BCHY_CERS4
ID BCHY_CERS4 Reviewed; 502 AA.
AC Q02432; Q3J199; Q9RFC1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chlorophyllide reductase 52.5 kDa chain;
DE EC=1.3.7.15 {ECO:0000250|UniProtKB:P26178};
DE AltName: Full=Chlorin reductase;
GN Name=bchY; OrderedLocusNames=RHOS4_18670; ORFNames=RSP_0261;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8437569; DOI=10.1007/bf00277117;
RA McGlynn P., Hunter C.N.;
RT "Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides.";
RL Mol. Gen. Genet. 236:227-234(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts chlorophylls (Chl) into bacteriochlorophylls (BChl)
CC by reducing ring B of the tetrapyrrole. {ECO:0000250|UniProtKB:P26178}.
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:0000250|UniProtKB:P26178};
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:0000250|UniProtKB:P26178};
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:0000250|UniProtKB:P26178};
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:0000250|UniProtKB:P26178}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000305}.
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DR EMBL; AJ010302; CAB38748.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24298.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79435.1; -; Genomic_DNA.
DR PIR; S30916; S30916.
DR PIR; T50754; T50754.
DR RefSeq; WP_011338110.1; NZ_CP030271.1.
DR RefSeq; YP_353336.1; NC_007493.2.
DR AlphaFoldDB; Q02432; -.
DR SMR; Q02432; -.
DR STRING; 272943.RSP_0261; -.
DR EnsemblBacteria; ABA79435; ABA79435; RSP_0261.
DR KEGG; rsp:RSP_0261; -.
DR PATRIC; fig|272943.9.peg.2205; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; QSMCPAF; -.
DR PhylomeDB; Q02432; -.
DR BioCyc; MetaCyc:MON-13257; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002703; Chromosome 1.
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 3: Inferred from homology;
KW Bacteriochlorophyll biosynthesis; Cell membrane; Chlorophyll biosynthesis;
KW Membrane; Oxidoreductase; Photosynthesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..502
FT /note="Chlorophyllide reductase 52.5 kDa chain"
FT /id="PRO_0000208623"
FT TRANSMEM 70..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 144
FT /note="G -> A (in Ref. 1; CAB38748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 52341 MW; A5D4EE727F2787E5 CRC64;
MSQTPGGAPM APEAMGCHST ADMAAAASAA GNGELMERFK ADYPVGPHDK PQSMCPAFGS
LRTGLRMRRV GTIISGSACC TYGLSFVSHF YGARRSIGYV PFNSESLVTG KLFEDIREAV
HEMADPQRYD AIVVTNLCVP TASGVPLRLL PSEINGVRIV GIDVPGFGVP THAEAKDVLA
GAMLKYARSE IEAGPVQAPV SGRSDRPTVA LLGEMFPADP VMIGALLAPL GLAAGPVVPC
RDWRELYAAL DSGVAAAIHP FYTASVREFQ AAGRAIVGSA PVGHDGTAAW LAAIGEAYGI
AADKVAAAQN AFLPAIRGAL AGAPIKGRIT LSGYEGSELI VARLLIESGA EVPYVGTAAG
RTPWSAADRE WLEARGTVVK FRASLEDDLA AMQGFEPDLA VGTTPVVQKA KSLGIPSLYF
TNLISARPLM GPAGAGSLAQ VINAAIGNRE RMSKMKAFFA GVGEGDTAGI WEGAPNLRPD
FRAAHQKKLE KAARAAKSEE MI
