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Q42682

- HEM2_CHLRE

UniProt

Q42682 - HEM2_CHLRE

Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (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 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei251 – 2511Schiff-base intermediate with substrateBy similarity
    Binding sitei261 – 2611Substrate 1By similarity
    Binding sitei281 – 2811Substrate 1By similarity
    Metal bindingi297 – 2971MagnesiumBy similarity
    Active sitei312 – 3121Schiff-base intermediate with substrateBy similarity
    Binding sitei338 – 3381Substrate 2By similarity
    Binding sitei377 – 3771Substrate 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-KW
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00251; UER00318.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-aminolevulinic acid dehydratase, chloroplastic (EC:4.2.1.24)
    Short name:
    ALADH
    Alternative name(s):
    Porphobilinogen synthase
    Gene namesi
    Name:HEMB
    Synonyms:ALAD
    OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
    Taxonomic identifieri3055 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast stroma Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424ChloroplastSequence AnalysisAdd
    BLAST
    Chaini25 – 390366Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013315Add
    BLAST

    Proteomic databases

    PRIDEiQ42682.
    ProMEXiQ42682.

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ42682.
    SMRiQ42682. Positions 58-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0113.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q42682-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQMMQRNVVG QRPVAGSRRS LVVANVAEVT RPAVSTNGKH RTGVPEGTPI    50
    VTPQDLPSRP RRNRRSESFR ASVREVNVSP ANFILPIFIH EESNQNVPIA 100
    SMPGINRLAY GKNVIDYVAE PRSYGVNQVV VFPKTPDHLK TQTAEEAFNK 150
    NGLSQRTIRL LKDSFPDLEV YTDVALDPYN SDGHDGIVSD AGVILNDETI 200
    EYLCRQAVSQ AEAGADVVSP SDMMDGRVGA IRRALDREGF TNVSIMSYTA 250
    KYASAYYGPF RDALASAPKP GQAHRRIPPN KKTYQMDPAN YREAIREAKA 300
    DEAEGADIMM VKPGMPYLDV VRLLRETSPL PVAVYHVSGE YAMLKAAAER 350
    GWLNEKDAVL EAMTCFRRAG GDLILTYYGI EASKWLAGEK 390
    Length:390
    Mass (Da):43,046
    Last modified:November 1, 1997 - v1
    Checksum:i6114C4E0325A4242
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19876 mRNA. Translation: AAA79515.1.
    PIRiS53487.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19876 mRNA. Translation: AAA79515.1 .
    PIRi S53487.

    3D structure databases

    ProteinModelPortali Q42682.
    SMRi Q42682. Positions 58-387.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q42682.
    ProMEXi Q42682.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0113.

    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 ]
    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. "Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, delta-aminolevulinic acid dehydratase (porphobilinogen synthase)."
      Matters G.L., Beale S.I.
      Plant Mol. Biol. 27:607-617(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NO-.

    Entry informationi

    Entry nameiHEM2_CHLRE
    AccessioniPrimary (citable) accession number: Q42682
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

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

    External Data

    Dasty 3