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P11392

- PHEA_PORPP

UniProt

P11392 - PHEA_PORPP

Protein

B-phycoerythrin alpha chain

Gene

cpeA

Organism
Porphyridium purpureum (Red alga) (Porphyridium cruentum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Phycoerythrobilin chromophore 1 (covalent; via 1 link)
    Binding sitei139 – 1391Phycoerythrobilin chromophore 2 (covalent; via 1 link)

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW
    2. photosynthesis Source: UniProtKB-KW
    3. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Photosynthesis, Transport

    Keywords - Ligandi

    Bile pigment, Chromophore

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-phycoerythrin alpha chain
    Gene namesi
    Name:cpeA
    Encoded oniPlastid; Chloroplast
    OrganismiPorphyridium purpureum (Red alga) (Porphyridium cruentum)
    Taxonomic identifieri35688 [NCBI]
    Taxonomic lineageiEukaryotaRhodophytaBangiophyceaePorphyridialesPorphyridiaceaePorphyridium

    Subcellular locationi

    Plastidchloroplast thylakoid membrane By similarity; Peripheral membrane protein By similarity; Stromal side By similarity
    Note: Forms the periphery of the phycobilisome rod.By similarity

    GO - Cellular componenti

    1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
    2. phycobilisome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164B-phycoerythrin alpha chainPRO_0000199176Add
    BLAST

    Post-translational modificationi

    Contains two covalently linked bilin chromophores.

    Interactioni

    Subunit structurei

    Heteropolymer of 6 alpha, 6 beta and one gamma chain.By similarity

    Protein-protein interaction databases

    IntActiP11392. 1 interaction.
    MINTiMINT-8389565.

    Structurei

    Secondary structure

    1
    164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1512
    Helixi21 – 6242
    Helixi64 – 674
    Helixi76 – 9924
    Helixi103 – 1086
    Turni109 – 1124
    Helixi113 – 1197
    Helixi124 – 13714
    Turni140 – 1434
    Helixi146 – 16217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3V57X-ray1.70A/C1-164[»]
    3V58X-ray1.85A/C1-164[»]
    ProteinModelPortaliP11392.
    SMRiP11392. Positions 1-164.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phycobiliprotein family.Curated

    Family and domain databases

    Gene3Di1.10.490.20. 1 hit.
    InterProiIPR009050. Globin-like.
    IPR012128. Phycobilisome_asu/bsu.
    [Graphical view]
    PfamiPF00502. Phycobilisome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000081. Phycocyanin. 1 hit.
    SUPFAMiSSF46458. SSF46458. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P11392-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSVITTVVS AADAAGRFPS NSDLESIQGN IQRSAARLEA AEKLAGNHEA    50
    VVKEAGDACF AKYAYLKNPG EAGENQEKIN KCYRDVDHYM RLVNYDLVVG 100
    GTGPLDEWGI AGAREVYRTL NLPTSAYVAS IAYTRDRLCV PRDMSAQAGV 150
    EFSAYLDYLI NALS 164
    Length:164
    Mass (Da):17,817
    Last modified:July 1, 1989 - v1
    Checksum:iA704CE21D52B8D7E
    GO

    Sequence databases

    PIRiS02817.

    Cross-referencesi

    Sequence databases

    PIRi S02817.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3V57 X-ray 1.70 A/C 1-164 [» ]
    3V58 X-ray 1.85 A/C 1-164 [» ]
    ProteinModelPortali P11392.
    SMRi P11392. Positions 1-164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11392. 1 interaction.
    MINTi MINT-8389565.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.490.20. 1 hit.
    InterProi IPR009050. Globin-like.
    IPR012128. Phycobilisome_asu/bsu.
    [Graphical view ]
    Pfami PF00502. Phycobilisome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000081. Phycocyanin. 1 hit.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum."
      Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.
      Biol. Chem. Hoppe-Seyler 370:115-124(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies."
      Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.
      J. Biol. Chem. 259:5472-5480(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 79-84 AND 136-142, CHROMOPHORE BINDING AT CYS-82 AND CYS-139.

    Entry informationi

    Entry nameiPHEA_PORPP
    AccessioniPrimary (citable) accession number: P11392
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3