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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Zinc; catalyticBy similarity
Metal bindingi122 – 1221Zinc; catalyticBy similarity
Metal bindingi130 – 1301Zinc; catalyticBy similarity
Active sitei195 – 1951Schiff-base intermediate with substrateBy similarity
Binding sitei205 – 2051Substrate 1By similarity
Binding sitei217 – 2171Substrate 1By similarity
Metal bindingi233 – 2331MagnesiumBy similarity
Active sitei248 – 2481Schiff-base intermediate with substrateBy similarity
Binding sitei274 – 2741Substrate 2By similarity
Binding sitei313 – 3131Substrate 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. 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, 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
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU28130. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Delta-aminolevulinic acid dehydratasePRO_0000140493Add
BLAST

Proteomic databases

PaxDbiP30950.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU28130.

Structurei

3D structure databases

ProteinModelPortaliP30950.
SMRiP30950. Positions 5-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP30950.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.
PhylomeDBiP30950.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR030656. ALAD_AS.
IPR013785. 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.

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:June 30, 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.
SMRiP30950. Positions 5-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU28130.

Proteomic databases

PaxDbiP30950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU28130. [Micado]

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP30950.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.
PhylomeDBiP30950.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciBSUB:BSU28130-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR030656. ALAD_AS.
IPR013785. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III."
    Hansson M., Rutberg L., Schroeder I., Hederstedt L.
    J. Bacteriol. 173:2590-2599(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiHEM2_BACSU
AccessioniPrimary (citable) accession number: P30950
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1993
Last sequence update: June 30, 1993
Last modified: March 31, 2015
This is version 106 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

External Data

Dasty 3

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 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.