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Database: UniProt
Entry: Q6N9L6_RHOPA
LinkDB: Q6N9L6_RHOPA
Original site: Q6N9L6_RHOPA 
ID   Q6N9L6_RHOPA            Unreviewed;       482 AA.
AC   Q6N9L6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Chlorophyllide reductase subunit Z {ECO:0000256|ARBA:ARBA00019776};
DE            EC=1.3.7.15 {ECO:0000256|ARBA:ARBA00012326};
DE   AltName: Full=Chlorin reductase subunit Z {ECO:0000256|ARBA:ARBA00032447};
GN   Name=bchZ {ECO:0000313|EMBL:CAE26966.1};
GN   OrderedLocusNames=RPA1524 {ECO:0000313|EMBL:CAE26966.1};
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE26966.1, ECO:0000313|Proteomes:UP000001426};
RN   [1] {ECO:0000313|EMBL:CAE26966.1, ECO:0000313|Proteomes:UP000001426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA   Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
CC   -!- FUNCTION: Converts chlorophylls (Chl) into bacteriochlorophylls (BChl)
CC       by reducing ring B of the tetrapyrrole.
CC       {ECO:0000256|ARBA:ARBA00003934}.
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:0000256|ARBA:ARBA00001586};
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:0000256|ARBA:ARBA00000965};
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:0000256|ARBA:ARBA00000410};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004800}.
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:0000256|ARBA:ARBA00011283}.
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DR   EMBL; BX572597; CAE26966.1; -; Genomic_DNA.
DR   RefSeq; WP_011157085.1; NZ_CP116810.1.
DR   AlphaFoldDB; Q6N9L6; -.
DR   STRING; 258594.RPA1524; -.
DR   GeneID; 66892554; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_564837_0_0_5; -.
DR   PhylomeDB; Q6N9L6; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000001426; Chromosome.
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   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   InterPro; IPR010244; BchZ.
DR   InterPro; IPR013580; LI-POR_suB-like_C.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   NCBIfam; TIGR02014; BchZ; 1.
DR   PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   PIRSF; PIRSF000163; PCP_ChlB; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   4: Predicted;
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023181};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAE26966.1};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001426}.
FT   DOMAIN          12..391
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          421..473
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
SQ   SEQUENCE   482 AA;  53279 MW;  328F4BB35DBC03A8 CRC64;
     MLVLDHDRAG GYWGAVYAFT AVKGLQVIID GPVGCENLPV TSVLHYTDAL PPHELPIVVT
     GLGEEELGKL GTEGAMHRAH KALDPYLPAV VVTGSIAEMI GGGVTPEGTG IKRFLPRTID
     EDQWQSADRA ISWLWKEYGP KKIPERKRKD GEKPRVNIIG PIYGTFNMPS DLAEIRRLIE
     GIGAEVNMVF PLGTHLADIP KLVNADVNVC MYREFGRLLC ESLERPYLQA PIGLHSTTRF
     LRKLGELTGL DPEPFIEREK NTTIKPLWDL WRSVTQDFFG TASFAVVATD TYARGVRHFL
     EDEMGLPCTF AVSRCVGKKT DNEAVRAAIR QTPPLIMFGS YNERMYLAET GGRAVYIPAS
     FPGAVIRRHT GTPFMGYSGA TYLVQEVCNA LFDALFNILP LGSDLDRVDP TPARRHEELL
     WSDEAKALLD EVLEQHPVLV RISAAKRLRD AAENSARRAG QEKVTTEFVS KARAALLDGQ
     SV
//
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