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