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PHEA_POLUR
ID   PHEA_POLUR              Reviewed;         164 AA.
AC   P84861;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=R-phycoerythrin alpha chain;
GN   Name=cpeA; Synonyms=rpeA;
OS   Polysiphonia urceolata (Red alga) (Conferva urceolata).
OG   Plastid; Chloroplast {ECO:0000305}.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Rhodomelaceae; Polysiphonioideae; Polysiphonia.
OX   NCBI_TaxID=65404;
RN   [1] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PHEB AND
RP   PHYCOCYANOBILIN, CHROMOPHORE BINDING AT ASN-47; LYS-81; CYS-82; ARG-84;
RP   HIS-88; ARG-137; CYS-139 AND ARG-142, AND SUBUNIT.
RX   PubMed=8876649; DOI=10.1006/jmbi.1996.0547;
RA   Chang W.-R., Jiang T., Wan Z.-L., Zhang J.-P., Yang Z.-X., Liang D.-C.;
RT   "Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A
RT   resolution.";
RL   J. Mol. Biol. 262:721-731(1996).
CC   -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC       protein from the phycobiliprotein complex.
CC       {ECO:0000269|PubMed:8876649}.
CC   -!- SUBUNIT: Heterododecamer of 6 alpha and 6 beta chains. The basic
CC       functional unit of phycobiliproteins is a ring-shaped hexamer formed
CC       from two back-to-back trimers contacting via the alpha chain subunits.
CC       The trimers are composed of alpha/beta subunit heterodimers arranged
CC       around a three-fold axis of symmetry. The phycoerythrins also contain a
CC       gamma subunit which is located in the center of the hexamer.
CC       {ECO:0000269|PubMed:8876649}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Stromal side. Note=Forms the periphery of
CC       the phycobilisome rod.
CC   -!- PTM: Contains two covalently linked phycoerythrobilin chromophores. In
CC       PubMed:8876649 the authors refer to the bilins as phycoerythrobilins.
CC       In the PDB entries, the bilins are named as phycocyanobilins although
CC       the modeled compounds correspond to phycoerythrobilins.
CC   -!- MISCELLANEOUS: The light-harvesting antenna system in red algae and
CC       cyanobacteria is formed of phycobilisomes. These are composed of the
CC       phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and
CC       allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin
CC       (PCC). The phycobiliproteins all share the same subunit composition and
CC       organization with variations in the covalently bound open-chain
CC       tetrapyrrole chromophores. The phycobiliprotein complexes are arranged
CC       sequentially in antenna complexes linked by linker proteins with CPE at
CC       the periphery, CPC in the middle and APC at the core feeding to the
CC       photosynthetic reaction center.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000255}.
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DR   PDB; 1LIA; X-ray; 2.80 A; A/K=1-164.
DR   PDB; 3MWN; X-ray; 2.60 A; A=32-164.
DR   PDBsum; 1LIA; -.
DR   PDBsum; 3MWN; -.
DR   AlphaFoldDB; P84861; -.
DR   SMR; P84861; -.
DR   EvolutionaryTrace; P84861; -.
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   Electron transport; Membrane; Photosynthesis; Phycobilisome; Plastid;
KW   Thylakoid; Transport.
FT   CHAIN           1..164
FT                   /note="R-phycoerythrin alpha chain"
FT                   /id="PRO_0000240598"
FT   BINDING         47
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="2"
FT   BINDING         81
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="1"
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         84
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="1"
FT   BINDING         88
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="1"
FT   BINDING         137
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="2"
FT   BINDING         139
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="2"
FT                   /note="covalent, via 1 link"
FT   BINDING         142
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /ligand_label="2"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           21..46
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           48..62
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           76..99
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           103..108
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   TURN            109..112
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           113..119
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           124..137
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:1LIA"
FT   HELIX           146..163
FT                   /evidence="ECO:0007829|PDB:1LIA"
SQ   SEQUENCE   164 AA;  17836 MW;  CD0F348B0EF7716F CRC64;
     MKSVITTTIS AADAAGRYPS TSDLQSVQGN IQRAAARLEA AEKLGSNHEA VVKEAGDACF
     SKYGYNKNPG EAGENQEKIN KCYRDIDHYM RLINYTLVVG GTGPLDEWGI AGAREVYRTL
     NLPSAAYIAA FVFTRDRLCI PRDMSAQAGV EFCTALDYLI NSLS
 
 
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