PEBA_SYNPY
ID PEBA_SYNPY Reviewed; 236 AA.
AC Q02189;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=15,16-dihydrobiliverdin:ferredoxin oxidoreductase;
DE EC=1.3.7.2;
GN Name=pebA;
OS Synechococcus sp. (strain WH8020).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32052;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8425055; DOI=10.1007/bf00019939;
RA de Lorimier R., Wilbanks S.M., Glazer A.N.;
RT "Genes of the R-phycocyanin II locus of marine Synechococcus spp., and
RT comparison of protein-chromophore interactions in phycocyanins differing in
RT bilin composition.";
RL Plant Mol. Biol. 21:225-237(1993).
RN [2]
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).
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 ---------------------------------------------------------------------------
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; M95288; AAA27343.1; -; Genomic_DNA.
DR EMBL; AF400984; AAK77915.1; -; Genomic_DNA.
DR PIR; S31058; S31058.
DR RefSeq; WP_048347955.1; NZ_CP011941.1.
DR PDB; 2X9O; X-ray; 1.55 A; A=2-236.
DR PDBsum; 2X9O; -.
DR AlphaFoldDB; Q02189; -.
DR SMR; Q02189; -.
DR STRING; 32052.WB44_13640; -.
DR BioCyc; MetaCyc:MON-13950; -.
DR BRENDA; 1.3.7.2; 6187.
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 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase.
FT CHAIN 1..236
FT /note="15,16-dihydrobiliverdin:ferredoxin oxidoreductase"
FT /id="PRO_0000216730"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2X9O"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:2X9O"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2X9O"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 160..178
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:2X9O"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:2X9O"
SQ SEQUENCE 236 AA; 27245 MW; 27CFCEBF17B50D8D CRC64;
MFDSFLNELH SDITKRGGSP LPLPEGLEEC RSSKSSSVIQ SWLWDVPGFR RWRVTRLDAG
DSLQVFNSVA YPDYNYDHPL MGVDLLWFGA RQKLVAVLDF QPLVQDKDYL DRYFSGLKEL
NQRFPDLNGE ETMRSFDPNQ YFSSWLLFCR GGAEQADLSL PKAFSAFLKA YWDLHDNAKS
IPSTIPPEEV KNLQDKYDIY SAERDPAHGL FTSHFGKDWS NRFLHEFLFP ASSSHK
