ID   BCHZ_CERSP              Reviewed;         408 AA.
AC   P0C0X6; Q02433; Q9RFC0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Chlorophyllide reductase subunit Z;
DE            EC=1.3.7.15 {ECO:0000250|UniProtKB:P26179};
DE   AltName: Full=Chlorin reductase subunit Z;
DE   Flags: Fragment;
GN   Name=bchZ;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NC13;
RX   PubMed=1779756; DOI=10.1111/j.1365-2958.1991.tb01974.x;
RA   Hunter C.N., McGlynn P., Ashby M.K., Burgess J.G., Olsen J.D.;
RT   "DNA sequencing and complementation/deletion analysis of the bchA-puf
RT   operon region of Rhodobacter sphaeroides: in vivo mapping of the oxygen-
RT   regulated puf promoter.";
RL   Mol. Microbiol. 5:2649-2661(1991).
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   PIR; S30917; S30917.
DR   AlphaFoldDB; P0C0X6; -.
DR   SMR; P0C0X6; -.
DR   UniPathway; UPA00669; -.
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   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   TIGRFAMs; TIGR02014; BchZ; 1.
PE   3: Inferred from homology;
KW   Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW   Photosynthesis.
FT   CHAIN           <1..408
FT                   /note="Chlorophyllide reductase subunit Z"
FT                   /id="PRO_0000219851"
FT   NON_TER         1
SQ   SEQUENCE   408 AA;  44444 MW;  8580ADC26887AF62 CRC64;
     DPALPAVVVT GSIAEMIGGG VTPQGTNIQR FLPRTIDEDQ WEAADRAMTW IFSEFGMTKG
     RMPPEAKRPE GAKPRVNILG PMYGVFNMAS DLHEIRRLVE GIGAEVNMVM PLGAHLAEMR
     HLVNADANIV MYREFAGLAE VLGKPYLQAP IGVESTTAFL RRLGEILGLD PEPFIERAPH
     STLKPVWDLW RSVTQDFFGT ANFGIVATET YARGIRNYLE GDLGLPCAFA VARKRGSKTD
     NEAVRGLIRQ HRPLVLMGSI NEKIYLAELK AGHGPQPSFI AASFPGAAIR RATGTPVMGY
     AGATWLLQEV CNALFDALFH ILPLGTQMDS AAATPTTLRR DFPWDADAQA ALDRIVEEHP
     VLTRISAARA LRDAAEKAAL DAGAERVVRE TVEALRGPGF GERKGENQ