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B-phycoerythrin beta chain

 PHEB_RHDS2              Reviewed;         177 AA.
P27198;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
22-NOV-2017, entry version 94.
RecName: Full=B-phycoerythrin beta chain;
Name=cpeB;
Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24)).
Plastid; Chloroplast.
Eukaryota; Cryptophyta; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
NCBI_TaxID=79257;
[1]
PROTEIN SEQUENCE.
PubMed=1554738; DOI=10.1016/0167-4838(92)90432-D;
Godovac-Zimmermann J., Sheil M., Wrench P.M., Hiller R.G.;
"Amino acid sequence of the beta-subunit of phycoerythrin from the
cryptophyte algae Chroomonas CS 24.";
Biochim. Biophys. Acta 1120:117-121(1992).
[2]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3
AND PHYCOERYTHROBILIN, SUBUNIT, AND METHYLATION AT ASN-72.
PubMed=10430868; DOI=10.1073/pnas.96.16.8901;
Wilk K.E., Harrop S.J., Jankova L., Edler D., Keenan G., Sharples F.,
Hiller R.G., Curmi P.M.;
"Evolution of a light-harvesting protein by addition of new subunits
and rearrangement of conserved elements: crystal structure of a
cryptophyte phycoerythrin at 1.63-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 96:8901-8906(1999).
[3]
X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3
AND PHYCOERYTHROBILIN, SUBUNIT, AND METHYLATION AT ASN-72.
PubMed=15504407; DOI=10.1016/j.jmb.2004.09.044;
Doust A.B., Marai C.N., Harrop S.J., Wilk K.E., Curmi P.M.,
Scholes G.D.;
"Developing a structure-function model for the cryptophyte
phycoerythrin 545 using ultrahigh resolution crystallography and
ultrafast laser spectroscopy.";
J. Mol. Biol. 344:135-153(2004).
-!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole
chromophore-protein from the phycobiliprotein complex.
-!- SUBUNIT: Heterotetramer of 2 different alpha chains and 2
identical beta chains. The subunit composition could comprise any
combination of 2 out of 4 different alpha units with an invariant
beta unit. {ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
Peripheral membrane protein; Lumenal side.
-!- PTM: Contains three covalently linked phycoerythrobilin
chromophores.
-!- MISCELLANEOUS: The light-harvesting system in Cryptophytes
contains phycobiliprotein complexes. Unusually they are composed
of either phycoerythrin (CPE) or phycocyanin (CPC) but never
allophycocyanin (APC), with only one type of biliprotein being
present in any one species. Unlike cyanobacteria or red algae
these proteins are not arranged into higher-order phycobilisome
complexes, and they are found in the thylakoid lumen.
-!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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PDB; 1QGW; X-ray; 1.63 A; C/D=1-177.
PDB; 1XF6; X-ray; 1.10 A; C/D=1-177.
PDB; 1XG0; X-ray; 0.97 A; C/D=1-177.
PDBsum; 1QGW; -.
PDBsum; 1XF6; -.
PDBsum; 1XG0; -.
ProteinModelPortal; P27198; -.
SMR; P27198; -.
iPTMnet; P27198; -.
EvolutionaryTrace; P27198; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0030089; C:phycobilisome; IEA:InterPro.
GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR012128; Phycobilisome_asu/bsu.
Pfam; PF00502; Phycobilisome; 1.
PIRSF; PIRSF000081; Phycocyanin; 1.
SUPFAM; SSF46458; SSF46458; 1.
1: Evidence at protein level;
3D-structure; Bile pigment; Chloroplast; Chromophore;
Direct protein sequencing; Electron transport; Membrane; Methylation;
Photosynthesis; Plastid; Thylakoid; Transport.
CHAIN 1 177 B-phycoerythrin beta chain.
/FTId=PRO_0000199200.
REGION 77 78 Phycoerythrobilin chromophore 2 binding.
REGION 82 82 Phycoerythrobilin chromophore 2 binding.
REGION 147 148 Phycoerythrobilin chromophore 1 binding.
REGION 154 158 Phycoerythrobilin chromophore 3 binding.
BINDING 28 28 Phycoerythrobilin chromophore 3.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 35 35 Phycoerythrobilin chromophore 3.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 39 39 Phycoerythrobilin chromophore 3.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 50 50 Phycoerythrobilin chromophore 1
(covalent; via 2 links).
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 54 54 Phycoerythrobilin chromophore 1.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 61 61 Phycoerythrobilin chromophore 1
(covalent; via 2 links).
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 72 72 Phycoerythrobilin chromophore 2.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 82 82 Phycoerythrobilin chromophore 2
(covalent; via 1 link).
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 129 129 Phycoerythrobilin chromophore 1.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
BINDING 158 158 Phycoerythrobilin chromophore 3
(covalent; via 1 link).
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
MOD_RES 72 72 N4-methylasparagine.
{ECO:0000269|PubMed:10430868,
ECO:0000269|PubMed:15504407}.
CONFLICT 50 50 C -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 V -> Y (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 C -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 65 65 S -> H (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 73 73 C -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 4 9 {ECO:0000244|PDB:1XG0}.
STRAND 17 20 {ECO:0000244|PDB:1XG0}.
HELIX 22 30 {ECO:0000244|PDB:1XG0}.
HELIX 34 45 {ECO:0000244|PDB:1XG0}.
HELIX 48 62 {ECO:0000244|PDB:1XG0}.
HELIX 64 67 {ECO:0000244|PDB:1XG0}.
HELIX 76 99 {ECO:0000244|PDB:1XG0}.
HELIX 103 108 {ECO:0000244|PDB:1XG0}.
TURN 109 112 {ECO:0000244|PDB:1XG0}.
HELIX 113 120 {ECO:0000244|PDB:1XG0}.
HELIX 124 142 {ECO:0000244|PDB:1XG0}.
STRAND 146 148 {ECO:0000244|PDB:1XG0}.
HELIX 159 176 {ECO:0000244|PDB:1XG0}.
SEQUENCE 177 AA; 18508 MW; 51008EFCF1D7C717 CRC64;
MLDAFSRVVT NADSKAAYVG GADLQALKKF ISEGNKRLDS VNSIVSNASC IVSDAVSGMI
CENPSLISPS GNCYTNRRMA ACLRDGEIIL RYVSYALLSG DASVLEDRCL NGLKETYSSL
GVPANSNARA VSIMKACAVA FVNNTASQKK LSTPQGDCSG LASEVGGYFD KVTAAIS


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