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Database: UniProt
Entry: B4S3D3_PROA2
LinkDB: B4S3D3_PROA2
Original site: B4S3D3_PROA2 
ID   B4S3D3_PROA2            Unreviewed;       469 AA.
AC   B4S3D3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   OrderedLocusNames=Paes_0168 {ECO:0000313|EMBL:ACF45227.1};
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF45227.1, ECO:0000313|Proteomes:UP000002725};
RN   [1] {ECO:0000313|EMBL:ACF45227.1, ECO:0000313|Proteomes:UP000002725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) 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}.
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DR   EMBL; CP001108; ACF45227.1; -; Genomic_DNA.
DR   RefSeq; WP_012504764.1; NC_011059.1.
DR   AlphaFoldDB; B4S3D3; -.
DR   STRING; 290512.Paes_0168; -.
DR   KEGG; paa:Paes_0168; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_564837_0_0_10; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000002725; 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; 3.
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:UP000002725}.
FT   DOMAIN          13..391
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          417..466
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
SQ   SEQUENCE   469 AA;  52607 MW;  F51E04E7BD204B32 CRC64;
     MTRTIRDEST ASAYWAAVNT FCALHDVHVI ADAPVGCYNL VGVAVMDYTD AVPYLENLTP
     TSLTEKEISS SGSTQKVQGI IEKLKNEKKE LILISSAESE MIGSNHTMML RHSYPDVHFF
     DSRSLGENEW QGRDRALVWL HEQFDDGRPA EVEPGTVSII GPTYGCFNSP SDLAEIKRIV
     EGCGLTIKHV YPFESNLHDI SDLKNSDIVI VMYREFGQTL ADLLGRPVLQ APFGLSETEH
     FIENLGRLTN RQKEAAAFLT LEKKTILKPI WDLWRGPQSE WFPTIRFGVV ADQTYTEGLK
     KFLSQEMGMA CLFNHNSQTT NNNDVREELA NQQPQFLFGR MADKIYLAEL GAKTRFIPAG
     FPGPIVRRAL GTPFMGHSGA VYLLQEIVNA LYDTLFHFLP ISMRSSEGPI ETKKITWTKE
     ANAILEEIVK KAPFISQISF GRDMKKKAEA LAAKQGKETV TPDILHMLK
//
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