BCHZ_RHOCB
ID BCHZ_RHOCB Reviewed; 490 AA.
AC P26179; D5AP82;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chlorophyllide reductase subunit Z;
DE EC=1.3.7.15 {ECO:0000269|PubMed:16571720};
DE AltName: Full=Chlorin reductase subunit Z;
GN Name=bchZ; OrderedLocusNames=RCAP_rcc00689;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8468299; DOI=10.1128/jb.175.8.2407-2413.1993;
RA Burke D.H., Alberti M., Hearst J.E.;
RT "The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA,
RT consists of three genes, bchX, bchY, and bchZ.";
RL J. Bacteriol. 175:2407-2413(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=16571720; DOI=10.1074/jbc.m601750200;
RA Nomata J., Mizoguchi T., Tamiaki H., Fujita Y.;
RT "A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis:
RT reconstitution of chlorophyllide a reductase with purified X-protein (BchX)
RT and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.";
RL J. Biol. Chem. 281:15021-15028(2006).
CC -!- FUNCTION: Converts chlorophylls (Chl) into bacteriochlorophylls (BChl)
CC by reducing ring B of the tetrapyrrole. {ECO:0000269|PubMed:16571720}.
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:0000269|PubMed:16571720};
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:0000269|PubMed:16571720};
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:0000269|PubMed:16571720};
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:0000269|PubMed:16571720}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z11165; CAA77550.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84454.1; -; Genomic_DNA.
DR PIR; D49850; D49850.
DR RefSeq; WP_013066433.1; NC_014034.1.
DR AlphaFoldDB; P26179; -.
DR SMR; P26179; -.
DR STRING; 272942.RCAP_rcc00689; -.
DR EnsemblBacteria; ADE84454; ADE84454; RCAP_rcc00689.
DR GeneID; 31489635; -.
DR KEGG; rcp:RCAP_rcc00689; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_564837_0_0_5; -.
DR OMA; VWDLWRS; -.
DR OrthoDB; 363662at2; -.
DR BioCyc; MetaCyc:MON-13255; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000002361; 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 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 1: Evidence at protein level;
KW Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Direct protein sequencing; Oxidoreductase; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Chlorophyllide reductase subunit Z"
FT /id="PRO_0000219849"
SQ SEQUENCE 490 AA; 53218 MW; 163120EC644749E8 CRC64;
MFLLDHDRAG GYWGAVYTFC AVKGLQVVID GPVGCENLPV TSVLHYTDGL PPHELPIVVT
GLGDAELGRE GTEGAMSRAW KTLDPLLPSV VVTGSIAEMI GGGVTPQGTN LQRFLARTID
EDQWQCADRA MTWLFTEYGM TKGRMPGERM RPDGAKPRVN ILGPMYGAFN MASDLHEIRR
LVEGIGAEVN MVFPLGTHLS EVRNLVNADV NVVMYREFGR NLAEILGKPY LQAPIGLEST
TKFLRSLGEL LGLDPEPFIE REKHATLKPL WDLWRSVTQD FFATASFGIC ATETYARGIK
AYLEGDLGLP CAFAVARKAG EKTKSDEVRG LIRQTRPLVV FGSINEKIYL AETKAGHGPA
ASFVPASFPG AAIRRATGTP FMGYMGSVYL LQEICNGLFD ALFNILPLAS EMDSAAATPA
TLRRDMPWDA DAQAALDRIV SQHPVLTRIS AAKSLRDAAE KAALDQGAER VVLEMVEALG
DATMDRKGGN
