ID   CHLB_EPHAL              Reviewed;         509 AA.
AC   P37846;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 84.
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   Ephedra altissima (High-climbing jointfir).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Gnetopsida; Gnetidae; Ephedrales; Ephedraceae; Ephedra.
OX   NCBI_TaxID=3391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8812302; DOI=10.1006/mpev.1996.0054;
RA   Boivin R., Richard M., Beauseigle D., Bousquet J., Bellemare G.;
RT   "Phylogenetic inferences from chloroplast chlB gene sequences of
RT   Nephrolepis exaltata (Filicopsida), Ephedra altissima (Gnetopsida), and
RT   diverse land plants.";
RL   Mol. Phylogenet. Evol. 6:19-29(1996).
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; U21315; AAC49429.1; -; Genomic_DNA.
DR   EMBL; L25765; AAC37487.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37846; -.
DR   SMR; P37846; -.
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..509
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B"
FT                   /id="PRO_0000219821"
FT   ACT_SITE        298
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         433..434
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   509 AA;  57884 MW;  E86032E8B94B4031 CRC64;
     MKLAYWMYAG PAHIGTLRVA NSFKNVHAIM HAPLGDDYFN VMRSMLERER NFTPATASIV
     DRRVLGRGSQ KKVVDNLLRK DKEENPDLII LTPTCTSSIL QEDLQNFVDR ASVISDSNII
     LADVDHYQVN EIQAADRTLE QVVRFYLSKQ KKEKLDRFLT DVPSVNIIGI FTLGFHHQHD
     CRELKRLFQD LNIQINQVIP EGGSVEDLQN LPKAWLNLVP YREIGLMTAF FLKKEFGMPY
     LSITPMGVID NAECIRRIEK SVNPFASIFG EKGVNYESYI DRQTRFISQA VWFSRSIDCQ
     NFTGKQTVVF GDATHAASIT KILAREMGIR VSCTGTYCKH DAEWFKEQVQ DFSNEILITE
     DHAKVGKKIA CVEPSAIFGT QMERHIGKRF DISCGVISAP VHIQNFPLGY RPFMGYEGTN
     QIADLVYNSF ALGMEDHLLD IFGGHDMKEV ITKSNPIGGL DVIWDTESQL ELPQIPRFVR
     DKVKRETEKF AKIKGVVKIT IEVMYAAKE