ID   PEBA_NOSP7              Reviewed;         244 AA.
AC   Q93TL6; B2J9I3;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=15,16-dihydrobiliverdin:ferredoxin oxidoreductase;
DE            EC=1.3.7.2;
GN   Name=pebA; OrderedLocusNames=Npun_R0730;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
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=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK38598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACC79482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF352049; AAK38598.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001037; ACC79482.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041565166.1; NC_010628.1.
DR   AlphaFoldDB; Q93TL6; -.
DR   SMR; Q93TL6; -.
DR   STRING; 63737.Npun_R0730; -.
DR   EnsemblBacteria; ACC79482; ACC79482; Npun_R0730.
DR   KEGG; npu:Npun_R0730; -.
DR   eggNOG; ENOG502Z8J9; Bacteria.
DR   HOGENOM; CLU_086208_0_0_3; -.
DR   OMA; FYDANQY; -.
DR   OrthoDB; 846073at2; -.
DR   PhylomeDB; Q93TL6; -.
DR   BRENDA; 1.3.7.2; 4370.
DR   Proteomes; UP000001191; 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..244
FT                   /note="15,16-dihydrobiliverdin:ferredoxin oxidoreductase"
FT                   /id="PRO_0000216725"
SQ   SEQUENCE   244 AA;  28844 MW;  ED2BC4214AE2D22E CRC64;
     MYKPFLEFLE KELFQRFDLQ SRVIPPGLEF KVSDRGRNPA TIRSWCYQSQ ELRKIRYTYI
     DAGESAQIFN SVVYPSHNYD LPLLGIDFLS FGKVKNLIVL DFQPLFQDED YQNKYIAPLK
     YLHNKYPDLA QNLEMKFYDA NQYFSKYLLF AKTDAETVST RVFEAFQDYL NLYWQMLADA
     QALHDPEDIQ RIVKAQKDYD QYSADRDPAS GLFSSYFGHE WAERFLHEFL FEDAVPLAVS
     ASKR