BCHX_CERS4
ID BCHX_CERS4 Reviewed; 333 AA.
AC Q02431; Q3J198; Q9RFC2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chlorophyllide reductase 35.5 kDa chain;
DE EC=1.3.7.15 {ECO:0000250|UniProtKB:P26177};
DE AltName: Full=Chlorin reductase;
GN Name=bchX; OrderedLocusNames=RHOS4_18680; ORFNames=RSP_0262;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8437569; DOI=10.1007/bf00277117;
RA McGlynn P., Hunter C.N.;
RT "Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides.";
RL Mol. Gen. Genet. 236:227-234(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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:P26177}.
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:P26177};
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:P26177};
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:P26177};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:D5ANS3};
CC Note=Binds 1 [4Fe-4S] cluster per dimer.
CC {ECO:0000250|UniProtKB:D5ANS3};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Homodimer (By similarity). Chlorophyllide reductase is
CC composed of three subunits; BchX, BchY and BchZ (By similarity).
CC {ECO:0000250|UniProtKB:D5ANS3, ECO:0000250|UniProtKB:P26178}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR EMBL; AJ010302; CAB38747.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24297.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79436.1; -; Genomic_DNA.
DR PIR; S30915; S30915.
DR PIR; T50753; T50753.
DR RefSeq; WP_002720427.1; NZ_CP030271.1.
DR RefSeq; YP_353337.1; NC_007493.2.
DR AlphaFoldDB; Q02431; -.
DR SMR; Q02431; -.
DR STRING; 272943.RSP_0262; -.
DR EnsemblBacteria; ABA79436; ABA79436; RSP_0262.
DR GeneID; 57470581; -.
DR GeneID; 67446996; -.
DR KEGG; rsp:RSP_0262; -.
DR PATRIC; fig|272943.9.peg.2206; -.
DR eggNOG; COG1348; Bacteria.
DR OMA; CQKVIVV; -.
DR PhylomeDB; Q02431; -.
DR BioCyc; MetaCyc:MON-13259; -.
DR BRENDA; 1.3.7.15; 5383.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010246; BchX.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02016; BchX; 1.
DR PROSITE; PS00746; NIFH_FRXC_1; 1.
DR PROSITE; PS00692; NIFH_FRXC_2; 1.
DR PROSITE; PS51026; NIFH_FRXC_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome.
FT CHAIN 1..333
FT /note="Chlorophyllide reductase 35.5 kDa chain"
FT /id="PRO_0000139549"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 219..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="G -> A (in Ref. 2; AAF24297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35576 MW; 077489BEB7FF7D63 CRC64;
MTDAPELKAF DQRLRDEAAE EPTLEVPQGE PKKKTQVIAI YGKGGIGKSF TLANLSYMMA
QIGKRVLLIG CDPKSDTTSL LFGGKACPTI IETSARKKLA GEEVQIGDVC FKRDGVFAME
LGGPEVGRGC GGRGIIHGFE LLEKLGFHDW DFDYVLLDFL GDVVCGGFGL PIARDMAQKV
ILVGSNDLQS LYVTNNVCSA VEYFRKLGGN VGVAGLVINK DDGTGEAKAF AEAADIPILA
TIPADEDLRR KSANYQIVGI PGTQWGPLFE GLAHAVGEAP PIRPKPLSQD GLLDLFTPEA
IGADFKLEPA TDADMRGKNA AAKKSLEVIY DDA
