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Q59295

- HEM2_CLOJO

UniProt

Q59295 - HEM2_CLOJO

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Clostridium josui
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 bindingi117 – 1171Zinc; catalyticBy similarity
    Metal bindingi119 – 1191Zinc; catalyticBy similarity
    Metal bindingi127 – 1271Zinc; catalyticBy similarity
    Active sitei192 – 1921Schiff-base intermediate with substrateBy similarity
    Binding sitei202 – 2021SubstrateBy 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

    Metal-binding, Zinc

    Enzyme and pathway databases

    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
    OrganismiClostridium josui
    Taxonomic identifieri1499 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›205›205Delta-aminolevulinic acid dehydratasePRO_0000140500Add
    BLAST

    Proteomic databases

    PRIDEiQ59295.

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ59295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    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]
    PRINTSiPR00144. DALDHYDRTASE.
    SMARTiSM01004. ALAD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q59295-1 [UniParc]FASTAAdd to Basket

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    MIKRPRRLRT NEVLRKAVRE TRLSTDSLIW PLFIVEGKNI KKEISSLPGQ    50
    YHFSPDMVGK AIEAALKADV KSVLLFGLPK HKDEKGSEAY NENGVLQQGI 100
    REIKQRYPQM QVITDICMCE YTSHGHCGIL EGERVDNDRT LPYLEKIALS 150
    HVMAGADMIA PSDMMDGRIY ALRSTLDKNG FTDIPIMSYA VKYASSFYGP 200
    FREAA 205
    Length:205
    Mass (Da):23,172
    Last modified:November 1, 1997 - v1
    Checksum:i886F9DAEFDB1144E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei205 – 2051

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28503 Genomic DNA. Translation: BAA05863.1.
    PIRiI40812.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28503 Genomic DNA. Translation: BAA05863.1 .
    PIRi I40812.

    3D structure databases

    ProteinModelPortali Q59295.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q59295.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .

    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 ]
    PRINTSi PR00144. DALDHYDRTASE.
    SMARTi SM01004. ALAD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
      Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
      J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FERM P-9684.

    Entry informationi

    Entry nameiHEM2_CLOJO
    AccessioniPrimary (citable) accession number: Q59295
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3