Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P42504

- HEM2_RHOCA

UniProt

P42504 - HEM2_RHOCA

Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Catalytic activityi

    2 5-aminolevulinate = porphobilinogen + 2 H2O.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei202 – 2021Schiff-base intermediate with substrateBy similarity
    Binding sitei212 – 2121Substrate 1By similarity
    Binding sitei225 – 2251Substrate 1By similarity
    Active sitei256 – 2561Schiff-base intermediate with substrateBy similarity
    Binding sitei282 – 2821Substrate 2By similarity
    Binding sitei321 – 3211Substrate 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: InterPro
    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13250.
    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
    OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
    Taxonomic identifieri1061 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Delta-aminolevulinic acid dehydratasePRO_0000140508Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP42504.
    SMRiP42504. Positions 8-331.
    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]
    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.

    P42504-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLITPPFPT NRLRRMRRTE ALRDLAQENR LSVKDLIWPI FITDVPGADV    50
    EISSMPGVVR RTMDGALKAA EGSRDAGHSR DLPVPLTDPA VKTETCEMAW 100
    QPDNFTNRVI AAMKQAVPEV AIMTDIALDP YNANGHDGLV RDGILLNDET 150
    TEALVKMALA QAAAGADILG PSDMMDGRVG AIRQAMEAAG HKDIAILSYA 200
    AKYASAFYGP FRDAVGASSA LKGDKKTYQM NPANSAEALR NVARDIAEGA 250
    DMVMVKPGMP YLDIVRQVKD AFGMPTYAYQ VSGEYAMLMA AVQNGWLNHD 300
    KVMLESLMAF RRAGCDGVLT YFAPAAAKLI GA 332
    Length:332
    Mass (Da):35,854
    Last modified:November 1, 1995 - v1
    Checksum:i4118DED5A15C8DBE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14593 Genomic DNA. Translation: AAA92884.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14593 Genomic DNA. Translation: AAA92884.1 .

    3D structure databases

    ProteinModelPortali P42504.
    SMRi P42504. Positions 8-331.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00318 .
    BioCyci MetaCyc:MONOMER-13250.

    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. "Nucleotide sequence of the Rhodobacter capsulatus hemB gene."
      Indest K., Biel A.J.
      Plant Physiol. 108:421-421(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PAS100.
    2. "Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer."
      Bollivar D.W., Clauson C., Lighthall R., Forbes S., Kokona B., Fairman R., Kundrat L., Jaffe E.K.
      BMC Biochem. 5:17-17(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, ABSENCE OF METAL COFACTOR REQUIREMENT, SUBUNIT.

    Entry informationi

    Entry nameiHEM2_RHOCA
    AccessioniPrimary (citable) accession number: P42504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Does not seem to have a metal requirement for activity.

    Documents

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

    External Data

    Dasty 3