BCHX_RHOCB
ID BCHX_RHOCB Reviewed; 333 AA.
AC P26177; D5AP80;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chlorophyllide reductase 35.5 kDa chain;
DE EC=1.3.7.15 {ECO:0000269|PubMed:16571720};
DE AltName: Full=Chlorin reductase;
GN Name=bchX; OrderedLocusNames=RCAP_rcc00687;
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;
RX PubMed=8468299; DOI=10.1128/jb.175.8.2407-2413.1993;
RA Burke D.H., Alberti M., Hearst J.E.;
RT "The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA,
RT consists of three genes, bchX, bchY, and bchZ.";
RL J. Bacteriol. 175:2407-2413(1993).
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 FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=16571720; DOI=10.1074/jbc.m601750200;
RA Nomata J., Mizoguchi T., Tamiaki H., Fujita Y.;
RT "A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis:
RT reconstitution of chlorophyllide a reductase with purified X-protein (BchX)
RT and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.";
RL J. Biol. Chem. 281:15021-15028(2006).
CC -!- FUNCTION: Converts chlorophylls (Chl) into bacteriochlorophylls (BChl)
CC by reducing ring B of the tetrapyrrole. {ECO:0000269|PubMed:16571720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deacetyl-3-vinylbacteriochlorophyllide a + ADP + 2 oxidized
CC [2Fe-2S]-[ferredoxin] + phosphate = ATP + chlorophyllide a + H(+) +
CC H2O + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:37051,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348,
CC ChEBI:CHEBI:83373, ChEBI:CHEBI:456216; EC=1.3.7.15;
CC Evidence={ECO:0000269|PubMed:16571720};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-
CC [ferredoxin] + phosphate = 3-acetyl-3-devinylchlorophyllide a + ATP +
CC H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:48944,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:90794,
CC ChEBI:CHEBI:90795, ChEBI:CHEBI:456216; EC=1.3.7.15;
CC Evidence={ECO:0000269|PubMed:16571720};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + ADP +
CC 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-devinyl-3-(1-
CC hydroxyethyl)chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:48948, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:90791, ChEBI:CHEBI:90792,
CC ChEBI:CHEBI:456216; EC=1.3.7.15;
CC Evidence={ECO:0000269|PubMed:16571720};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:D5ANS3};
CC Note=Binds 1 [4Fe-4S] cluster per dimer.
CC {ECO:0000250|UniProtKB:D5ANS3};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Homodimer (By similarity). Chlorophyllide reductase is
CC composed of three subunits; BchX, BchY and BchZ.
CC {ECO:0000250|UniProtKB:D5ANS3, ECO:0000269|PubMed:16571720}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR EMBL; Z11165; CAA77548.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84452.1; -; Genomic_DNA.
DR PIR; S17823; S17823.
DR RefSeq; WP_013066431.1; NC_014034.1.
DR AlphaFoldDB; P26177; -.
DR SMR; P26177; -.
DR STRING; 272942.RCAP_rcc00687; -.
DR EnsemblBacteria; ADE84452; ADE84452; RCAP_rcc00687.
DR GeneID; 31489633; -.
DR KEGG; rcp:RCAP_rcc00687; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_1_0_5; -.
DR OMA; CQKVIVV; -.
DR OrthoDB; 729012at2; -.
DR BioCyc; MetaCyc:MON-13253; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000002361; Chromosome.
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:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010246; BchX.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02016; BchX; 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..333
FT /note="Chlorophyllide reductase 35.5 kDa chain"
FT /id="PRO_0000139548"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
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:0000250"
FT BINDING 219..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 35574 MW; CD697D641C8943EE CRC64;
MTDAPNLKGF DARLREEAAE EPTLEIPEQP PTKKTQIIAI YGKGGSGKSF TLANLSHMMA
EMGKRVLLIG CDPKSDTTSL LFGGKNCPTI IETATKKKLA GEEVKVGDVC FKSGGVFAME
LGGPEVGRGC GGRGIIHGFE LLEKLGFHDW DFDFVLLDFL GDVVCGGFGL PIARDMAQKV
IVIGSNDLQS LYVANNVCNA VEYFRKLGGN VGVAGIVINK DDGTGEAQAF AREVGIPILA
AIPADEELRR KSAAYQIVGS HATPWGKLFE ELAGNVADAP PLRPRPLSPD ALLALFETDE
ETRVVDLVPA TDEDLRGSNA APKKSLEVIY DDV
