Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Porphobilinogen deaminase (hemC)
  3. Uroporphyrinogen-III synthase (hemD)
  4. Uroporphyrinogen decarboxylase (hemE)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Zinc; catalytic2 Publications1
Metal bindingi122Zinc; catalytic2 Publications1
Metal bindingi130Zinc; catalytic2 Publications1
Active sitei195Schiff-base intermediate with substrate1
Binding sitei205Substrate 11
Binding sitei216Substrate 11
Metal bindingi232Magnesium2 Publications1
Active sitei247Schiff-base intermediate with substrate1
Binding sitei273Substrate 21
Binding sitei312Substrate 21

GO - Molecular functioni

  • metal ion binding Source: EcoCyc
  • porphobilinogen synthase activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • heme biosynthetic process Source: EcoliWiki
  • 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.
BRENDAi4.2.1.24. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10428. hemB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi127H → A: No significant effect on activity; when associated with A-129. 1 Publication1
Mutagenesisi129H → A: No significant effect on activity; when associated with A-127. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3286083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001405012 – 324Delta-aminolevulinic acid dehydrataseAdd BLAST323

Proteomic databases

EPDiP0ACB2.
PaxDbiP0ACB2.
PRIDEiP0ACB2.

2D gel databases

SWISS-2DPAGEP0ACB2.

Interactioni

Subunit structurei

Homooctamer.3 Publications

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP0ACB2.

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 12Combined sources5
Helixi15 – 21Combined sources7
Helixi28 – 30Combined sources3
Beta strandi31 – 38Combined sources8
Beta strandi48 – 50Combined sources3
Beta strandi54 – 57Combined sources4
Helixi58 – 60Combined sources3
Helixi61 – 70Combined sources10
Beta strandi75 – 81Combined sources7
Beta strandi86 – 88Combined sources3
Helixi90 – 93Combined sources4
Helixi98 – 109Combined sources12
Beta strandi113 – 119Combined sources7
Turni122 – 124Combined sources3
Beta strandi125 – 127Combined sources3
Beta strandi129 – 133Combined sources5
Beta strandi135 – 138Combined sources4
Helixi140 – 157Combined sources18
Beta strandi160 – 164Combined sources5
Helixi171 – 181Combined sources11
Beta strandi188 – 190Combined sources3
Beta strandi194 – 196Combined sources3
Helixi199 – 201Combined sources3
Helixi202 – 208Combined sources7
Turni217 – 219Combined sources3
Helixi226 – 238Combined sources13
Beta strandi242 – 248Combined sources7
Helixi250 – 252Combined sources3
Helixi253 – 260Combined sources8
Beta strandi267 – 271Combined sources5
Helixi273 – 284Combined sources12
Helixi290 – 303Combined sources14
Beta strandi307 – 311Combined sources5
Helixi314 – 319Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4EX-ray2.00A2-324[»]
1I8JX-ray1.90A/B2-324[»]
1L6SX-ray1.70A/B2-324[»]
1L6YX-ray1.90A/B2-324[»]
5IC2X-ray2.10A1-324[»]
ProteinModelPortaliP0ACB2.
SMRiP0ACB2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACB2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiP0ACB2.
KOiK01698.
OMAiISYHAKE.
PhylomeDBiP0ACB2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA12842 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18 – 19RA → PR in AAA62629 (PubMed:2656410).Curated2
Sequence conflicti19 – 42AMFEE…EEEID → VCLKRQHLSLTTWCCRSLLK KKLT in CAA35467 (PubMed:2464127).CuratedAdd BLAST24
Sequence conflicti90 – 91SD → ER in AAA62629 (PubMed:2656410).Curated2
Sequence conflicti104R → P in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti226R → P in CAA35467 (PubMed:2464127).Curated1
Sequence conflicti227R → A in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti229A → G in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti231R → A in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti233S → Y in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti241A → P in AAA62629 (PubMed:2656410).Curated1
Sequence conflicti254D → N in AAA62629 (PubMed:2656410).Curated1

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.
WP_001295337.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73472; AAC73472; b0369.
BAE76150; BAE76150; BAE76150.
GeneIDi945017.
KEGGiecj:JW0361.
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.
PIRiA64765. SYECPF.
RefSeqiNP_414903.4. NC_000913.3.
WP_001295337.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4EX-ray2.00A2-324[»]
1I8JX-ray1.90A/B2-324[»]
1L6SX-ray1.70A/B2-324[»]
1L6YX-ray1.90A/B2-324[»]
5IC2X-ray2.10A1-324[»]
ProteinModelPortaliP0ACB2.
SMRiP0ACB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP0ACB2.
ChEMBLiCHEMBL3286083.

2D gel databases

SWISS-2DPAGEP0ACB2.

Proteomic databases

EPDiP0ACB2.
PaxDbiP0ACB2.
PRIDEiP0ACB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73472; AAC73472; b0369.
BAE76150; BAE76150; BAE76150.
GeneIDi945017.
KEGGiecj:JW0361.
eco:b0369.
PATRICi32115877. VBIEscCol129921_0380.

Organism-specific databases

EchoBASEiEB0423.
EcoGeneiEG10428. hemB.

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiP0ACB2.
KOiK01698.
OMAiISYHAKE.
PhylomeDBiP0ACB2.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciEcoCyc:PORPHOBILSYNTH-MONOMER.
ECOL316407:JW0361-MONOMER.
MetaCyc:PORPHOBILSYNTH-MONOMER.
BRENDAi4.2.1.24. 2026.

Miscellaneous databases

EvolutionaryTraceiP0ACB2.
PROiP0ACB2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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]
ProtoNetiSearch...

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 2, 2016
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.