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P30950

- HEM2_BACSU

UniProt

P30950 - HEM2_BACSU

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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

    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

    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: 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 ALADH family.Curated

    Phylogenomic databases

    eggNOGiCOG0113.
    HOGENOMiHOG000020323.
    KOiK01698.
    OMAiDMILTYF.
    OrthoDBiEOG6VXFCB.
    PhylomeDBiP30950.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. 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

    MSQSFNRHRR LRTSKAMREM VKETRLHPSD FIYPIFVVEG LEGKKAVPSM    50
    PDVHHVSLDL LKDEVAELVK LGIQSVIVFG IPEEKDDCGT QAYHDHGIVQ 100
    KAITEIKEHF PEMVVVADTC LCEYTDHGHC GLVKDGVILN DESLELLAQT 150
    AVSQAKAGAD IIAPSNMMDG FVTVIREALD KEGFVNIPIM SYAVKYSSEF 200
    YGPFRDAANS TPQFGDRKTY QMDPANRMEA LREAQSDVEE GADFLIVKPS 250
    LSYMDIMRDV KNEFTLPLVA YNVSGEYSMV KAAAQNGWIK EKEIVLEILT 300
    SMKRAGADLI ITYHAKDAAK WLAE 324
    Length:324
    Mass (Da):36,209
    Last modified:July 1, 1993 - v1
    Checksum:iC1CF7E157AE6CB07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_CM000487.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57676 Genomic DNA. Translation: AAA22514.1 .
    AL009126 Genomic DNA. Translation: CAB14773.1 .
    PIRi C42728.
    RefSeqi NP_390691.1. NC_000964.3.
    WP_003229631.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P30950.
    SMRi P30950. Positions 5-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU28130.

    Proteomic databases

    PaxDbi P30950.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14773 ; CAB14773 ; BSU28130 .
    GeneIDi 936972.
    KEGGi bsu:BSU28130.
    PATRICi 18977502. VBIBacSub10457_2940.

    Organism-specific databases

    GenoListi BSU28130. [Micado ]

    Phylogenomic databases

    eggNOGi COG0113.
    HOGENOMi HOG000020323.
    KOi K01698.
    OMAi DMILTYF.
    OrthoDBi EOG6VXFCB.
    PhylomeDBi P30950.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .
    BioCyci BSUB:BSU28130-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR001731. Porphobilinogen_synth.
    [Graphical view ]
    PANTHERi PTHR11458. PTHR11458. 1 hit.
    Pfami PF00490. ALAD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
    PRINTSi PR00144. DALDHYDRTASE.
    SMARTi SM01004. ALAD. 1 hit.
    [Graphical view ]
    PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1991) [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(1997) [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: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 102 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