ID A0A2V2LFE6_9RHOB Unreviewed; 289 AA.
AC A0A2V2LFE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-OCT-2025, entry version 27.
DE RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000256|HAMAP-Rule:MF_00355};
DE Short=DPOR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE Short=LI-POR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00355};
GN Name=bchL {ECO:0000256|HAMAP-Rule:MF_00355};
GN ORFNames=DKT77_03525 {ECO:0000313|EMBL:PWR04155.1};
OS Meridianimarinicoccus roseus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Meridianimarinicoccus.
OX NCBI_TaxID=2072018 {ECO:0000313|EMBL:PWR04155.1, ECO:0000313|Proteomes:UP000245680};
RN [1] {ECO:0000313|EMBL:PWR04155.1, ECO:0000313|Proteomes:UP000245680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TG-679 {ECO:0000313|EMBL:PWR04155.1,
RC ECO:0000313|Proteomes:UP000245680};
RA Ren Y.;
RT "Rhodobacteraceae gen. nov., sp. nov. isolated from sea water.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2
CC phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] +
CC 2 ATP + 2 H2O; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA-
CC COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722,
CC ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348,
CC ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC Rule:MF_00355};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000256|HAMAP-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; BchL, BchN and BchB. {ECO:0000256|HAMAP-Rule:MF_00355}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|HAMAP-Rule:MF_00355,
CC ECO:0000256|RuleBase:RU003688}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWR04155.1}.
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DR EMBL; QGKU01000012; PWR04155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2LFE6; -.
DR OrthoDB; 9778641at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000245680; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR CDD; cd02032; Bchl-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01281; DPOR_bchL; 1.
DR PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR PRINTS; PR00091; NITROGNASEII.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00355};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Bacteriochlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023181,
KW ECO:0000256|HAMAP-Rule:MF_00355};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00355};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00355};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00355}; Reference proteome {ECO:0000313|Proteomes:UP000245680}.
FT BINDING 33..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 203..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
SQ SEQUENCE 289 AA; 31524 MW; 4959CE5481B4902B CRC64;
MKGRDGEGSV QVHQDDSMKI EGAKVFSVYG KGGIGKSTTS SNLSAAFAKL GKRVLQIGCD
PKHDSTFTLT GSLVPTVIDI LKEVDFHAEE LRPEDFVFDG WGGVKCVEAG GPPAGTGCGG
YVVGQTVKLL KQHHMLEDTD VVIFDVLGDV VCGGFAAPLQ HADKAVIVTA NDFDSIYAMN
RIIAAVQAKS NNYKVRLAGC IANRSRDTDE VDRYCDRVGF KRIGHMPDVD ALRRSRLKKK
TLFEMPDEED IVQCRAEYIR LAEALYNGTE SHAPAPLPDR EIFELLGFD
//
