ID   PEBS_BPPRM              Reviewed;         233 AA.
AC   Q58MU6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   23-FEB-2022, entry version 59.
DE   RecName: Full=Phycoerythrobilin synthase;
DE            EC=1.3.7.6;
DE   AltName: Full=(3Z)-phycoerythrobilin:ferredoxin oxidoreductase;
GN   Name=pebS; ORFNames=PSSM2_058;
OS   Prochlorococcus phage P-SSM2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Salacisavirus; Prochlorococcus virus PSSM2.
OX   NCBI_TaxID=268746;
OH   NCBI_TaxID=1218; Prochlorococcus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15828858; DOI=10.1371/journal.pbio.0030144;
RA   Sullivan M.B., Coleman M.L., Weigele P., Rohwer F., Chisholm S.W.;
RT   "Three Prochlorococcus cyanophage genomes: signature features and
RT   ecological interpretations.";
RL   PLoS Biol. 3:E144-E144(2005).
RN   [2]
RP   CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=18356052; DOI=10.1016/j.cub.2008.02.067;
RA   Dammeyer T., Bagby S.C., Sullivan M.B., Chisholm S.W.,
RA   Frankenberg-Dinkel N.;
RT   "Efficient phage-mediated pigment biosynthesis in oceanic cyanobacteria.";
RL   Curr. Biol. 18:442-448(2008).
CC   -!- FUNCTION: Plays a role in phycoerythrobilin biosynthesis, the red
CC       pigment chromophore photosynthetically active biliproteins of the host
CC       cyanobacteria. Uses a four-electron reduction to carry out the
CC       reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-phycoerythrobilin + 2 oxidized 2[4Fe-4S]-[ferredoxin] =
CC         biliverdin IXalpha + 4 H(+) + 2 reduced 2[4Fe-4S]-[ferredoxin];
CC         Xref=Rhea:RHEA:25359, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC         ChEBI:CHEBI:57438, ChEBI:CHEBI:57991; EC=1.3.7.6;
CC         Evidence={ECO:0000269|PubMed:18356052};
CC   -!- SIMILARITY: Belongs to the HY2 family. {ECO:0000305}.
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; AY939844; AAX44436.1; -; Genomic_DNA.
DR   RefSeq; YP_214290.1; NC_006883.2.
DR   PDB; 2VCK; X-ray; 1.80 A; A/B/C/D=1-233.
DR   PDB; 2VCL; X-ray; 1.55 A; A=1-233.
DR   PDB; 2VGR; X-ray; 2.10 A; A/B/C/D=1-233.
DR   PDB; 2X9I; X-ray; 2.20 A; A/B/C/D=1-233.
DR   PDB; 2X9J; X-ray; 1.85 A; A/B=1-233.
DR   PDBsum; 2VCK; -.
DR   PDBsum; 2VCL; -.
DR   PDBsum; 2VGR; -.
DR   PDBsum; 2X9I; -.
DR   PDBsum; 2X9J; -.
DR   SMR; Q58MU6; -.
DR   GeneID; 3294481; -.
DR   KEGG; vg:3294481; -.
DR   BRENDA; 1.3.7.6; 10990.
DR   EvolutionaryTrace; Q58MU6; -.
DR   Proteomes; UP000000991; Genome.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   GO; GO:0010024; P:phytochromobilin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR009249; Ferredoxin-dep_bilin_Rdtase.
DR   Pfam; PF05996; Fe_bilin_red; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Phycoerythrobilin synthase"
FT                   /id="PRO_0000354064"
FT   HELIX           25..34
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          39..49
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          59..68
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          71..81
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          84..93
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          101..110
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:2VCK"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:2VCK"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           161..167
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           168..185
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           192..195
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:2VCL"
FT   TURN            228..232
FT                   /evidence="ECO:0007829|PDB:2VCL"
SQ   SEQUENCE   233 AA;  27256 MW;  4DAABD1CCF307137 CRC64;
     MTKNPRNNKP KKILDSSYKS KTIWQNYIDA LFETFPQLEI SEVWAKWDGG NVTKDGGDAK
     LTANIRTGEH FLKAREAHIV DPNSDIYNTI LYPKTGADLP CFGMDLMKFS DKKVIIVFDF
     QHPREKYLFS VDGLPEDDGK YRFFEMGNHF SKNIFVRYCK PDEVDQYLDT FKLYLTKYKE
     MIDNNKPVGE DTTVYSDFDT YMTELDPVRG YMKNKFGEGR SEAFVNDFLF SYK