BCHL_ACIRU
ID BCHL_ACIRU Reviewed; 87 AA.
AC Q9WXB7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein;
DE Short=DPOR subunit L;
DE Short=LI-POR subunit L;
DE EC=1.3.7.7;
DE Flags: Fragment;
GN Name=bchL;
OS Acidiphilium rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=526;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10559247; DOI=10.1074/jbc.274.47.33594;
RA Masuda T., Inoue K., Masuda M., Nagayama M., Tamaki A., Ohta H.,
RA Shimada H., Takamiya K.;
RT "Magnesium insertion by magnesium chelatase in the biosynthesis of zinc
RT bacteriochlorophyll a in an aerobic acidophilic bacterium Acidiphilium
RT rubrum.";
RL J. Biol. Chem. 274:33594-33600(1999).
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 L component serves as a unique
CC electron donor to the NB-component of the complex, and binds Mg-ATP (By
CC 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 dimer. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent).
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; BchL, BchN and BchB (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017351; BAA76539.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WXB7; -.
DR SMR; Q9WXB7; -.
DR STRING; 526.SAMN05421828_102100; -.
DR UniPathway; UPA00671; -.
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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00142; Fer4_NifH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis.
FT CHAIN 1..>87
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000139575"
FT BINDING 53..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT NON_TER 87
SQ SEQUENCE 87 AA; 8917 MW; A9E05DAEF5AC530A CRC64;
MNDISTVNKL AERIGGSSCS TSCGDGEGSL QVALDPHIKI TGAKVFAVYG KGGIGKSTTS
SNLSAAFSRL GKRVLQICRD RGADATI
