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PHEB_PORPP
ID   PHEB_PORPP              Reviewed;         177 AA.
AC   P11393;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=B-phycoerythrin beta chain;
GN   Name=cpeB;
OS   Porphyridium purpureum (Red alga) (Porphyridium cruentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Porphyridiales; Porphyridiaceae;
OC   Porphyridium.
OX   NCBI_TaxID=35688;
RN   [1]
RP   PROTEIN SEQUENCE, AND METHYLATION AT ASN-72.
RX   PubMed=2495805; DOI=10.1515/bchm3.1989.370.1.115;
RA   Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.;
RT   "The complete amino-acid sequence of the alpha and beta subunits of B-
RT   phycoerythrin from the rhodophytan alga Porphyridium cruentum.";
RL   Biol. Chem. Hoppe-Seyler 370:115-124(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 38-77; 79-84 AND 151-171, AND CHROMOPHORE ATTACHMENT
RP   SITES.
RX   PubMed=6715353; DOI=10.1016/s0021-9258(18)91035-5;
RA   Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.;
RT   "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin.
RT   Amino acid sequence studies.";
RL   J. Biol. Chem. 259:5472-5480(1984).
CC   -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC       phycobiliprotein complex.
CC   -!- SUBUNIT: Heteromer of 6 alpha, 6 beta and one gamma chain.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC       {ECO:0000250}. Note=Forms the periphery of the phycobilisome rod.
CC       {ECO:0000250}.
CC   -!- PTM: Contains two covalently linked phycoerythrobilin chromophores and
CC       one covalently linked phycourobilin chromophore.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR   PIR; S02818; S02818.
DR   RefSeq; YP_008965770.1; NC_023133.1.
DR   PDB; 3V57; X-ray; 1.70 A; B/D=1-177.
DR   PDB; 3V58; X-ray; 1.85 A; B/D=1-177.
DR   PDB; 6KGX; EM; 2.80 A; 11/14/A5/AC/B1/B3/B4/B5/BC/BD/BE/BG/C5/C9/CC/CJ/D1/D3/D4/D8/DA/DD/DE/DG/E9/EJ/F1/F3/F4/F5=1-177.
DR   PDB; 7LIX; EM; 2.80 A; B/C/D=1-177.
DR   PDB; 7LIY; EM; 2.80 A; B/C=1-177.
DR   PDB; 7LIZ; EM; 2.80 A; B/C=1-177.
DR   PDB; 7LJ0; EM; 2.80 A; B=1-177.
DR   PDBsum; 3V57; -.
DR   PDBsum; 3V58; -.
DR   PDBsum; 6KGX; -.
DR   PDBsum; 7LIX; -.
DR   PDBsum; 7LIY; -.
DR   PDBsum; 7LIZ; -.
DR   PDBsum; 7LJ0; -.
DR   AlphaFoldDB; P11393; -.
DR   SMR; P11393; -.
DR   IntAct; P11393; 1.
DR   MINT; P11393; -.
DR   iPTMnet; P11393; -.
DR   GeneID; 17963946; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.20; -; 1.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012128; Phycobilisome_asu/bsu.
DR   InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR   Pfam; PF00502; Phycobilisome; 1.
DR   PIRSF; PIRSF000081; Phycocyanin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW   Direct protein sequencing; Electron transport; Membrane; Methylation;
KW   Photosynthesis; Phycobilisome; Plastid; Thylakoid; Transport.
FT   CHAIN           1..177
FT                   /note="B-phycoerythrin beta chain"
FT                   /id="PRO_0000199194"
FT   BINDING         50
FT                   /ligand="phycourobilin"
FT                   /ligand_id="ChEBI:CHEBI:189062"
FT                   /note="covalent, via 2 links"
FT   BINDING         61
FT                   /ligand="phycourobilin"
FT                   /ligand_id="ChEBI:CHEBI:189062"
FT                   /note="covalent, via 2 links"
FT   BINDING         82
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="1"
FT                   /note="covalent, via 1 link"
FT   BINDING         158
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="2"
FT                   /note="covalent, via 1 link"
FT   MOD_RES         72
FT                   /note="N4-methylasparagine"
FT                   /evidence="ECO:0000269|PubMed:2495805"
FT   CONFLICT        167
FT                   /note="S -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:7LIX"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           48..62
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           76..99
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           103..108
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   TURN            109..112
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           113..120
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           124..142
FT                   /evidence="ECO:0007829|PDB:3V57"
FT   HELIX           159..176
FT                   /evidence="ECO:0007829|PDB:3V57"
SQ   SEQUENCE   177 AA;  18554 MW;  168E71372A29CD89 CRC64;
     MLDAFSRVVV NSDAKAAYVG GSDLQALKSF IADGNKRLDA VNSIVSNASC MVSDAVSGMI
     CENPGLISPG GNCYTNRRMA ACLRDGEIIL RYVSYALLAG DASVLEDRCL NGLKETYIAL
     GVPTNSSIRA VSIMKAQAVA FITNTATERK MSFAAGDCTS LASEVASYFD RVGAAIS
 
 
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