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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandMagnesium, 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3308970

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
SMRiP30950
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiENOG4105D52 Bacteria
COG0113 LUCA
HOGENOMiHOG000020323
InParanoidiP30950
KOiK01698
OMAiYQMDYAN
PhylomeDBiP30950

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM
PANTHERiPTHR11458 PTHR11458, 1 hit
PfamiView protein in Pfam
PF00490 ALAD, 1 hit
PIRSFiPIRSF001415 Porphbilin_synth, 1 hit
PRINTSiPR00144 DALDHYDRTASE
SMARTiView protein in SMART
SM01004 ALAD, 1 hit
PROSITEiView protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit

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
PATRICifig|224308.179.peg.3056

Similar proteinsi

Entry informationi

Entry nameiHEM2_BACSU
AccessioniPrimary (citable) accession number: P30950
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 18, 2018
This is version 118 of the entry and version 1 of the sequence. See 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

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