PCYA_SYNY3
ID PCYA_SYNY3 Reviewed; 248 AA.
AC Q55891;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phycocyanobilin:ferredoxin oxidoreductase;
DE EC=1.3.7.5;
GN Name=pcyA; OrderedLocusNames=slr0116;
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=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the four-electron reduction of biliverdin IX-alpha
CC (2-electron reduction at both the A and D rings); the reaction proceeds
CC via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3Z)-phycocyanobilin + 4 oxidized [2Fe-2S]-[ferredoxin] =
CC biliverdin IXalpha + 4 H(+) + 4 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:15309, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57437, ChEBI:CHEBI:57991; EC=1.3.7.5;
CC -!- SIMILARITY: Belongs to the HY2 family. {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; BA000022; BAA10653.1; -; Genomic_DNA.
DR PIR; S76709; S76709.
DR PDB; 2D1E; X-ray; 1.51 A; A=1-248.
DR PDB; 2DKE; X-ray; 2.50 A; A=1-248.
DR PDB; 3AJG; X-ray; 1.90 A; A/B=1-248.
DR PDB; 3AJH; X-ray; 2.25 A; A/B=1-248.
DR PDB; 3F0L; X-ray; 1.30 A; A=1-248.
DR PDB; 3F0M; X-ray; 1.50 A; A=1-248.
DR PDB; 3I8U; X-ray; 1.48 A; X=1-248.
DR PDB; 3I94; X-ray; 1.04 A; A=1-248.
DR PDB; 3I95; X-ray; 1.40 A; A=1-248.
DR PDB; 3NB8; X-ray; 1.30 A; A=1-248.
DR PDB; 3NB9; X-ray; 1.50 A; A=1-248.
DR PDB; 4EOC; X-ray; 1.49 A; A=8-246.
DR PDB; 4EOD; X-ray; 1.30 A; A=1-248.
DR PDB; 4EOE; X-ray; 1.20 A; A=1-248.
DR PDB; 4QCD; Other; 1.93 A; A=1-248.
DR PDB; 5B4H; X-ray; 1.11 A; A=1-248.
DR PDB; 5B4I; X-ray; 1.11 A; A=1-248.
DR PDB; 5B4J; X-ray; 1.05 A; A=1-248.
DR PDBsum; 2D1E; -.
DR PDBsum; 2DKE; -.
DR PDBsum; 3AJG; -.
DR PDBsum; 3AJH; -.
DR PDBsum; 3F0L; -.
DR PDBsum; 3F0M; -.
DR PDBsum; 3I8U; -.
DR PDBsum; 3I94; -.
DR PDBsum; 3I95; -.
DR PDBsum; 3NB8; -.
DR PDBsum; 3NB9; -.
DR PDBsum; 4EOC; -.
DR PDBsum; 4EOD; -.
DR PDBsum; 4EOE; -.
DR PDBsum; 4QCD; -.
DR PDBsum; 5B4H; -.
DR PDBsum; 5B4I; -.
DR PDBsum; 5B4J; -.
DR AlphaFoldDB; Q55891; -.
DR SMR; Q55891; -.
DR IntAct; Q55891; 1.
DR STRING; 1148.1208485; -.
DR PaxDb; Q55891; -.
DR EnsemblBacteria; BAA10653; BAA10653; BAA10653.
DR KEGG; syn:slr0116; -.
DR eggNOG; ENOG502Z7RN; Bacteria.
DR InParanoid; Q55891; -.
DR OMA; YQTPQFR; -.
DR PhylomeDB; Q55891; -.
DR BioCyc; MetaCyc:MON-13954; -.
DR BRENDA; 1.3.7.5; 382.
DR EvolutionaryTrace; Q55891; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0050620; F:phycocyanobilin:ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010024; P:phytochromobilin biosynthetic process; IEA:InterPro.
DR HAMAP; MF_00618; Ferredoxin_bilin_red; 1.
DR InterPro; IPR009249; Ferredoxin-dep_bilin_Rdtase.
DR InterPro; IPR022870; Ferredoxin_bilin_OxRdtase.
DR PANTHER; PTHR34557; PTHR34557; 1.
DR Pfam; PF05996; Fe_bilin_red; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..248
FT /note="Phycocyanobilin:ferredoxin oxidoreductase"
FT /id="PRO_0000216747"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 68..80
FT /evidence="ECO:0007829|PDB:3I94"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3AJH"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:3I94"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 170..193
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3I94"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:3I94"
SQ SEQUENCE 248 AA; 28129 MW; BEB10CEBCE5E515B CRC64;
MAVTDLSLTN SSLMPTLNPM IQQLALAIAA SWQSLPLKPY QLPEDLGYVE GRLEGEKLVI
ENRCYQTPQF RKMHLELAKV GKGLDILHCV MFPEPLYGLP LFGCDIVAGP GGVSAAIADL
SPTQSDRQLP AAYQKSLAEL GQPEFEQQRE LPPWGEIFSE YCLFIRPSNV TEEERFVQRV
VDFLQIHCHQ SIVAEPLSEA QTLEHRQGQI HYCQQQQKND KTRRVLEKAF GEAWAERYMS
QVLFDVIQ