CHLB_PLETE
ID CHLB_PLETE Reviewed; 514 AA.
AC A6YGA3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
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};
OS Pleurastrum terricola (Filamentous green alga) (Leptosira terrestris).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Pleurastraceae; Pleurastrum.
OX NCBI_TaxID=34116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 463/2 / UTEX 333;
RX PubMed=17610731; DOI=10.1186/1471-2164-8-213;
RA de Cambiaire J.-C., Otis C., Turmel M., Lemieux C.;
RT "The chloroplast genome sequence of the green alga Leptosira terrestris:
RT multiple losses of the inverted repeat and extensive genome rearrangements
RT within the Trebouxiophyceae.";
RL BMC Genomics 8:213-213(2007).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; EF506945; ABO69319.1; -; Genomic_DNA.
DR RefSeq; YP_001382180.1; NC_009681.1.
DR AlphaFoldDB; A6YGA3; -.
DR SMR; A6YGA3; -.
DR GeneID; 5383758; -.
DR UniPathway; UPA00670; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid.
FT CHAIN 1..514
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000324049"
FT ACT_SITE 300
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 435..436
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 514 AA; 57904 MW; DADCF483A2F83885 CRC64;
MKLAYWMYAG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTPVTASIV
DRHVLARGSQ EKVVETITRK DKEEQPDLIL LTPTCTSSIL QEDLQNFVNR AATESKSDVI
LADVNHYRVN ELQAADRTLE QIVRFYIEKA KTQNDLATIK TEKPSVNIIG IFTLGFHNHH
DCRELKRLLT DLGISINEVI PEGGSIKNLK NLPKAWFNLI PYREVGLMTA KYLEKELNMP
FVATTPMGVI DTAICIREIE AILNFTNQSK IDKEPYNFED YIDQQTRFVS QAAWFSRSID
CQNLTGKKAI VFGDSTHAAS MTKILAREMG IRISCAGTYC KHDADWFREQ VSGFCDSVLI
TDDHTKVGDM IARVEPAAIF GTQMERHVGK RLDIPCGVIS APVHIQNFPL GYRPFLGYEG
TNQIADLVYN SFTLGMEDHL LEIFGGHDTK QVITKSLSTD SNLTWTIEGL AELNKIPGFV
RAKIKRNTEK FARENNISEI TIETMYAAKE AVGA
