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BCHZ_ROSDO
ID   BCHZ_ROSDO              Reviewed;         491 AA.
AC   P26277; Q16DU9;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chlorophyllide reductase subunit Z;
DE            EC=1.3.7.15 {ECO:0000250|UniProtKB:P26179};
DE   AltName: Full=Chlorin reductase subunit Z;
GN   Name=bchZ; Synonyms=bchA; OrderedLocusNames=RD1_0109;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-491.
RX   PubMed=1787796; DOI=10.1111/j.1365-2958.1991.tb00792.x;
RA   Liebetanz R., Hornberger U., Drews G.;
RT   "Organization of the genes coding for the reaction-centre L and M subunits
RT   and B870 antenna polypeptides alpha and beta from the aerobic
RT   photosynthetic bacterium Erythrobacter species OCH114.";
RL   Mol. Microbiol. 5:1459-1468(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   EMBL; CP000362; ABG29844.1; -; Genomic_DNA.
DR   EMBL; X57597; CAA40816.1; -; Genomic_DNA.
DR   RefSeq; WP_011566466.1; NZ_FOOO01000011.1.
DR   AlphaFoldDB; P26277; -.
DR   SMR; P26277; -.
DR   STRING; 375451.RD1_0109; -.
DR   EnsemblBacteria; ABG29844; ABG29844; RD1_0109.
DR   KEGG; rde:RD1_0109; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_564837_0_0_5; -.
DR   OMA; VWDLWRS; -.
DR   OrthoDB; 363662at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000007029; 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   3: Inferred from homology;
KW   Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW   Photosynthesis; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Chlorophyllide reductase subunit Z"
FT                   /id="PRO_0000064869"
FT   CONFLICT        403
FT                   /note="H -> L (in Ref. 2; CAA40816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        427
FT                   /note="W -> R (in Ref. 2; CAA40816)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   491 AA;  53375 MW;  E873A3CACD5AA969 CRC64;
     MLVTDHDRAG GYWGAVYAFC AVKGLQVVID GPVGCENLPV TSVLHYTDAL PPHELPIVVT
     GLGEGEMGSG TEESMKRAWD TLDPALPAVV VTGSIAEMIG GGVTPQGTNI QRFLPRTIDE
     DQWEAADRAM TWIFTEFGMT KGRMPPEKKR GEGARPRVNI LGPMYGTFNM PSDLAEIRRL
     VEGIGCEVNM VLPLGAHVAE MRNLVNADVN ICMYREFGRG LSELLAKPYL QAPIGVESTT
     KFLRALGNLV GLDPEPFITQ EKHSTIKPVW DLWRSVTQDF FATASFGIVA NETYARGIRQ
     FLENDLGFPC AFAVARIAGK KTNNEEVRAM IGQKKPLIVL GSINEKMYLA EQKAGFGPAP
     AFIPASFPGA AIRRHTGTPF MGYAGATYLL QEICNGLFDA LFHILPLGTD MDATDATLTP
     LRRDFPWDED AQAMLDRIVE THPILTRISA AKSLRDAAEK AALAAGDERV VLSTVRALDP
     ASAGPDLEDQ T
 
 
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