ID   PEBA_PROMP              Reviewed;         236 AA.
AC   Q93SN8;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=15,16-dihydrobiliverdin:ferredoxin oxidoreductase;
DE            EC=1.3.7.2;
GN   Name=pebA; OrderedLocusNames=PMM1593;
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 two-electron reduction of biliverdin IX-alpha
CC       at the C15 methine bridge.
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; AY030300; AAK38141.1; -; Genomic_DNA.
DR   EMBL; BX548174; CAE20052.1; -; Genomic_DNA.
DR   RefSeq; WP_011133221.1; NC_005072.1.
DR   AlphaFoldDB; Q93SN8; -.
DR   SMR; Q93SN8; -.
DR   STRING; 59919.PMM1593; -.
DR   EnsemblBacteria; CAE20052; CAE20052; PMM1593.
DR   KEGG; pmm:PMM1593; -.
DR   eggNOG; ENOG502Z8J9; Bacteria.
DR   HOGENOM; CLU_086208_0_0_3; -.
DR   OMA; FYDANQY; -.
DR   OrthoDB; 846073at2; -.
DR   Proteomes; UP000001026; 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.
FT   CHAIN           1..236
FT                   /note="15,16-dihydrobiliverdin:ferredoxin oxidoreductase"
FT                   /id="PRO_0000216728"
FT   CONFLICT        47
FT                   /note="Q -> R (in Ref. 1; AAK38141)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  28340 MW;  D4F215B59B1282D2 CRC64;
     MFESLKNFVK TNIEDLDGKE LEISKEFKEH HNKDSKYIIK NWIFESQQYR KWRITKLDGG
     DKLQVFNTVA YPNFKSEFPI LGADILWFGT SQKLLAIFDY QPLIQEKKYL QKYCSSLDFI
     KNQYSVFDNH KMKNIYDSKK YFSPWVMICR GNKLNLDRDL NNIFCSFVSN YLTINKLHQN
     NQFLDLEQIK NNQIDYDKYS AEKDPADKLF KTFFGETWTE NFINNFLFTL NHNPLK