ID   PCYA_PROMP              Reviewed;         241 AA.
AC   Q93TL5;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Phycocyanobilin:ferredoxin oxidoreductase;
DE            EC=1.3.7.5;
GN   Name=pcyA; OrderedLocusNames=PMM0747;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
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=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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   -!- 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}.
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DR   EMBL; AF352050; AAK38599.1; -; Genomic_DNA.
DR   EMBL; BX548174; CAE19206.1; -; Genomic_DNA.
DR   RefSeq; WP_011132381.1; NC_005072.1.
DR   AlphaFoldDB; Q93TL5; -.
DR   SMR; Q93TL5; -.
DR   STRING; 59919.PMM0747; -.
DR   EnsemblBacteria; CAE19206; CAE19206; PMM0747.
DR   KEGG; pmm:PMM0747; -.
DR   eggNOG; ENOG502Z7RN; Bacteria.
DR   HOGENOM; CLU_074224_0_0_3; -.
DR   OMA; YQTPQFR; -.
DR   OrthoDB; 1105902at2; -.
DR   Proteomes; UP000001026; 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_0000216743"
SQ   SEQUENCE   241 AA;  28077 MW;  B19E93EB85A45E68 CRC64;
     MLSKSLTKTK LIDPLILTLL QNIKVQRSKL NDLNCIEVDP KLSNIISNEE GKELYIENEF
     YKAKGFRKLH IEVAEFSKSL KILHCVFFPD PKYDIPIFGM DLVKVNELVS AAIVDLSPSS
     KNQNLKYDHL LSHIDKSVFK SKREIPIWGN IFSKNVFFAS LKNESEKNAF CKIVDNYLSV
     LIQLSQSTSP DSDYEIIEER INYQKNYCVQ QMKNEKTSLV LLKYFDKVWV DEYIKKVLFD
     F