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Q43058

- HEM2_PHYPA

UniProt

Q43058 - HEM2_PHYPA

Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (03 Sep 2014)
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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 sitei300 – 3001Schiff-base intermediate with substrateBy similarity
    Binding sitei310 – 3101Substrate 1By similarity
    Binding sitei322 – 3221Substrate 1By similarity
    Metal bindingi338 – 3381MagnesiumBy similarity
    Active sitei353 – 3531Schiff-base intermediate with substrateBy similarity
    Binding sitei379 – 3791Substrate 2By similarity
    Binding sitei418 – 4181Substrate 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. porphyrin-containing compound biosynthetic process Source: UniProtKB-KW
    3. 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
    ORF Names:PHYPADRAFT_221821
    OrganismiPhyscomitrella patens subsp. patens (Moss)
    Taxonomic identifieri3218 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
    ProteomesiUP000006727: Partially assembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 432Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013318
    Transit peptidei1 – ?ChloroplastSequence Analysis

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ43058.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALADH family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0113.
    HOGENOMiHOG000020323.

    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]
    PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q43058-1 [UniParc]FASTAAdd to Basket

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    MVGVMMAAAA TPGCGVSQAL TACGSHEGLR RVAPVFGPGV VSVSAPCKLP    50
    RKLNVQAVAE PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA 100
    ISPLVMPARP RRNRRSPALR AAFQETTISP ANFILPLFVH EGEQNAPIGA 150
    MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL FPKVPDALKS STGDEAYNPD 200
    GLVPRCIRLL KDKFPDLVIY TDVALDPYSS DGHDGIVRED GLIMNDETVH 250
    QLCKQAVAQA QAGADVVSPS DMMDGRVGAI RKALDLAGHQ DVSIMAYTAK 300
    YASAFYGPFR EALDSNPRFG DKKTYQMNPA NYREALIETR MDEAEGADIL 350
    MVKPAMPYLD VIRLLRDNTA LPISAYQVSG EYSMIRAAAA AGMLDEKKAV 400
    LESLLSIRRA GADVILTYFA IQAAQWLCAE RV 432
    Length:432
    Mass (Da):46,263
    Last modified:September 3, 2014 - v2
    Checksum:iE90018ADAAAA12FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151G → R in CAA61978. 1 PublicationCurated
    Sequence conflicti24 – 241G → S in CAA61978. 1 PublicationCurated
    Sequence conflicti212 – 2143DKF → AI in CAA61978. 1 PublicationCurated
    Sequence conflicti295 – 2951M → I in CAA61978. 1 PublicationCurated
    Sequence conflicti309 – 3091F → S in CAA61978. 1 PublicationCurated
    Sequence conflicti388 – 3914AAAA → GCR in CAA61978. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89886 mRNA. Translation: CAA61978.1.
    DS545108 Genomic DNA. Translation: EDQ57858.1.
    PIRiS58169.
    UniGeneiPpa.5213.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89886 mRNA. Translation: CAA61978.1 .
    DS545108 Genomic DNA. Translation: EDQ57858.1 .
    PIRi S58169.
    UniGenei Ppa.5213.

    3D structure databases

    ProteinModelPortali Q43058.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0113.
    HOGENOMi HOG000020323.

    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 ]
    PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Gwarek M.A.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
      Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
      , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
      Science 319:64-69(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Gransden 2004.

    Entry informationi

    Entry nameiHEM2_PHYPA
    AccessioniPrimary (citable) accession number: Q43058
    Secondary accession number(s): A9TFG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 3, 2014
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3