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Database: UniProt
Entry: M9P8F1_9CHLO
LinkDB: M9P8F1_9CHLO
Original site: M9P8F1_9CHLO 
ID   M9P8F1_9CHLO            Unreviewed;       561 AA.
AC   M9P8F1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:0000313|EMBL:AFY64458.1};
OS   Pleodorina starrii.
OG   Plastid {ECO:0000313|EMBL:AFY64458.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Pleodorina.
OX   NCBI_TaxID=330485 {ECO:0000313|EMBL:AFY64458.1};
RN   [1] {ECO:0000313|EMBL:AFY64458.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIES-1363 {ECO:0000313|EMBL:AFY64458.1};
RX   PubMed=23300255; DOI=10.1093/molbev/mst002;
RA   Smith D.R., Hamaji T., Olson B.J., Durand P.M., Ferris P., Michod R.E.,
RA   Featherston J., Nozaki H., Keeling P.J.;
RT   "Organelle genome complexity scales positively with organism size in
RT   volvocine green algae.";
RL   Mol. Biol. Evol. 30:793-797(2013).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; JX977846; AFY64458.1; -; Genomic_DNA.
DR   RefSeq; YP_007890189.1; NC_021109.1.
DR   AlphaFoldDB; M9P8F1; -.
DR   GeneID; 15332319; -.
DR   UniPathway; UPA00670; -.
DR   GO; GO:0009507; C:chloroplast; 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: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   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|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW   Rule:MF_00352}; 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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00352};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00352}; Plastid {ECO:0000313|EMBL:AFY64458.1}.
FT   DOMAIN          94..537
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   BINDING         94
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         119
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         179
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   561 AA;  63446 MW;  31069A536EB54903 CRC64;
     MFTLQSKVTR EVKSLINKKN KNEIPLDCYT QLVYQTLLLT PRVHNNLEHL KNKKQRYNTI
     LSNFVNSAGD SSLYNLLFLN GLFECETGNY HTFCPISCVA WLYQKIEDSF FLVIGTKTCG
     YFLQNALGVM IFAEPRYAMA ELEESDISAQ LNDYKELKRL CLHIKQDRNP SVIVWIGTCT
     TEIIKMDLEG MAPRLEADIG LPIVVARANG LDYAFTQGED TVLSAMALAS LKQKTVPKIT
     SPVDTALHKI DVPQADQKNR QLNQRSIIPD TEKKNKANIH SLVLFGSVPS TVATQLTLEL
     KKEGITVSGW LPSQRYHDLP NFNKNTFVCG INPFLSRTAT TLMRRSKCTL ICAPFPIGPD
     GTRVWIEKIC GAFGICPSVN HSTALVTETK TKLQEREKFI FEGLEDYLKF IRGKSVFFMG
     DNLLEISLAR FLTRCGMIVY EIGIPYLDKR FQAAELALLE QTCKEMNVPM PRIVEKPDNY
     YQIQRIRELQ PDLTITGMAH ANPLEARGIT TKWSVEFTFA QIHGFTNTRE ILELVTRPLR
     RNLMCSLTTK AKGNKTASLA A
//
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