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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 (By similarity).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.1 Publication

Cofactori

Mg2+2 Publications

Enzyme regulationi

Stimulated by magnesium ions.

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
Active sitei205Schiff-base intermediate with substrate2 Publications1
Binding sitei215Substrate 12 Publications1
Binding sitei229Substrate 12 Publications1
Metal bindingi245Magnesium2 Publications1
Active sitei260Schiff-base intermediate with substrate2 Publications1
Binding sitei286Substrate 22 Publications1
Binding sitei324Substrate 22 Publications1

GO - Molecular functioni

  • porphobilinogen synthase activity Source: PseudoCAP
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • heme biosynthetic process Source: GO_Central
  • porphyrin-containing compound biosynthetic process Source: PseudoCAP
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.24. 5087.
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
Ordered Locus Names:PA5243
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5243.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3286086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001405071 – 337Delta-aminolevulinic acid dehydrataseAdd BLAST337

Proteomic databases

PaxDbiQ59643.
PRIDEiQ59643.

Interactioni

Subunit structurei

Homooctamer; formed by oligomerization of dimers.3 Publications

Protein-protein interaction databases

STRINGi208964.PA5243.

Chemistry databases

BindingDBiQ59643.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 12Combined sources3
Turni15 – 19Combined sources5
Helixi22 – 28Combined sources7
Helixi35 – 37Combined sources3
Beta strandi38 – 49Combined sources12
Beta strandi51 – 53Combined sources3
Beta strandi61 – 64Combined sources4
Helixi65 – 77Combined sources13
Beta strandi82 – 87Combined sources6
Helixi91 – 93Combined sources3
Beta strandi95 – 97Combined sources3
Helixi99 – 102Combined sources4
Helixi107 – 118Combined sources12
Beta strandi122 – 128Combined sources7
Turni131 – 133Combined sources3
Beta strandi134 – 136Combined sources3
Helixi150 – 166Combined sources17
Beta strandi170 – 174Combined sources5
Helixi181 – 191Combined sources11
Beta strandi198 – 206Combined sources9
Helixi209 – 211Combined sources3
Helixi212 – 216Combined sources5
Helixi221 – 224Combined sources4
Helixi229 – 231Combined sources3
Beta strandi232 – 234Combined sources3
Helixi240 – 251Combined sources12
Beta strandi255 – 261Combined sources7
Helixi263 – 265Combined sources3
Helixi266 – 276Combined sources11
Beta strandi280 – 284Combined sources5
Helixi286 – 297Combined sources12
Helixi305 – 316Combined sources12
Beta strandi319 – 323Combined sources5
Helixi326 – 334Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4KX-ray1.67A/B1-337[»]
1GZGX-ray1.66A/B1-337[»]
1W54X-ray2.20A/B1-337[»]
1W56X-ray1.70A/B1-337[»]
1W5MX-ray1.60A/B1-337[»]
1W5NX-ray1.65A/B1-337[»]
1W5OX-ray1.85A/B1-337[»]
1W5PX-ray1.55A/B1-337[»]
1W5QX-ray1.40A/B1-337[»]
2C13X-ray2.15A/B1-337[»]
2C14X-ray1.90A/B1-337[»]
2C15X-ray1.48A/B1-337[»]
2C16X-ray2.02A/B1-337[»]
2C18X-ray1.93A/B1-337[»]
2C19X-ray2.05A/B1-337[»]
2WOQX-ray1.75A1-337[»]
ProteinModelPortaliQ59643.
SMRiQ59643.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59643.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiQ59643.
KOiK01698.
OMAiMDPANSN.
PhylomeDBiQ59643.

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.

Q59643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFTPANRAY PYTRLRRNRR DDFSRRLVRE NVLTVDDLIL PVFVLDGVNQ
60 70 80 90 100
RESIPSMPGV ERLSIDQLLI EAEEWVALGI PALALFPVTP VEKKSLDAAE
110 120 130 140 150
AYNPEGIAQR ATRALRERFP ELGIITDVAL DPFTTHGQDG ILDDDGYVLN
160 170 180 190 200
DVSIDVLVRQ ALSHAEAGAQ VVAPSDMMDG RIGAIREALE SAGHTNVRIM
210 220 230 240 250
AYSAKYASAY YGPFRDAVGS ASNLGKGNKA TYQMDPANSD EALHEVAADL
260 270 280 290 300
AEGADMVMVK PGMPYLDIVR RVKDEFRAPT FVYQVSGEYA MHMGAIQNGW
310 320 330
LAESVILESL TAFKRAGADG ILTYFAKQAA EQLRRGR
Length:337
Mass (Da):37,037
Last modified:November 1, 1996 - v1
Checksum:i7D650C49795D542C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91820 Genomic DNA. Translation: CAA62930.1.
AE004091 Genomic DNA. Translation: AAG08628.1.
PIRiS60577.
RefSeqiNP_253930.1. NC_002516.2.
WP_003096352.1. NZ_ASJY01000816.1.

Genome annotation databases

EnsemblBacteriaiAAG08628; AAG08628; PA5243.
GeneIDi879701.
KEGGipae:PA5243.
PATRICi19845337. VBIPseAer58763_5495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91820 Genomic DNA. Translation: CAA62930.1.
AE004091 Genomic DNA. Translation: AAG08628.1.
PIRiS60577.
RefSeqiNP_253930.1. NC_002516.2.
WP_003096352.1. NZ_ASJY01000816.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4KX-ray1.67A/B1-337[»]
1GZGX-ray1.66A/B1-337[»]
1W54X-ray2.20A/B1-337[»]
1W56X-ray1.70A/B1-337[»]
1W5MX-ray1.60A/B1-337[»]
1W5NX-ray1.65A/B1-337[»]
1W5OX-ray1.85A/B1-337[»]
1W5PX-ray1.55A/B1-337[»]
1W5QX-ray1.40A/B1-337[»]
2C13X-ray2.15A/B1-337[»]
2C14X-ray1.90A/B1-337[»]
2C15X-ray1.48A/B1-337[»]
2C16X-ray2.02A/B1-337[»]
2C18X-ray1.93A/B1-337[»]
2C19X-ray2.05A/B1-337[»]
2WOQX-ray1.75A1-337[»]
ProteinModelPortaliQ59643.
SMRiQ59643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5243.

Chemistry databases

BindingDBiQ59643.
ChEMBLiCHEMBL3286086.

Proteomic databases

PaxDbiQ59643.
PRIDEiQ59643.

Protocols and materials databases

DNASUi879701.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08628; AAG08628; PA5243.
GeneIDi879701.
KEGGipae:PA5243.
PATRICi19845337. VBIPseAer58763_5495.

Organism-specific databases

PseudoCAPiPA5243.

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiQ59643.
KOiK01698.
OMAiMDPANSN.
PhylomeDBiQ59643.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BRENDAi4.2.1.24. 5087.

Miscellaneous databases

EvolutionaryTraceiQ59643.
PROiQ59643.

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_PSEAE
AccessioniPrimary (citable) accession number: Q59643
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.