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Database: UniProt
Entry: CHLB_SYNS9
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ID   CHLB_SYNS9              Reviewed;         541 AA.
AC   Q3AWT5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353};
GN   Name=chlB {ECO:0000255|HAMAP-Rule:MF_00353};
GN   OrderedLocusNames=Syncc9902_1620;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC       (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC       protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC       reaction is light-independent. The NB-protein (ChlN-ChlB) is the
CC       catalytic component of the complex. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC         phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC         4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC         Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC       Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at
CC       the heterodimer interface by residues from both subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00353};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC       ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00353}.
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DR   EMBL; CP000097; ABB26578.1; -; Genomic_DNA.
DR   RefSeq; WP_011360389.1; NC_007513.1.
DR   AlphaFoldDB; Q3AWT5; -.
DR   SMR; Q3AWT5; -.
DR   STRING; 316279.Syncc9902_1620; -.
DR   KEGG; sye:Syncc9902_1620; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025470_0_0_3; -.
DR   OrthoDB; 5717231at2; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR   GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR   Gene3D; 1.20.89.20; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   Gene3D; 1.10.8.550; Proto-chlorophyllide reductase 57 kD subunit B; 1.
DR   HAMAP; MF_00353; ChlB_BchB; 1.
DR   InterPro; IPR013580; LI-POR_suB-like_C.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR042298; P-CP_red_C.
DR   InterPro; IPR005969; Protochl_reductB.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   NCBIfam; TIGR01278; DPOR_BchB; 1.
DR   PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   PIRSF; PIRSF000163; PCP_ChlB; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT   CHAIN           1..541
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B"
FT                   /id="PRO_1000048430"
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT   BINDING         425..426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   541 AA;  59364 MW;  7B07368A8781F74E CRC64;
     MELTLWTYEG PPHVGAMRIA ASMKGVHYVL HAPQGDTYAD LLFTMIERRG KRPPVTYTTF
     QARDLGGDTA ELVKRHIREA VERFKPDALL VGESCTAELI QDQPGALAGG MGFDLPIVSL
     ELPAYSKKEN WGASETLYQL VRGLLKNQEI NSEGHNPKAW QNQGRRPRVN LIGPSLLGFR
     CRDDVIEISR LLASHGIDVN TVVPLEATVA DVMRLTEADL NICLYAEISE SCCSWMERQF
     GMPFSRTMPI GVGATADFLA EVHGLLGMDP PDPREGEHSS KLPWYSASVD STYLTGKRVF
     IFGDGSHVLA AARIANEELG FQVVGLGTYS REMARPVRAA AKELGLEALI SDDYLAVEAA
     MAEAVPELVL GTQMERHSAK RLGIPCAVIS TPMHVQDVPA RFSPQMGWEG ANVIFDSWVH
     PLMMGLEEHL IGMFRHDFEF VDGHQSHLGH LGGLQSAQVE DAPAAIANNS TETHAIEADT
     SSVAVATATL EWTMDGEAEL KKIPFFVRGK VRRNTEAFAK EKGLNQIDSE TLYDAKAHYS
     A
//
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