BCHY_RHOCB
ID BCHY_RHOCB Reviewed; 497 AA.
AC P26178; D5AP81;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chlorophyllide reductase 52.5 kDa chain;
DE EC=1.3.7.15 {ECO:0000269|PubMed:16571720};
DE AltName: Full=Chlorin reductase;
GN Name=bchY; OrderedLocusNames=RCAP_rcc00688;
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 -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent).
CC -!- SUBUNIT: Chlorophyllide reductase is composed of three subunits; BchX,
CC BchY and BchZ. Forms a heterodimer of one BchY and one BchZ subunit.
CC {ECO:0000269|PubMed:16571720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BchN/ChlN 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; Z11165; CAA77549.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84453.1; -; Genomic_DNA.
DR PIR; C49850; C49850.
DR RefSeq; WP_013066432.1; NC_014034.1.
DR AlphaFoldDB; P26178; -.
DR SMR; P26178; -.
DR STRING; 272942.RCAP_rcc00688; -.
DR PRIDE; P26178; -.
DR EnsemblBacteria; ADE84453; ADE84453; RCAP_rcc00688.
DR GeneID; 31489634; -.
DR KEGG; rcp:RCAP_rcc00688; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_536179_0_0_5; -.
DR OMA; QSMCPAF; -.
DR OrthoDB; 401751at2; -.
DR BioCyc; MetaCyc:MON-13254; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR010245; BchY.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR TIGRFAMs; TIGR02015; BchY; 1.
PE 1: Evidence at protein level;
KW Bacteriochlorophyll biosynthesis; Cell membrane; Chlorophyll biosynthesis;
KW Membrane; Oxidoreductase; Photosynthesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..497
FT /note="Chlorophyllide reductase 52.5 kDa chain"
FT /id="PRO_0000208622"
FT TRANSMEM 65..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..233
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 52619 MW; 99369F0EA91A4209 CRC64;
MTDLPQAEGG CGAGNERLAA QAAAAGNAEL MARFKADYPV GPHDKPQTMC PAFGALRVGL
RMRRVATVLC GSACCVYGLS FISHFYGARR SVGYVPFDSE TLVTGKLFED VRASVHDLAD
PARYDAIVVI NLCVPTASGV PLQLLPNEIN GVRVVGIDVP GFGVPTHAEA KDVLSGAMLA
YARQEVMAGP VPAPISGRSD RPTVTLLGEM FPADPMVIGA MLAPMGLAVG PTVPMRDWRE
LYAALDSKVV AAIHPFYTAA IRQFEAAGRA IVGSAPVGHD GTMEWLANIG RAYDVSPDKI
AAAQNAFGPA IRGAIAGAPI KGRITVSGYE GSELLVARLL IESGAEVPYV GTAAPRTPWS
AWDKDWLESR GVVVKYRASL EDDCAAMEGF EPDLAIGTTP LVQKAKALGI PALYFTNLIS
ARPLMGPAGA GSLAQVMNAA MGNRERMGKM KAFFEGVGEG DTAGIWQDTP KLYPDFREQQ
RKKMEKAAKL AKAEEMI
