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CHLL_TETOB
ID   CHLL_TETOB              Reviewed;         289 AA.
AC   Q1KVR9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 393;
RX   PubMed=16638149; DOI=10.1186/1471-2148-6-37;
RA   de Cambiaire J.-C., Otis C., Lemieux C., Turmel M.;
RT   "The complete chloroplast genome sequence of the chlorophycean green alga
RT   Scenedesmus obliquus reveals a compact gene organization and a biased
RT   distribution of genes on the two DNA strands.";
RL   BMC Evol. Biol. 6:37-37(2006).
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; DQ396875; ABD48288.1; -; Genomic_DNA.
DR   RefSeq; YP_636005.1; NC_008101.1.
DR   AlphaFoldDB; Q1KVR9; -.
DR   SMR; Q1KVR9; -.
DR   GeneID; 4099798; -.
DR   UniPathway; UPA00670; -.
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.
FT   CHAIN           1..289
FT                   /note="Light-independent protochlorophyllide reductase
FT                   iron-sulfur ATP-binding protein"
FT                   /id="PRO_0000275267"
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"
SQ   SEQUENCE   289 AA;  31812 MW;  CC4E62A71ADCA1C4 CRC64;
     MKLAVYGKGG IGKSTTSCNI SIALAKRGKK VLQIGCDPKS DSTFTLTGFL IPTIIDTLQA
     KDYHYEDVWP EDVIYQGYAG VDCVEAGGPP AGAGCGGYVV GETVKLLKEF NAFYEYDVIL
     FDVLGDVVCG GFAAPLNYAD YCIIVTDNGF DALFAANRIT ASVREKARTH PLRLAGLIGN
     RTKKRDLIEK YVETCPMPIL EVLPLIEDIR VSRVKGKTLF EMTESEPTLQ FVCDFYLNIA
     DQLLTQPEGV IPRELGDREL FNLLSNFYLN SSNSTNTTLK NETNLFDLV
 
 
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