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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

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; catalyticBy similarity1
Metal bindingi122Zinc; catalyticBy similarity1
Metal bindingi130Zinc; catalyticBy similarity1
Active sitei195Schiff-base intermediate with substrateBy similarity1
Binding sitei205Substrate 1By similarity1
Binding sitei217Substrate 1By similarity1
Metal bindingi233MagnesiumBy similarity1
Active sitei248Schiff-base intermediate with substrateBy similarity1
Binding sitei274Substrate 2By similarity1
Binding sitei313Substrate 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU28130-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
Ordered Locus Names:BSU28130
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001404931 – 324Delta-aminolevulinic acid dehydrataseAdd BLAST324

Proteomic databases

PaxDbiP30950.
PRIDEiP30950.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015371.

Structurei

3D structure databases

ProteinModelPortaliP30950.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiP30950.
KOiK01698.
OMAiMDPANSN.
PhylomeDBiP30950.

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.

P30950-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSFNRHRR LRTSKAMREM VKETRLHPSD FIYPIFVVEG LEGKKAVPSM
60 70 80 90 100
PDVHHVSLDL LKDEVAELVK LGIQSVIVFG IPEEKDDCGT QAYHDHGIVQ
110 120 130 140 150
KAITEIKEHF PEMVVVADTC LCEYTDHGHC GLVKDGVILN DESLELLAQT
160 170 180 190 200
AVSQAKAGAD IIAPSNMMDG FVTVIREALD KEGFVNIPIM SYAVKYSSEF
210 220 230 240 250
YGPFRDAANS TPQFGDRKTY QMDPANRMEA LREAQSDVEE GADFLIVKPS
260 270 280 290 300
LSYMDIMRDV KNEFTLPLVA YNVSGEYSMV KAAAQNGWIK EKEIVLEILT
310 320
SMKRAGADLI ITYHAKDAAK WLAE
Length:324
Mass (Da):36,209
Last modified:July 1, 1993 - v1
Checksum:iC1CF7E157AE6CB07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22514.1.
AL009126 Genomic DNA. Translation: CAB14773.1.
PIRiC42728.
RefSeqiNP_390691.1. NC_000964.3.
WP_003229631.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14773; CAB14773; BSU28130.
GeneIDi936972.
KEGGibsu:BSU28130.
PATRICi18977502. VBIBacSub10457_2940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22514.1.
AL009126 Genomic DNA. Translation: CAB14773.1.
PIRiC42728.
RefSeqiNP_390691.1. NC_000964.3.
WP_003229631.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP30950.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015371.

Proteomic databases

PaxDbiP30950.
PRIDEiP30950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14773; CAB14773; BSU28130.
GeneIDi936972.
KEGGibsu:BSU28130.
PATRICi18977502. VBIBacSub10457_2940.

Phylogenomic databases

eggNOGiENOG4105D52. Bacteria.
COG0113. LUCA.
HOGENOMiHOG000020323.
InParanoidiP30950.
KOiK01698.
OMAiMDPANSN.
PhylomeDBiP30950.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciBSUB:BSU28130-MONOMER.

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_BACSU
AccessioniPrimary (citable) accession number: P30950
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 5, 2016
This is version 114 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.