CHLL_CHLRE
ID CHLL_CHLRE Reviewed; 293 AA.
AC Q00469; B7U1F2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=chlL {ECO:0000255|HAMAP-Rule:MF_00355}; Synonyms=frxC, gidB;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2137;
RX PubMed=1392602; DOI=10.2307/3869460;
RA Suzuki J.Y., Bauer C.E.;
RT "Light-independent chlorophyll biosynthesis: involvement of the chloroplast
RT gene chlL (frxC).";
RL Plant Cell 4:929-940(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1581576; DOI=10.1007/bf00019214;
RA Huang C., Liu X.-Q.;
RT "Nucleotide sequence of the frxC, petB and trnL genes in the chloroplast
RT genome of Chlamydomonas reinhardtii.";
RL Plant Mol. Biol. 18:985-988(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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}.
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 Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC Rule:MF_00355};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; ChlL, ChlN and ChlB. {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC Rule:MF_00355}.
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DR EMBL; X60490; CAA43020.1; -; Genomic_DNA.
DR EMBL; X62905; CAA44691.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50099.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00912.1; -; Genomic_DNA.
DR PIR; JQ1675; JQ1675.
DR RefSeq; NP_958366.1; NC_005353.1.
DR AlphaFoldDB; Q00469; -.
DR SMR; Q00469; -.
DR STRING; 3055.DAA00912; -.
DR PaxDb; Q00469; -.
DR PRIDE; Q00469; -.
DR GeneID; 2717052; -.
DR KEGG; cre:ChreCp009; -.
DR eggNOG; ENOG502QW4A; Eukaryota.
DR HOGENOM; CLU_059373_2_0_1; -.
DR InParanoid; Q00469; -.
DR OrthoDB; 1086003at2759; -.
DR BioCyc; MetaCyc:CHRECP009-MON; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
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 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid; Reference proteome.
FT CHAIN 1..293
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000139554"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 180..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT VARIANT 25
FT /note="R -> A (in strain: 2137 and CC-503)"
SQ SEQUENCE 293 AA; 31945 MW; F0628502BC007D93 CRC64;
MKLAVYGKGG IGKSTTSCNI SIALRKRGKK VLQIGCDPKH DSTFTLTGFL IPTIIDTLSS
KDYHYEDIWP EDVIYGGYGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFFEYDVIL
FDVLGDVVCG GFAAPLNYAD YCIIVTDNGF DALFAANRIA ASVREKARTH PLRLAGLIGN
RTSKRDLIDK YVEACPMPVL EVLPLIEEIR ISRVKGKTLF EMSNKNNMTS AHMDGSKGDN
STVGVSETPS EDYICNFYLN IADQLLTEPE GVIPRELADK ELFTLLSDFY LKI
