ID A0A0U9HT71_KLENI Unreviewed; 289 AA.
AC A0A0U9HT71;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=chlLa {ECO:0000313|EMBL:GAQ93693.1};
GN Synonyms=chlL {ECO:0000256|HAMAP-Rule:MF_00355}, chlLb
GN {ECO:0000313|EMBL:GAQ93791.1};
GN ORFNames=KFL_018130120 {ECO:0000313|EMBL:GAQ93693.1}, KFL_018131470
GN {ECO:0000313|EMBL:GAQ93791.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OG Plastid; Chloroplast {ECO:0000313|EMBL:GAQ93693.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ93693.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ93693.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ93693.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
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=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: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; chlorophyll
CC biosynthesis (light-independent). {ECO:0000256|HAMAP-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; ChlL, ChlN and ChlB. {ECO:0000256|HAMAP-Rule:MF_00355}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF238762; GAQ93693.1; -; Genomic_DNA.
DR EMBL; DF238762; GAQ93791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U9HT71; -.
DR STRING; 105231.A0A0U9HT71; -.
DR InParanoid; A0A0U9HT71; -.
DR OrthoDB; 5482494at2759; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000054558; Chromosome Pltd.
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 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|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW Rule:MF_00355}; Chloroplast {ECO:0000313|EMBL:GAQ93693.1};
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}; Plastid {ECO:0000313|EMBL:GAQ93693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054558}.
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00355"
FT BINDING 180..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
SQ SEQUENCE 289 AA; 31731 MW; A7A19C8D19BBDC69 CRC64;
MKIAVYGKGG IGKSTTSCNI SIALARRGKR VLQIGCDPKH DSTFTLTGFL IPTIIDTLQS
KDYHYEDVWP EDVIYQGYGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFYEYDVIL
FDVLGDVVCG GFAAPLNYAD YCIIITDNGF DALFAANRIA ASVREKARTH PLRLAGLVGN
RTSKRDLIDK YVEACPMPVL EVLPLIEDIR VSRVKGKTLF EMAETEPSLS YVCDFYLNIA
DQILARPEGV VPKEVPDREL FSLLSDFYLN PTNQKAEQVP GEHLDFMMV
//
