位置:首页 > 蛋白库 > APCB_NEOYE
APCB_NEOYE
ID   APCB_NEOYE              Reviewed;         161 AA.
AC   P59857; Q1XDM6;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Allophycocyanin beta chain;
GN   Name=apcB;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CRYSTALLIZATION.
RX   PubMed=9761868; DOI=10.1107/s0907444997017824;
RA   Liu J.-Y., Zhang J.-P., Wan Z.-L., Liang D.-C., Zhang J.-P., Wu H.-J.;
RT   "Crystallization and preliminary X-ray studies of allophycocyanin from red
RT   alga Porphyra yezoensis.";
RL   Acta Crystallogr. D 54:662-664(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH APCA AND
RP   PHYCOCYANOBILIN, AND SUBUNIT.
RX   PubMed=10358042; DOI=10.1074/jbc.274.24.16945;
RA   Liu J.-Y., Jiang T., Zhang J.-P., Liang D.-C.;
RT   "Crystal structure of allophycocyanin from red algae Porphyra yezoensis at
RT   2.2-A resolution.";
RL   J. Biol. Chem. 274:16945-16952(1999).
CC   -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC       protein from the phycobiliprotein complex.
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:10358042}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Stromal side. Note=Forms the core of the
CC       phycobilisome.
CC   -!- PTM: Contains one covalently linked phycocyanobilin chromophore.
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. Allophycocyanin has a maximum
CC       absorption at approximately 650 nanometers.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
CC   -!- CAUTION: Neither a protein sequence nor a nucleotide sequence has been
CC       determined for this protein. This is the sequence of a model fit to
CC       electron density plots at 2.2 Angstroms resolution. The N-
CC       methylasparagine modification was omitted in the model. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006715; BAE92385.1; -; Genomic_DNA.
DR   RefSeq; YP_536942.1; NC_007932.1.
DR   PDB; 1KN1; X-ray; 2.20 A; B=1-161.
DR   PDBsum; 1KN1; -.
DR   AlphaFoldDB; P59857; -.
DR   SMR; P59857; -.
DR   GeneID; 3978964; -.
DR   EvolutionaryTrace; P59857; -.
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   CDD; cd12126; APC_beta; 1.
DR   Gene3D; 1.10.490.20; -; 1.
DR   InterPro; IPR006245; ApcB.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012128; Phycobilisome_asu/bsu.
DR   InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR   PANTHER; PTHR34011:SF3; PTHR34011:SF3; 1.
DR   Pfam; PF00502; Phycobilisome; 1.
DR   PIRSF; PIRSF000081; Phycocyanin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   TIGRFAMs; TIGR01337; apcB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW   Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW   Plastid; Thylakoid; Transport.
FT   CHAIN           1..161
FT                   /note="Allophycocyanin beta chain"
FT                   /id="PRO_0000199101"
FT   BINDING         66
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /evidence="ECO:0000269|PubMed:10358042"
FT   BINDING         71
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /evidence="ECO:0000269|PubMed:10358042"
FT   BINDING         76
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /evidence="ECO:0000269|PubMed:10358042"
FT   BINDING         81..84
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT   BINDING         81
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000269|PubMed:10358042"
FT   MOD_RES         71
FT                   /note="N4-methylasparagine"
FT                   /evidence="ECO:0000250"
FT   HELIX           4..13
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           21..46
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           48..59
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           75..98
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           102..107
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           112..119
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           123..141
FT                   /evidence="ECO:0007829|PDB:1KN1"
FT   HELIX           143..160
FT                   /evidence="ECO:0007829|PDB:1KN1"
SQ   SEQUENCE   161 AA;  17484 MW;  C94F17EE5BF694D3 CRC64;
     MQDAITSVIN AADVQGKYLD DSSVEKLRGY FQTGELRVRA AATIAANAAT IIKESVAKSL
     LYSDITRPGG NMYTTRRYAA CIRDLDYYLR YATYGMLAGD PSILEERVLN GLKETYNSLG
     VPIGATIQAI LAMKEVTISL VGPDAGKEMG LYFDYICSGL S
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024