CHLB_SPHCO
ID CHLB_SPHCO Reviewed; 103 AA.
AC Q33076;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit B;
DE Short=DPOR subunit B;
DE Short=LI-POR subunit B;
DE EC=1.3.7.7;
DE Flags: Fragment;
GN Name=chlB;
OS Sphaeropteris cooperi (Australian tree fern) (Cyathea cooperi).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Cyatheales; Cyatheaceae; Sphaeropteris.
OX NCBI_TaxID=49500;
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
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:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000305}.
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DR EMBL; U21314; AAC49432.1; -; Genomic_DNA.
DR AlphaFoldDB; Q33076; -.
DR SMR; Q33076; -.
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-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR Pfam; PF00148; Oxidored_nitro; 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..>103
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219845"
FT NON_TER 1
FT NON_TER 103
SQ SEQUENCE 103 AA; 11811 MW; F5D07C3A83C690D9 CRC64;
KRSLRDLGIP VNQIIPEGGS LKDLKDLPRA WFNIVPYREV GLMTATFLEK EYGMPYVSVT
PMGILDTAEF ISQVEKLVNA WASVLSEERV NYMLYIQNQT RFV
