BCHZ_CERS4
ID BCHZ_CERS4 Reviewed; 491 AA.
AC Q3J1A0; Q02433; Q9RFC0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chlorophyllide reductase subunit Z;
DE EC=1.3.7.15 {ECO:0000250|UniProtKB:P26179};
DE AltName: Full=Chlorin reductase subunit Z;
GN Name=bchZ; OrderedLocusNames=RHOS4_18660; ORFNames=RSP_0260;
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:P26179}.
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:P26179};
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:P26179};
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:P26179};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis.
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:P26179}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000305}.
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DR EMBL; AJ010302; CAB38749.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24299.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79434.1; -; Genomic_DNA.
DR PIR; S30917; S30917.
DR PIR; T50755; T50755.
DR RefSeq; WP_011338109.1; NZ_CP030271.1.
DR RefSeq; YP_353335.1; NC_007493.2.
DR AlphaFoldDB; Q3J1A0; -.
DR SMR; Q3J1A0; -.
DR STRING; 272943.RSP_0260; -.
DR EnsemblBacteria; ABA79434; ABA79434; RSP_0260.
DR KEGG; rsp:RSP_0260; -.
DR PATRIC; fig|272943.9.peg.2204; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; VWDLWRS; -.
DR PhylomeDB; Q3J1A0; -.
DR BioCyc; MetaCyc:MON-13258; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR010244; BchZ.
DR InterPro; IPR013580; LI-POR_suB-like_C.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR TIGRFAMs; TIGR02014; BchZ; 1.
PE 3: Inferred from homology;
KW Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..491
FT /note="Chlorophyllide reductase subunit Z"
FT /id="PRO_0000219852"
FT CONFLICT 218..219
FT /note="GR -> A (in Ref. 1; CAB38749)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..262
FT /note="EK -> AP (in Ref. 1; CAB38749)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="E -> Q (in Ref. 1; CAB38749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 53429 MW; F99B820C98C13FAE CRC64;
MLVQDHDRAG GYWGAVYAFC AVKGLQVVID GPVGCENLPV TSVLHYTDAL PPHELPIVVT
GLGESEMSEG TEASMSRAWK VLDPALPAVV VTGSIAEMIG GGVTPQGTNI QRFLPRTIDE
DQWEAADRAM TWIFSEFGMT KGRMPPEAKR PEGAKPRVNI LGPMYGVFNM ASDLHEIRRL
VEGIGAEVNM VMPLGAHLAE MRHLVNADAN IVMYREFGRG LAEVLGKPYL QAPIGVESTT
AFLRRLGEIL GLDPEPFIER EKHSTLKPVW DLWRSVTQDF FGTANFGIVA TETYARGIRN
YLEGDLGLPC AFAVARKRGS KTDNEAVRGL IRQHRPLVLM GSINEKIYLA ELKAGHGPQP
SFIAASFPGA AIRRATGTPV MGYAGATWLL QEVCNALFDA LFHILPLGTE MDSAAATPTT
LRRDFPWDAD AQAALDRIVE EHPVLTRISA ARALRDAAEK AALDAGAERV VRETVEALRG
PGFGERKGEN Q
