BCHL_RHOCB
ID BCHL_RHOCB Reviewed; 304 AA.
AC D5ANS3; P26237;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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, ECO:0000269|PubMed:10811655};
GN Name=bchL {ECO:0000255|HAMAP-Rule:MF_00355};
GN OrderedLocusNames=RCAP_rcc00662;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RA Burke D.H., Alberti M., Armstrong G.A., Hearst J.E.;
RL Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2203738; DOI=10.1128/jb.172.9.5001-5010.1990;
RA Yang Z.M., Bauer C.E.;
RT "Rhodobacter capsulatus genes involved in early steps of the
RT bacteriochlorophyll biosynthetic pathway.";
RL J. Bacteriol. 172:5001-5010(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=SB1003 / CB1029;
RX PubMed=10811655; DOI=10.1074/jbc.m002904200;
RA Fujita Y., Bauer C.E.;
RT "Reconstitution of light-independent protochlorophyllide reductase from
RT purified bchL and bchN-bchB subunits. In vitro confirmation of nitrogenase-
RT like features of a bacteriochlorophyll biosynthesis enzyme.";
RL J. Biol. Chem. 275:23583-23588(2000).
RN [5]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=15953479; DOI=10.1016/j.bbabio.2005.02.002;
RA Nomata J., Swem L.R., Bauer C.E., Fujita Y.;
RT "Overexpression and characterization of dark-operative protochlorophyllide
RT reductase from Rhodobacter capsulatus.";
RL Biochim. Biophys. Acta 1708:229-237(2005).
RN [6]
RP CHARACTERIZATION, COFACTOR, AND IRON-SULFUR CLUSTER.
RX PubMed=17064695; DOI=10.1016/j.febslet.2006.10.014;
RA Nomata J., Kitashima M., Inoue K., Fujita Y.;
RT "Nitrogenase Fe protein-like Fe-S cluster is conserved in L-protein (BchL)
RT of dark-operative protochlorophyllide reductase from Rhodobacter
RT capsulatus.";
RL FEBS Lett. 580:6151-6154(2006).
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:0000269|PubMed:10811655}.
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 ECO:0000269|PubMed:10811655, ECO:0000269|PubMed:15953479};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:17064695};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000269|PubMed:17064695};
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:0000269|PubMed:15953479}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC Rule:MF_00355}.
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; Z11165; CAA77523.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84427.1; -; Genomic_DNA.
DR EMBL; M34843; AAA26098.1; -; Genomic_DNA.
DR PIR; B36716; B36716.
DR RefSeq; WP_013066406.1; NC_014034.1.
DR AlphaFoldDB; D5ANS3; -.
DR SMR; D5ANS3; -.
DR STRING; 272942.RCAP_rcc00662; -.
DR EnsemblBacteria; ADE84427; ADE84427; RCAP_rcc00662.
DR GeneID; 31489608; -.
DR KEGG; rcp:RCAP_rcc00662; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_2_0_5; -.
DR OMA; EVDFHHE; -.
DR OrthoDB; 729012at2; -.
DR BRENDA; 1.3.7.7; 5381.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002361; 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 1: Evidence at protein level;
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..304
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000409926"
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:0000305"
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:0000305"
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 304 AA; 33205 MW; 3A49C39BCF15AECC CRC64;
MSPRDDIPDL KGFDGDGEGS VQVHDSEDIG LDVGGARVFS VYGKGGIGKS TTSSNLSAAF
SLLGKRVLQI GCDPKHDSTF TLTGRLQETV IDILKQVNFH PEELRPEDYV TEGFNGVMCV
EAGGPPAGTG CGGYVVGQTV KLLKQHHLLE DTDVVVFDVL GDVVCGGFAA PLQHADRALI
VTANDFDSIY AMNRIIAAVQ AKSVNYKVRL AGCVANRSRE TNEVDRYCEA ANFKRIAHMP
DLDSIRRSRL KKRTLFEMDD AEDVVMARAE YIRLAETLWR STGEPGLTPE PLTDRHIFEL
LGFD
