ID   PCYA_PROM5              Reviewed;         241 AA.
AC   A2BW83;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phycocyanobilin:ferredoxin oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00618};
DE            EC=1.3.7.5 {ECO:0000255|HAMAP-Rule:MF_00618};
GN   Name=pcyA {ECO:0000255|HAMAP-Rule:MF_00618}; OrderedLocusNames=P9515_08371;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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       {ECO:0000255|HAMAP-Rule:MF_00618}.
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:0000255|HAMAP-Rule:MF_00618};
CC   -!- SIMILARITY: Belongs to the HY2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00618}.
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; CP000552; ABM72044.1; -; Genomic_DNA.
DR   RefSeq; WP_011820149.1; NC_008817.1.
DR   AlphaFoldDB; A2BW83; -.
DR   SMR; A2BW83; -.
DR   STRING; 167542.P9515_08371; -.
DR   EnsemblBacteria; ABM72044; ABM72044; P9515_08371.
DR   KEGG; pmc:P9515_08371; -.
DR   eggNOG; ENOG502Z7RN; Bacteria.
DR   HOGENOM; CLU_074224_0_0_3; -.
DR   OMA; YQTPQFR; -.
DR   OrthoDB; 1105902at2; -.
DR   Proteomes; UP000001589; 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   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..241
FT                   /note="Phycocyanobilin:ferredoxin oxidoreductase"
FT                   /id="PRO_1000190498"
SQ   SEQUENCE   241 AA;  28173 MW;  2057B6BADB5BBEB7 CRC64;
     MLSESLTKTK LIDPLILTLL QNIRGHRSNL ENLKSIKIDP KLSNIISDKE GKELYIENEF
     HKAKGFRKLH IEVAEFSRRL KILHCVFFPD PHYDIPIFGM DLVKVNEVVS AAIVDLSPSS
     KNQNLKYDNL LSTIDKSVFE SEREIPGWGD IFSQNVFFAS LKNESEKSAF CKIVDHYLLV
     LIKLSKSSIL DHDQEIIQER IDFQKNYCRQ QMKNEKTSLV LLKYFDKKWV DEYIKKVLFD
     F