CHLB_SYNR3
ID CHLB_SYNR3 Reviewed; 527 AA.
AC A5GUA9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=SynRCC307_1565;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK28468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CT978603; CAK28468.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043737035.1; NC_009482.1.
DR AlphaFoldDB; A5GUA9; -.
DR SMR; A5GUA9; -.
DR STRING; 316278.SynRCC307_1565; -.
DR EnsemblBacteria; CAK28468; CAK28468; SynRCC307_1565.
DR KEGG; syr:SynRCC307_1565; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_3; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000001115; 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; 1.10.8.550; -; 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 Pfam; PF00148; Oxidored_nitro; 1.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR TIGRFAMs; TIGR01278; DPOR_BchB; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000324045"
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 527 AA; 58275 MW; 1C30949DE336378B CRC64;
MELTLWTYEG PPHVGAMRIA ASMQGVHYVL HAPQGDTYAD LLFTMIERRD QRPPVTYTTF
QARDLGGDTA ELVKRSIRDA ADRFQPQALL VGESCTAELI QDQPGALAQG MNLPMPVVSL
ELPAYSKKEN WGAAETFYQL IRTLLKPQLP PAGLSKPDPK RWQEQGRRPR VNLLGPSLLG
FRCRDDVREV RVLLDELGID THVVAPLGAS PEDLRRIPQA EANICLYPEV ADSSCRWLER
QFGMPTVSTV PIGIGATEMF CRELQELLGL EPTSQGSGQS RMPWYSRSVD STYLTGKRVF
IFADATHAIA AARIASRELG FEVVGLGSYS REQARAVRAA AEELGLAALI SDNYLEVEAA
MAEAAPELVL GTQMERHSAK RLGIPCAVIS SPLHVQDVPA RYAPQMGWEG ANVIFDSWVH
PLMMGLEEHL IGMFRHDFEF VDGHMSHKGE KPPGPEAADP ITLAAEANGV DEAELLRWAP
SGQAELSRIP FFVRGKVKRN TESYAQERGI INITDEVLYE AKAHFSR
