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Database: UniProt
Entry: H9A9C4_GINBI
LinkDB: H9A9C4_GINBI
Original site: H9A9C4_GINBI 
ID   H9A9C4_GINBI            Unreviewed;       459 AA.
AC   H9A9C4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            Short=DPOR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            Short=LI-POR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00352};
GN   Name=chlN {ECO:0000256|HAMAP-Rule:MF_00352,
GN   ECO:0000313|EMBL:AEX99053.1};
GN   ORFNames=GinbiCp071 {ECO:0000313|EMBL:AEX99053.1};
OS   Ginkgo biloba (Ginkgo) (Maidenhair tree).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEX99053.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX   NCBI_TaxID=3311 {ECO:0000313|EMBL:AEX99053.1};
RN   [1] {ECO:0000313|EMBL:AEX99053.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li X., Li Q., Lin X., Hu Z., Chen S.;
RT   "High-throughput multiplex sequencing reveals the prospect of chloroplast
RT   genomes as a plant super-barcode.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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 NB-protein (ChlN-ChlB) is the
CC       catalytic component of the complex. {ECO:0000256|HAMAP-Rule:MF_00352}.
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_00352};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00352};
CC       Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at
CC       the heterodimer interface by residues from both subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00352};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000256|HAMAP-Rule:MF_00352}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC       ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00352}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00352}.
CC   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; JN867578; AEX98468.1; -; Genomic_DNA.
DR   EMBL; JN867585; AEX99053.1; -; Genomic_DNA.
DR   RefSeq; YP_005352755.1; NC_016986.1.
DR   AlphaFoldDB; H9A9C4; -.
DR   GeneID; 11935067; -.
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   CDD; cd01979; Pchlide_reductase_N; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   HAMAP; MF_00352; ChlN_BchN; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR005970; Protochl_reductN.
DR   NCBIfam; TIGR01279; DPOR_bchN; 1.
DR   PANTHER; PTHR39429; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1.
DR   PANTHER; PTHR39429:SF3; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00352};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Chloroplast {ECO:0000313|EMBL:AEX99053.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Plastid {ECO:0000313|EMBL:AEX99053.1}.
FT   DOMAIN          20..436
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00352"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00352"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00352"
SQ   SEQUENCE   459 AA;  51808 MW;  46A80A04F7D8DB61 CRC64;
     MKISENLTFE CETGNYHTFC PISCVSWLYQ KIEDSSFLVV GTKTCGYFLQ NALGVMIFAE
     PRYAMAELEE GDISAQLNDY EELKRLCIRI GKDRDPSVII WIGTCTTEII KMDLEGMAPK
     LECEMGIPIV VARANGLDYA FTQGEDTVLA AMVHRCLGQE SSVREQNGII RNSFYFSSPE
     KEEELVEDEN HPPLVLFGSL PSDVVSQPNP ELKRQSVKVS GWLPAQKYTD LPSLVDGVYV
     CGVNPFLSRT ATTLVRRDKC ELIVAPFPIG PDGTRAWIEK ICPVFGIETE GLEEREERIW
     EGLKDYPDLI RGKSAFFMGD NILEVSLARF LIRCGMIVDE IGIPYIDKRY QAAELALLRD
     TCIRMCVPIP RIVEKPDNYN QIRRMRELQP DLAITGMAHA NPLEARGIGT KWSVEFTSAQ
     IHGFANARDV LELVTRPLRR NDNLEDLGRT APVRRDNKL
//
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