BCHL_CERS4
ID BCHL_CERS4 Reviewed; 297 AA.
AC Q9RFD6; Q3J173; Q9Z5E1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_00355};
DE Short=DPOR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE Short=LI-POR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00355};
GN Name=bchL {ECO:0000255|HAMAP-Rule:MF_00355}; OrderedLocusNames=RHOS4_18930;
GN ORFNames=RSP_0288;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Naylor G.W., Addlesee H.A., Gibson L.C.D., Hunter C.N.;
RT "The photosynthesis gene cluster of Rhodobacter sphaeroides.";
RL Photosyn. Res. 62:121-139(1999).
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.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 2-297 IN COMPLEX WITH 4FE-4S
RP CLUSTER AND MG-ADP, FUNCTION, SUBUNIT, AND COFACTOR.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=19006326; DOI=10.1021/bi801058r;
RA Sarma R., Barney B.M., Hamilton T.L., Jones A., Seefeldt L.C., Peters J.W.;
RT "Crystal structure of the L protein of Rhodobacter sphaeroides light-
RT independent protochlorophyllide reductase with MgADP bound: a homologue of
RT the nitrogenase Fe protein.";
RL Biochemistry 47:13004-13015(2008).
CC -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC reaction is light-independent. The L component serves as a unique
CC electron donor to the NB-component of the complex, and binds Mg-ATP.
CC {ECO:0000255|HAMAP-Rule:MF_00355, ECO:0000269|PubMed:19006326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC 4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00355};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00355,
CC ECO:0000269|PubMed:19006326};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC Rule:MF_00355, ECO:0000269|PubMed:19006326};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer (PubMed:19006326). Protochlorophyllide reductase is
CC composed of three subunits; BchL, BchN and BchB. {ECO:0000255|HAMAP-
CC Rule:MF_00355, ECO:0000269|PubMed:19006326}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC Rule:MF_00355}.
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DR EMBL; AF195122; AAF24272.1; -; Genomic_DNA.
DR EMBL; AJ010302; CAB38722.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79461.1; -; Genomic_DNA.
DR PIR; T50728; T50728.
DR RefSeq; WP_011338126.1; NZ_CP030271.1.
DR RefSeq; YP_353362.1; NC_007493.2.
DR PDB; 3FWY; X-ray; 1.63 A; A/B=2-297.
DR PDB; 6UYK; X-ray; 2.60 A; A/B/C/D=1-297.
DR PDBsum; 3FWY; -.
DR PDBsum; 6UYK; -.
DR AlphaFoldDB; Q9RFD6; -.
DR SMR; Q9RFD6; -.
DR STRING; 272943.RSP_0288; -.
DR EnsemblBacteria; ABA79461; ABA79461; RSP_0288.
DR GeneID; 57470606; -.
DR GeneID; 67447021; -.
DR KEGG; rsp:RSP_0288; -.
DR PATRIC; fig|272943.9.peg.2232; -.
DR eggNOG; COG1348; Bacteria.
DR OMA; EVDFHHE; -.
DR PhylomeDB; Q9RFD6; -.
DR BRENDA; 1.3.7.7; 5383.
DR UniPathway; UPA00671; -.
DR EvolutionaryTrace; Q9RFD6; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR DisProt; DP02993; -.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00355; ChlL_BchL; 1.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005971; Protochlorophyllide_ATP-bd.
DR PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01281; DPOR_bchL; 1.
DR PROSITE; PS00746; NIFH_FRXC_1; 1.
DR PROSITE; PS00692; NIFH_FRXC_2; 1.
DR PROSITE; PS51026; NIFH_FRXC_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..297
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000139582"
FT BINDING 41..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 211..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19006326"
FT BINDING 235..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19006326"
FT CONFLICT 14
FT /note="G -> V (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> A (in Ref. 2; CAB38722)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..262
FT /note="AA -> VV (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="L -> V (in Ref. 2; CAB38722)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> F (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="D -> Y (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> R (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> E (in Ref. 1; AAF24272)"
FT /evidence="ECO:0000305"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:3FWY"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:3FWY"
FT TURN 196..200
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:3FWY"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:3FWY"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 257..275
FT /evidence="ECO:0007829|PDB:3FWY"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:3FWY"
SQ SEQUENCE 297 AA; 32295 MW; BDDE6F40A21952CE CRC64;
MSPKDLTIPT GADGEGSVQV HLDEADKITG AKVFAVYGKG GIGKSTTSSN LSAAFSILGK
RVLQIGCDPK HDSTFTLTGS LVPTVIDVLK DVDFHPEELR PEDFVFEGFN GVMCVEAGGP
PAGTGCGGYV VGQTVKLLKQ HHLLDDTDVV IFDVLGDVVC GGFAAPLQHA DQAVVVTAND
FDSIYAMNRI IAAVQAKSKN YKVRLAGCVA NRSRATDEVD RFCKETNFRR LAHMPDLDAI
RRSRLKKKTL FEMDEDQDVL AARAEYIRLA ESLWRGLDPI DPHSLPDRDI FELLGFD
