ID BCHZ_RUBGI Reviewed; 487 AA.
AC Q9JPB9; I0HUM0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-NOV-2024, entry version 91.
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; OrderedLocusNames=RGE_33680;
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=11343129; DOI=10.1007/s002390010163;
RA Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA Nagashima K.V.P.;
RT "Horizontal transfer of the photosynthesis gene cluster and operon
RT rearrangement in purple bacteria.";
RL J. Mol. Evol. 52:333-341(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=22689232; DOI=10.1128/jb.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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 + 2 oxidized [2Fe-
CC 2S]-[ferredoxin] + ADP + phosphate = chlorophyllide a + 2 reduced
CC [2Fe-2S]-[ferredoxin] + ATP + H2O + H(+); 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=bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-[ferredoxin] +
CC ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced
CC [2Fe-2S]-[ferredoxin] + ATP + H2O + H(+); 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 + 2
CC oxidized [2Fe-2S]-[ferredoxin] + ADP + phosphate = 3-devinyl-3-(1-
CC hydroxyethyl)chlorophyllide a + 2 reduced [2Fe-2S]-[ferredoxin] + ATP
CC + H2O + H(+); Xref=Rhea:RHEA:48948, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90791, ChEBI:CHEBI:90792, ChEBI:CHEBI:456216;
CC EC=1.3.7.15; 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; AB034704; BAA94037.1; -; Genomic_DNA.
DR EMBL; AP012320; BAL96707.1; -; Genomic_DNA.
DR PIR; T50884; T50884.
DR RefSeq; WP_014429567.1; NC_017075.1.
DR AlphaFoldDB; Q9JPB9; -.
DR SMR; Q9JPB9; -.
DR STRING; 983917.RGE_33680; -.
DR KEGG; rge:RGE_33680; -.
DR PATRIC; fig|983917.3.peg.3293; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_564837_0_0_4; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000007883; 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 CDD; cd01982; Chlide_reductase_Z; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR InterPro; IPR010244; BchZ.
DR InterPro; IPR050152; ChlB/BchB/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 3: Inferred from homology;
KW Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..487
FT /note="Chlorophyllide reductase subunit Z"
FT /id="PRO_0000219850"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54063 MW; 057CCEE22694F62E CRC64;
MYVIDHDRAG GYWGAVYVFT AIKGLQVVID GPVGCENLPA TAVLHYTDAL PPHELPIVVT
GLGEEELGRE GTEGAMKRAH SVLDPDLPAV VVTGSIAEMI GGGVTPEGTT IQRFLPRTID
EDQWQCANRA MFWLWSEYGL RKIPQRTPFE QRPAGEKPRV NIIGPSYGTF NMPSDLAEIR
RLVEGIGAEV NMVFPLGSHL ADVQKLVDAD VNVCMYREFG RMLCEALERP YLQAPIGMHS
TTAFLRELGR LLNLDPEPFI EREKHTTLKP IWDLWRSVTQ DFFGTANFGI VAGETYARGV
RHFLEDELGL PCNFAVARKA GEKTDNESVR ELVHTKTPLV LFGSYNERMY LAETTSGHGP
KPAYIPASFP GAIIRRHTGT PFMGYAGATY LVQEFCNALF DALFNILPLG TELDRIDATP
SRRGDSRPWD DEAQQVLRDY VARQPVLVQI SAAKQLRDRA EREAGAAGEE RVTASRVRQL
LGQKEPA
//
