ID CPCT_NOSS1 Reviewed; 199 AA.
AC Q8YLF9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Phycocyanobilin lyase CpcT;
DE EC=4.-.-.-;
GN Name=cpcT1; Synonyms=cpeT1; OrderedLocusNames=all5339;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP FUNCTION AS A CHROMOPHORE LYASE, AND INDUCTION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17895251; DOI=10.1074/jbc.m703038200;
RA Zhao K.H., Zhang J., Tu J.M., Bohm S., Ploscher M., Eichacker L.,
RA Bubenzer C., Scheer H., Wang X., Zhou M.;
RT "Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and
RT sequential reconstitution of binding sites of phycoerythrocyanin and
RT phycocyanin beta-subunits.";
RL J. Biol. Chem. 282:34093-34103(2007).
RN [3]
RP SUBSTRATE SPECIFICITY.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17726096; DOI=10.1073/pnas.0706209104;
RA Zhao K.H., Su P., Tu J.M., Wang X., Liu H., Ploscher M., Eichacker L.,
RA Yang B., Zhou M., Scheer H.;
RT "Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for
RT cysteine-84-binding sites in cyanobacterial phycobiliproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14300-14305(2007).
CC -!- FUNCTION: Catalyzes the site-selective attachment of phycocyanobilin
CC (PCB) to 'Cys-154' of C-phycocyanin subunit beta (CpcB) and to 'Cys-
CC 153' of phycoerythrocyanin subunit beta (PecB). Does not have
CC chromophore lyase activity for ApcA1, ApcA2, ApcB, ApcD, ApcF or PecA.
CC {ECO:0000269|PubMed:17895251}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:17895251}.
CC -!- SIMILARITY: Belongs to the CpcT/CpeT biliprotein lyase family.
CC {ECO:0000305}.
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DR EMBL; BA000019; BAB77038.1; -; Genomic_DNA.
DR PIR; AC2473; AC2473.
DR RefSeq; WP_010999463.1; NZ_RSCN01000005.1.
DR PDB; 4O4O; X-ray; 1.95 A; A/B=1-199.
DR PDB; 4O4S; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-199.
DR PDBsum; 4O4O; -.
DR PDBsum; 4O4S; -.
DR AlphaFoldDB; Q8YLF9; -.
DR SMR; Q8YLF9; -.
DR STRING; 103690.gene:10497401; -.
DR KEGG; ana:all5339; -.
DR eggNOG; ENOG502Z877; Bacteria.
DR OrthoDB; 509174at2; -.
DR BioCyc; MetaCyc:MONOMER-18987; -.
DR BRENDA; 4.4.1.30; 4371.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017009; P:protein-phycocyanobilin linkage; IDA:UniProtKB.
DR CDD; cd16338; CpcT; 1.
DR Gene3D; 2.40.128.590; CpcT/CpeT domain; 1.
DR HAMAP; MF_01460; Chrphore_lyase_CpxT; 1.
DR InterPro; IPR010404; CpcT/CpeT.
DR InterPro; IPR038672; CpcT/CpeT_sf.
DR PANTHER; PTHR35137; CHROMOPHORE LYASE CRL, CHLOROPLASTIC; 1.
DR PANTHER; PTHR35137:SF1; CHROMOPHORE LYASE CRL, CHLOROPLASTIC; 1.
DR Pfam; PF06206; CpeT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..199
FT /note="Phycocyanobilin lyase CpcT"
FT /id="PRO_0000403160"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4O4O"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4O4O"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4O4O"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:4O4O"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4O4O"
SQ SEQUENCE 199 AA; 22870 MW; 144FFBFD85065AA5 CRC64;
MTHSTDIATL ARWMAADFSN QAQAFENPPF YAHIRVCMRP LPWEVLSGVG FFVEQAYDYM
LNDPYRLRVL KLMIVGDRIH IENYTVKQEE NFYGASRDLN RLQTLTSESL EKLPGCNMIV
EWTGNSFKGT VEPGKGCIVV RKGQKTYLDS EFEINEEKFI SLDRGRDLET DAHIWGSVAG
PFYFVRLHNF ADEVKISAE
//
