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Entry: A0A0N0JE40_9PROT
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ID   A0A0N0JE40_9PROT        Unreviewed;       305 AA.
AC   A0A0N0JE40;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
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:KPF50116.1};
GN   Synonyms=bchL {ECO:0000256|HAMAP-Rule:MF_00355};
GN   ORFNames=IP80_03750 {ECO:0000313|EMBL:KPF50116.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Proteobacteria; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF50116.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF50116.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF50116.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome
RT   Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide
CC       reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
CC       ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
CC       (Chlide). This reaction is light-independent. The L component
CC       serves as a unique electron donor to the NB-component of the
CC       complex, and binds Mg-ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
CC   -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
CC       ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
CC       phosphate. {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;
CC       bacteriochlorophyll biosynthesis (light-independent).
CC       {ECO:0000256|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; BchL, BchN and BchB. {ECO:0000256|HAMAP-
CC       Rule:MF_00355}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPF50116.1}.
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DR   EMBL; LJHW01000004; KPF50116.1; -; Genomic_DNA.
DR   RefSeq; WP_054138966.1; NZ_LJHW01000004.1.
DR   EnsemblBacteria; KPF50116; KPF50116; IP80_03750.
DR   PATRIC; fig|1523424.3.peg.2703; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000037849; 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-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
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   PANTHER; PTHR42864:SF1; PTHR42864:SF1; 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 {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037849};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037849}.
FT   NP_BIND      49     54       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     219    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     243    245       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   METAL        53     53       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       134    134       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       168    168       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   BINDING      78     78       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   305 AA;  33085 MW;  04836962401F84DC CRC64;
     MTETVTLPFP SLMKKAARGE DGEGSLQVQL DPSVKIGTAK VFAIYGKGGI GKSTTSSNLS
     AAFSMMGKRV LQIGCDPKHD STFTLTKKML PTVIDVLETV DFHAEELRVE DFVFPGYNGV
     MCVEAGGPPA GTGCGGYVVG QTVKLLKEHH LLEDTDVVIF DVLGDVVCGG FAAPLQHADR
     AMIVTANDFD SIFAMNRIVQ AIGAKAKNYN VRLGGVIANR SAATDQIDKY TAKIGLELAA
     HFPDLDVIRR SRLKKSVLFE METSPELEAV KREYMRLAAN LWLGDKSYSA VPMKDRDIFD
     LLGFD
//
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