ID   CPCE_SYNP2              Reviewed;         268 AA.
AC   P31967; B1XIU2;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Phycocyanobilin lyase subunit alpha;
DE            EC=4.-.-.-;
DE   AltName: Full=Phycocyanin operon protein CpcE;
GN   Name=cpcE; OrderedLocusNames=SYNPCC7002_A2213;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=1644801; DOI=10.1016/s0021-9258(18)41978-3;
RA   Zhou J., Gasparich G.E., Stirewalt V.L., de Lorimier R., Bryant D.A.;
RT   "The cpcE and cpcF genes of Synechococcus sp. PCC 7002. Construction and
RT   phenotypic characterization of interposon mutants.";
RL   J. Biol. Chem. 267:16138-16145(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1495995; DOI=10.1073/pnas.89.15.7017;
RA   Fairchild C.D., Zhao J., Zhou J., Colson S.E., Bryant D.A., Glazer A.N.;
RT   "Phycocyanin alpha-subunit phycocyanobilin lyase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7017-7021(1992).
CC   -!- FUNCTION: Required for the chromophorylation of the cpcA gene product.
CC   -!- SUBUNIT: CpcE and CpcF associate to form a lyase.
CC   -!- SIMILARITY: Belongs to the CpcE/RpcE/PecE family. {ECO:0000305}.
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DR   EMBL; M93569; AAA27308.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACB00194.1; -; Genomic_DNA.
DR   RefSeq; WP_012307812.1; NC_010475.1.
DR   AlphaFoldDB; P31967; -.
DR   SMR; P31967; -.
DR   STRING; 32049.SYNPCC7002_A2213; -.
DR   EnsemblBacteria; ACB00194; ACB00194; SYNPCC7002_A2213.
DR   KEGG; syp:SYNPCC7002_A2213; -.
DR   eggNOG; COG1413; Bacteria.
DR   HOGENOM; CLU_1010860_0_0_3; -.
DR   OMA; AWWLGKF; -.
DR   BRENDA; 4.4.1.32; 6187.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   Pfam; PF03130; HEAT_PBS; 2.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Antenna complex; Lyase; Phycobilisome; Reference proteome.
FT   CHAIN           1..268
FT                   /note="Phycocyanobilin lyase subunit alpha"
FT                   /id="PRO_0000199270"
FT   CONFLICT        173
FT                   /note="R -> P (in Ref. 1; AAA27308)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  29233 MW;  9AD7AFC6A301D1DA CRC64;
     MSDWQMAEAW TLEEAIANIQ QTEDTGKRYY AAWWFGKFRV QDERAVNALL AALKDETDRS
     PDGGYPLRRN AAKALGKLGN LAAVQPLIES LESPDYYVRE SAAQSLEMLG DRQAIPALQA
     LLAGGVAAAV KAEGKPHLVQ PYEAVIEALG TIGATAAIAE IEPFLDHEFA KIRYAALRAL
     YQLTQEAHYA EQLMEALNGN QLQLRRSALL DLGAIGYVPA GQAIAKAYAE NSLKLISLKG
     ILESHLQRTA ETLDADGLQL LELMDSLL