BCHL_RUBGI
ID BCHL_RUBGI Reviewed; 302 AA.
AC Q9JPA5; I0HUK1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_00355};
DE Short=DPOR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE Short=LI-POR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00355};
GN Name=bchL {ECO:0000255|HAMAP-Rule:MF_00355}; OrderedLocusNames=RGE_33490;
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=983917;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=11343129; DOI=10.1007/s002390010163;
RA Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA Nagashima K.V.P.;
RT "Horizontal transfer of the photosynthesis gene cluster and operon
RT rearrangement in purple bacteria.";
RL J. Mol. Evol. 52:333-341(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=22689232; DOI=10.1128/jb.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00355}.
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_00355};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00355};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC Rule:MF_00355};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; BchL, BchN and BchB. {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC Rule:MF_00355}.
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DR EMBL; AB034704; BAA94056.1; -; Genomic_DNA.
DR EMBL; AP012320; BAL96688.1; -; Genomic_DNA.
DR PIR; T50903; T50903.
DR RefSeq; WP_014429549.1; NC_017075.1.
DR AlphaFoldDB; Q9JPA5; -.
DR SMR; Q9JPA5; -.
DR STRING; 983917.RGE_33490; -.
DR EnsemblBacteria; BAL96688; BAL96688; RGE_33490.
DR KEGG; rge:RGE_33490; -.
DR PATRIC; fig|983917.3.peg.3275; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_2_0_4; -.
DR OMA; EVDFHHE; -.
DR OrthoDB; 729012at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000007883; 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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00355; ChlL_BchL; 1.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005971; Protochlorophyllide_ATP-bd.
DR PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01281; DPOR_bchL; 1.
DR PROSITE; PS00746; NIFH_FRXC_1; 1.
DR PROSITE; PS00692; NIFH_FRXC_2; 1.
DR PROSITE; PS51026; NIFH_FRXC_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome.
FT CHAIN 1..302
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000139580"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 165
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 216..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
SQ SEQUENCE 302 AA; 32658 MW; CD3DFFFA24FDAAE7 CRC64;
MSTATISPSQ IGRGARPDGE GSVQVQMETG AKIGNAKVFA IYGKGGIGKS TTSSNLSVAF
SKLGKRVLQI GCDPKHDSTF TLTKRMVPTV IDVLETVNFH PEELRVEDFV FEGTNGVMCV
EAGGPPAGTG CGGYVVGQTV KLLKEHHLLE ETDVVVFDVL GDVVCGGFAA PLQHADRALI
VTANDFDSIF AANRIVQAIG AKAKNYNVRL GGIIANRSDA TDQIDKFNER IGMRSLARIP
ALDVIRKSRL KKATLFEMEE SPEVLAVQAE YLQLAQRLWD GVDPLYCEPL KDRDIFDLLG
YD
