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Database: UniProt
Entry: M2WWR6_GALSU
LinkDB: M2WWR6_GALSU
Original site: M2WWR6_GALSU 
ID   M2WWR6_GALSU            Unreviewed;       288 AA.
AC   M2WWR6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=chlL {ECO:0000313|EMBL:AIG92618.1};
GN   ORFNames=Gasu_40000 {ECO:0000313|EMBL:EME28455.1};
OS   Galdieria sulphuraria (Red alga).
OG   Plastid {ECO:0000313|EMBL:AIG92618.1}.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME28455.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
RN   [2] {ECO:0000313|EMBL:EME28455.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=074W {ECO:0000313|EMBL:EME28455.1};
RA   Schoenknecht G., Chen W.-H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.M.;
RT   "Gene Transfer from Bacteria and Archaea Facilitated Evolution of an
RT   Extremophilic Eukaryote.";
RL   Science 0:0-0(2013).
RN   [3] {ECO:0000313|EMBL:AIG92618.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=074W {ECO:0000313|EMBL:AIG92618.1};
RX   PubMed=25552531;
RA   Jain K., Krause K., Grewe F., Nelson G.F., Weber A.P., Christensen A.C.,
RA   Mower J.P.;
RT   "Extreme features of the Galdieria sulphuraria organellar genomes: a
RT   consequence of polyextremophily?";
RL   Genome Biol. Evol. 7:367-380(2015).
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   -!- 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}.
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DR   EMBL; KJ700459; AIG92618.1; -; Genomic_DNA.
DR   EMBL; KB454519; EME28455.1; -; Genomic_DNA.
DR   RefSeq; XP_005704975.1; XM_005704918.1.
DR   RefSeq; YP_009051176.1; NC_024665.1.
DR   AlphaFoldDB; M2WWR6; -.
DR   STRING; 130081.M2WWR6; -.
DR   EnsemblPlants; EME28455; EME28455; Gasu_40000.
DR   GeneID; 17087287; -.
DR   GeneID; 20005692; -.
DR   Gramene; EME28455; EME28455; Gasu_40000.
DR   KEGG; gsl:Gasu_40000; -.
DR   KEGG; gsl:JL72_p031; -.
DR   eggNOG; ENOG502QW4A; Eukaryota.
DR   OrthoDB; 5482494at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
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};
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}; Magnesium {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:AIG92618.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
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   288 AA;  31642 MW;  3353A314653BAB40 CRC64;
     MKIAVYGKGG IGKSTTSCNI SVALAKRGKK VLQIGCDPKH DSTFTLTGFL IPTIIDTLQE
     KDYHYEDVWP EDVIYRGYGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFDEYDIIL
     FDVLGDVVCG GFAAPLNYAD YCIIVTDNGF DSLFAANRIA ASIREKARTH NLRLAGLIGN
     RTLKRDLIEQ YVKSIPMPIL EVLPLIEDIR VSRVKGKTLF EMAEEDSSLK YICNYYLNIA
     DQLISLPEGL VPKEANDREI FTLLSDFYLS PNLSSVPNNK EAEKLLIS
//
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