ID   PEBA_PROMA              Reviewed;         241 AA.
AC   Q9K4U6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=15,16-dihydrobiliverdin:ferredoxin oxidoreductase;
DE            EC=1.3.7.2;
GN   Name=pebA; OrderedLocusNames=Pro_1749;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RA   Irlbacher H.M., Hess W.R.;
RT   "Organization of the ORF241/257 coding region from Prochlorococcus marinus
RT   SS120.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC   -!- FUNCTION: Catalyzes the two-electron reduction of biliverdin IX-alpha
CC       at the C15 methine bridge. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15,16-dihydrobiliverdin + oxidized 2[4Fe-4S]-[ferredoxin] =
CC         biliverdin IXalpha + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin];
CC         Xref=Rhea:RHEA:10168, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC         ChEBI:CHEBI:57899, ChEBI:CHEBI:57991; EC=1.3.7.2;
CC   -!- SIMILARITY: Belongs to the HY2 family. {ECO:0000305}.
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DR   EMBL; AJ278499; CAB95700.1; -; Genomic_DNA.
DR   EMBL; AE017126; AAQ00793.1; -; Genomic_DNA.
DR   RefSeq; NP_876140.3; NC_005042.1.
DR   RefSeq; WP_024015424.1; NC_005042.1.
DR   AlphaFoldDB; Q9K4U6; -.
DR   SMR; Q9K4U6; -.
DR   STRING; 167539.Pro_1749; -.
DR   EnsemblBacteria; AAQ00793; AAQ00793; Pro_1749.
DR   GeneID; 54201076; -.
DR   KEGG; pma:Pro_1749; -.
DR   PATRIC; fig|167539.5.peg.1847; -.
DR   eggNOG; ENOG502Z8J9; Bacteria.
DR   HOGENOM; CLU_086208_0_0_3; -.
DR   OMA; FYDANQY; -.
DR   OrthoDB; 846073at2; -.
DR   Proteomes; UP000001420; Chromosome.
DR   GO; GO:0050617; F:15,16-dihydrobiliverdin:ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0010024; P:phytochromobilin biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00792; PebA; 1.
DR   InterPro; IPR023658; DiHydbiliverdin_OxRdtase.
DR   InterPro; IPR009249; Ferredoxin-dep_bilin_Rdtase.
DR   PANTHER; PTHR34557; PTHR34557; 1.
DR   Pfam; PF05996; Fe_bilin_red; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..241
FT                   /note="15,16-dihydrobiliverdin:ferredoxin oxidoreductase"
FT                   /id="PRO_0000216726"
SQ   SEQUENCE   241 AA;  28699 MW;  4569F322DC35BBFC CRC64;
     MNKLMLQDLH NNLKRRIISH GGKPIEVENG MSERFSHKQD TVIKSWLWDV PGFRRWRVTR
     MDAGDKLQVL NSVAYPAYTN DKPILGIDIL WFGLKRKLVA VLDFQPLVQE ERYFCRYYKD
     LQILKNRFVD FNSQKTMKIY DSNKYFSPWV LLYNGSFDDL QCSLAKILDE FLHAYWQVDN
     NNSREYIKII PSKVEQLHIN YDIYSAERDP AHGLFKSYFG QTWADQFVRE FLFPHSHLTA
     D