Combined sources
Helixi250 – 2523Combined sources
Helixi253 – 2608Combined sources
Beta strandi267 – 2715Combined sources
Helixi273 – 28412Combined sources
Helixi290 – 30314Combined sources
Beta strandi307 – 3115Combined sources
Helixi314 – 3196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4EX-ray2.00A2-324[»]
1I8JX-ray1.90A/B2-324[»]
1L6SX-ray1.70A/B2-324[»]
1L6YX-ray1.90A/B2-324[»]
ProteinModelPortaliP0ACB2.
SMRiP0ACB2. Positions 2-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACB2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP0ACB2.
KOiK01698.
OMAiQMNPANR.
OrthoDBiEOG6VXFCB.
PhylomeDBiP0ACB2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ACB2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDLIQRPRR LRKSPALRAM FEETTLSLND LVLPIFVEEE IDDYKAVEAM
60 70 80 90 100
PGVMRIPEKH LAREIERIAN AGIRSVMTFG ISHHTDETGS DAWREDGLVA
110 120 130 140 150
RMSRICKQTV PEMIVMSDTC FCEYTSHGHC GVLCEHGVDN DATLENLGKQ
160 170 180 190 200
AVVAAAAGAD FIAPSAAMDG QVQAIRQALD AAGFKDTAIM SYSTKFASSF
210 220 230 240 250
YGPFREAAGS ALKGDRKSYQ MNPMNRREAI RESLLDEAQG ADCLMVKPAG
260 270 280 290 300
AYLDIVRELR ERTELPIGAY QVSGEYAMIK FAALAGAIDE EKVVLESLGS
310 320
IKRAGADLIF SYFALDLAEK KILR
Length:324
Mass (Da):35,625
Last modified:January 23, 2007 - v2
Checksum:iCE814E5705BFD255
GO

Sequence cautioni

The sequence AAB18092.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA12842.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 192RA → PR in AAA62629. (PubMed:2656410)Curated
Sequence conflicti19 – 4224AMFEE…EEEID → VCLKRQHLSLTTWCCRSLLK KKLT in CAA35467. (PubMed:2464127)CuratedAdd
BLAST
Sequence conflicti90 – 912SD → ER in AAA62629. (PubMed:2656410)Curated
Sequence conflicti104 – 1041R → P in AAA62629. (PubMed:2656410)Curated
Sequence conflicti226 – 2261R → P in CAA35467. (PubMed:2464127)Curated
Sequence conflicti227 – 2271R → A in AAA62629. (PubMed:2656410)Curated
Sequence conflicti229 – 2291A → G in AAA62629. (PubMed:2656410)Curated
Sequence conflicti231 – 2311R → A in AAA62629. (PubMed:2656410)Curated
Sequence conflicti233 – 2331S → Y in AAA62629. (PubMed:2656410)Curated
Sequence conflicti241 – 2411A → P in AAA62629. (PubMed:2656410)Curated
Sequence conflicti254 – 2541D → N in AAA62629. (PubMed:2656410)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA64765. SYECPF.
RefSeqiNP_414903.4. NC_000913.3.
YP_488662.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73472; AAC73472; b0369.
BAE76150; BAE76150; BAE76150.
GeneIDi12932508.
945017.
KEGGiecj:Y75_p0358.
eco:b0369.
PATRICi32115877. VBIEscCol129921_0380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A64765. SYECPF.
RefSeqi NP_414903.4. NC_000913.3.
YP_488662.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B4E X-ray 2.00 A 2-324 [» ]
1I8J X-ray 1.90 A/B 2-324 [» ]
1L6S X-ray 1.70 A/B 2-324 [» ]
1L6Y X-ray 1.90 A/B 2-324 [» ]
ProteinModelPortali P0ACB2.
SMRi P0ACB2. Positions 2-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36209N.
IntActi P0ACB2. 6 interactions.
MINTi MINT-6765615.
STRINGi 511145.b0369.

Chemistry

BindingDBi P0ACB2.

2D gel databases

SWISS-2DPAGE P0ACB2.

Proteomic databases

PaxDbi P0ACB2.
PRIDEi P0ACB2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73472 ; AAC73472 ; b0369 .
BAE76150 ; BAE76150 ; BAE76150 .
GeneIDi 12932508.
945017.
KEGGi ecj:Y75_p0358.
eco:b0369.
PATRICi 32115877. VBIEscCol129921_0380.

Organism-specific databases

EchoBASEi EB0423.
EcoGenei EG10428. hemB.

Phylogenomic databases

eggNOGi COG0113.
HOGENOMi HOG000020323.
InParanoidi P0ACB2.
KOi K01698.
OMAi QMNPANR.
OrthoDBi EOG6VXFCB.
PhylomeDBi P0ACB2.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci EcoCyc:PORPHOBILSYNTH-MONOMER.
ECOL316407:JW0361-MONOMER.
MetaCyc:PORPHOBILSYNTH-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ACB2.
PROi P0ACB2.

Gene expression databases

Genevestigatori P0ACB2.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHEM2_ECOLI
AccessioniPrimary (citable) accession number: P0ACB2
Secondary accession number(s): P15002, P78247, Q2MC56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3