ID   APCD_SYNY3              Reviewed;         161 AA.
AC   P72870;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Allophycocyanin subunit alpha-B;
GN   Name=apcD; OrderedLocusNames=sll0928;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RA   Ashby M.K., Mullineaux C.W.;
RT   "The role of ApcD and ApcF in energy transfer from phycobilisomes to PS I
RT   and PS II in a cyanobacterium.";
RL   Photosyn. Res. 61:169-179(1999).
CC   -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC       phycobiliprotein complex. Allophycocyanin has a maximum absorption at
CC       approximately 654 nanometers (By similarity). {ECO:0000250,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Heterohexamer of two alpha chains, one alpha-B chain and three
CC       beta chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=Forms the core of the phycobilisome.
CC       {ECO:0000250}.
CC   -!- PTM: Contains one covalently linked bilin chromophore. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Increased levels of phycobilisomes (PBS) and
CC       photosystem I (PSI), decreased levels of photosystem II (PSII) per
CC       cell. Cells are unable to undergo state transitions. When combined with
CC       an ApcF deletion mutant the cells have decreased PBS, PSI and PSII, and
CC       require glucose to grow. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA16886.1; -; Genomic_DNA.
DR   PIR; S74735; S74735.
DR   PDB; 4PO5; X-ray; 1.75 A; A/C/E=1-161.
DR   PDBsum; 4PO5; -.
DR   AlphaFoldDB; P72870; -.
DR   SMR; P72870; -.
DR   STRING; 1148.1651960; -.
DR   PaxDb; P72870; -.
DR   EnsemblBacteria; BAA16886; BAA16886; BAA16886.
DR   KEGG; syn:sll0928; -.
DR   eggNOG; ENOG502Z81S; Bacteria.
DR   InParanoid; P72870; -.
DR   OMA; LIGVREM; -.
DR   PhylomeDB; P72870; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; Chromophore;
KW   Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW   Reference proteome; Thylakoid; Transport.
FT   CHAIN           1..161
FT                   /note="Allophycocyanin subunit alpha-B"
FT                   /id="PRO_0000403177"
FT   BINDING         81
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="N4-methylasparagine"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           20..30
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           47..61
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           75..98
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           123..138
FT                   /evidence="ECO:0007829|PDB:4PO5"
FT   HELIX           143..161
FT                   /evidence="ECO:0007829|PDB:4PO5"
SQ   SEQUENCE   161 AA;  17923 MW;  C9309E2B7F69D713 CRC64;
     MSVVSQVILQ ADDQLRYPTS GELKGIQAFL TTGAQRIRIA ETLAENEKKI VDQAQKQLFK
     KHPEYRAPGG NAYGQRQYNQ CLRDYGWYLR LVTYGVLAGN KEPIETTGLI GVKEMYNSLN
     VPVPGMVDAV TVLKDAALGL LSAEDANETA PYFDYIIQFM S