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Entry: BCHL_RHOCB
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Original site: 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   27-MAR-2024, entry version 67.
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; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; 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}.
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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   GeneID; 31489608; -.
DR   KEGG; rcp:RCAP_rcc00662; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_2_0_5; -.
DR   OrthoDB; 9778641at2; -.
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   CDD; cd02032; Bchl-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01281; DPOR_bchL; 1.
DR   PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   PRINTS; PR00091; NITROGNASEII.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
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