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PCYA_NOSS1
ID   PCYA_NOSS1              Reviewed;         245 AA.
AC   Q93TN0;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phycocyanobilin:ferredoxin oxidoreductase;
DE            Short=PCB:ferredoxin oxidoreductase;
DE            EC=1.3.7.5;
GN   Name=pcyA; OrderedLocusNames=alr3707;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11283349; DOI=10.2307/3871353;
RA   Frankenberg N., Mukougawa K., Kohchi T., Lagarias J.C.;
RT   "Functional genomic analysis of the HY2 family of ferredoxin-dependent
RT   bilin reductases from oxygenic photosynthetic organisms.";
RL   Plant Cell 13:965-978(2001).
RN   [2]
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   [3]
RP   FUNCTION.
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=16452471; DOI=10.1074/jbc.m513796200;
RA   Zhao K.H., Su P., Li J., Tu J.M., Zhou M., Bubenzer C., Scheer H.;
RT   "Chromophore attachment to phycobiliprotein beta-subunits:
RT   phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-
RT   like protein from Anabaena Sp. PCC7120.";
RL   J. Biol. Chem. 281:8573-8581(2006).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-245, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF HIS-71 AND GLU-73.
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=17279614; DOI=10.1021/bi062038f;
RA   Tu S.L., Rockwell N.C., Lagarias J.C., Fisher A.J.;
RT   "Insight into the radical mechanism of phycocyanobilin-ferredoxin
RT   oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical
RT   measurements.";
RL   Biochemistry 46:1484-1494(2007).
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       Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS
CC       and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB
CC       or PecB. {ECO:0000269|PubMed:16452471}.
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         Evidence={ECO:0000269|PubMed:17279614};
CC   -!- SIMILARITY: Belongs to the HY2 family. {ECO:0000305}.
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DR   EMBL; AF339056; AAK38587.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB75406.1; -; Genomic_DNA.
DR   PIR; AD2269; AD2269.
DR   RefSeq; WP_010997850.1; NZ_RSCN01000007.1.
DR   PDB; 2G18; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-245.
DR   PDBsum; 2G18; -.
DR   AlphaFoldDB; Q93TN0; -.
DR   SMR; Q93TN0; -.
DR   STRING; 103690.17132841; -.
DR   EnsemblBacteria; BAB75406; BAB75406; BAB75406.
DR   KEGG; ana:alr3707; -.
DR   eggNOG; ENOG502Z7RN; Bacteria.
DR   OMA; YQTPQFR; -.
DR   OrthoDB; 1105902at2; -.
DR   BioCyc; MetaCyc:MON-18997; -.
DR   BRENDA; 1.3.7.5; 8113.
DR   EvolutionaryTrace; Q93TN0; -.
DR   Proteomes; UP000002483; 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..245
FT                   /note="Phycocyanobilin:ferredoxin oxidoreductase"
FT                   /id="PRO_0000216738"
FT   MUTAGEN         71
FT                   /note="H->Q: Has 5% bilin reductase activity."
FT                   /evidence="ECO:0000269|PubMed:17279614"
FT   MUTAGEN         73
FT                   /note="E->Q: Has 20% bilin reductase activity, only the
FT                   two-electron reduction of the A ring occurs."
FT                   /evidence="ECO:0000269|PubMed:17279614"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           15..31
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          53..63
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          65..77
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          109..118
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           167..190
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           196..216
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           219..227
FT                   /evidence="ECO:0007829|PDB:2G18"
FT   HELIX           229..238
FT                   /evidence="ECO:0007829|PDB:2G18"
SQ   SEQUENCE   245 AA;  27959 MW;  8F6CE652EFEE011A CRC64;
     MSLTSIPSLR EQQHPLIRQL ADCIEEVWHQ HLDLSPYHLP AELGYVEGRL EGEKLTIENR
     CYQTPQFRKM HLELAKVGNM LDILHCVMFP RPEYDLPMFG CDLVGGRGQI SAAIADLSPV
     HLDRTLPESY NSALTSLNTL NFSQPRELPE WGNIFSDFCI FVRPSSPEEE AMFLGRVREF
     LQVHCQGAIA ASPVSAEQKQ QILAGQHNYC SKQQQNDKTR RVLEKAFGVD WAENYMTTVL
     FDLPE
 
 
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