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Database: UniProt
Entry: A0A2M8MVG2_9RHOB
LinkDB: A0A2M8MVG2_9RHOB
Original site: A0A2M8MVG2_9RHOB 
ID   A0A2M8MVG2_9RHOB        Unreviewed;       500 AA.
AC   A0A2M8MVG2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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:PJF08190.1};
GN   ORFNames=CUR21_16120 {ECO:0000313|EMBL:PJF08190.1};
OS   Pseudorhodobacter sp. MZDSW-24AT.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudorhodobacter.
OX   NCBI_TaxID=2052957 {ECO:0000313|EMBL:PJF08190.1, ECO:0000313|Proteomes:UP000230388};
RN   [1] {ECO:0000313|EMBL:PJF08190.1, ECO:0000313|Proteomes:UP000230388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZDSW-24AT {ECO:0000313|EMBL:PJF08190.1,
RC   ECO:0000313|Proteomes:UP000230388};
RA   Mayilraj S.;
RT   "Pseudorhodobacter sp. nov., strain MZDSW-24AT genome sequence and
RT   assembly.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJF08190.1}.
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DR   EMBL; PGOI01000012; PJF08190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8MVG2; -.
DR   OrthoDB; 5713965at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000230388; Unassembled WGS sequence.
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; 1.
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   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230388}.
FT   DOMAIN          12..401
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          431..480
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
SQ   SEQUENCE   500 AA;  54321 MW;  FB3E409FA4B8A936 CRC64;
     MLIQDHDRAG GYWGAIYAFC AVKGLQVVID GPVGCENLPV TSVLHYTDAL PPHELPIVVT
     GLAEDEMSSG TEASMARAWK VLDPALPAVV VTGSIAEMIG GGVTPAGTNI QRFLPRTIDE
     DQWQCADRAM TWIFTEFGMT KGRMPVEKKR EDGAPPRVNI LGPMYGTFNM ASDLHEIRRL
     VEGIGAEVNM VMPLGAHLAE MRNLVNADVN IVMYREFGRG LAEVLGKPYL QAPFGLESTT
     KFLRSLGELL GLDPEPFIAR EKHSTLKPVW DLWRSVTQDF FATASFAIVA NDTYTRGVRN
     YLEHDLGLPC AFAVSRVAGA KTNNEAVRAL LKQHRPLIVM GSINEKMYMA EMKGGPGSFG
     GPAPSFIAAS FPGAAIRRHT GTPFMGYAGA VWILQEVCNG LFEALFHILP LGSEMDSAAA
     TPTTLRRDFP WDLDAQAALD RIVSEHPVLT RISAAKSLRD AAEKAALDHG AERVIVEFVE
     GLRGDARPTQ DANAKGGIHE
//
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