BCHZ_ERYLO
ID BCHZ_ERYLO Reviewed; 494 AA.
AC Q9KWI8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 63.
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;
OS Erythrobacter longus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MBIC2294;
RA Hamada T.;
RT "Nucleotide sequences of genes coding for photosynthetic reaction centers
RT and light-harvesting proteins and BChl biosynthesis enzyme of Erythrobacter
RT longus.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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; AB035570; BAA96512.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KWI8; -.
DR SMR; Q9KWI8; -.
DR STRING; 1044.EH31_08740; -.
DR eggNOG; COG2710; Bacteria.
DR UniPathway; UPA00669; -.
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.
FT CHAIN 1..494
FT /note="Chlorophyllide reductase subunit Z"
FT /id="PRO_0000219848"
SQ SEQUENCE 494 AA; 54127 MW; 6EB73D03AB0D99F7 CRC64;
MTLVLDHDRA GGYWGATYVF TAVKGLQVII DGPVGCENLP VTSVLHYTDA LPPHELPIVV
TGLGEEELGK TGTEAAMKRA WQTLDPELPA VVVTGSISEM IGGGVTPEGT NIKRFLPRTI
DEDQWQSADR ALTWLWTEFG PKKMPQPRPR KEGEKPVVNI IGPSYGMFNM PSDLAEIRRL
VEGIGAEVGV VFPLGCHLAD IRKLGTADAN VCMYREFGRN LCETLERPYF QAPVGLSSTT
KFLRALAAEL GLDPEPFIER EKHTTIKPLW DLWRSVTQDF FATANFGIVA NDTYARGIRH
FLEDDMGLPC AFAYSREAGV KPRNDEVRED IHKSPPLVMF GSYNERMYMA EVGARGKFIP
ASFPGAAIRR HIGTPFMGYS GATYLVQEVC NALFDALFHI LPLGTDMDKG QATLARGADV
PVKAGSNGAP THEVTWDTEA KARLDELVEE QPVLIRISAA KRLRDAAEAA ARAKGADTVT
KDCLQEALLE GEAV