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Light-independent protochlorophyllide reductase subunit N (DPOR subunit N) (LI-POR subunit N) (EC 1.3.7.7)

 W6MDC7_ACEAT            Unreviewed;       486 AA.
W6MDC7;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
05-DEC-2018, entry version 14.
RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
Short=DPOR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
Short=LI-POR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00352};
Name=chlN {ECO:0000256|HAMAP-Rule:MF_00352,
ECO:0000313|EMBL:CDI27960.1};
Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia
mediterranea).
Plastid; Chloroplast {ECO:0000313|EMBL:CDI27960.1}.
Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Dasycladales;
Polyphysaceae; Acetabularia.
NCBI_TaxID=35845 {ECO:0000313|EMBL:CDI27960.1};
[1] {ECO:0000313|EMBL:CDI27960.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DI1 {ECO:0000313|EMBL:CDI27960.1};
Gould S.;
Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CDI27960.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DI1 {ECO:0000313|EMBL:CDI27960.1};
De Vries J., Habicht J., Woehle C., Changjie H., Christa G.,
Martin W.F., Gould S.B.;
"Is ftsH the key to plastid longevity in sacoglossan slugs?";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Component of the dark-operative protochlorophyllide
reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
(Chlide). This reaction is light-independent. The NB-protein
(ChlN-ChlB) is the catalytic component of the complex.
{ECO:0000256|HAMAP-Rule:MF_00352}.
-!- CATALYTIC ACTIVITY:
Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-
[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide
a + reduced 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:28202,
Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350,
ChEBI:CHEBI:456216; EC=1.3.7.7; Evidence={ECO:0000256|HAMAP-
Rule:MF_00352};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00352};
Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is
bound at the heterodimer interface by residues from both subunits.
{ECO:0000256|HAMAP-Rule:MF_00352};
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis (light-independent). {ECO:0000256|HAMAP-
Rule:MF_00352}.
-!- SUBUNIT: Protochlorophyllide reductase is composed of three
subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB
and two ChlN subunits. {ECO:0000256|HAMAP-Rule:MF_00352}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
Rule:MF_00352}.
-!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
Rule:MF_00352}.
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EMBL; HG518434; CDI27960.1; -; Genomic_DNA.
UniPathway; UPA00670; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
HAMAP; MF_00352; ChlN_BchN; 1.
InterPro; IPR000510; Nase/OxRdtase_comp1.
InterPro; IPR005970; Protochl_reductN.
Pfam; PF00148; Oxidored_nitro; 1.
PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
TIGRFAMs; TIGR01279; DPOR_bchN; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00352};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352};
Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
Chloroplast {ECO:0000313|EMBL:CDI27960.1};
Iron {ECO:0000256|HAMAP-Rule:MF_00352};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00352};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00352};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00352};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00352};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
Plastid {ECO:0000313|EMBL:CDI27960.1}.
DOMAIN 46 467 Oxidored_nitro.
{ECO:0000259|Pfam:PF00148}.
METAL 46 46 Iron-sulfur (4Fe-4S); shared with
heterodimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00352}.
METAL 71 71 Iron-sulfur (4Fe-4S); shared with
heterodimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00352}.
METAL 131 131 Iron-sulfur (4Fe-4S); shared with
heterodimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00352}.
SEQUENCE 486 AA; 55177 MW; 843BCD210FE96F10 CRC64;
MKRLHIDQRS FKILKYKKKT KNMTTNILSN EKIVFECETG NYHTFCPISC VAWLYQKIED
SFFLVIGTKT CGYFLQNALG VMIFAEPRYA MAELEESDIS AQLNDYKELK RICFQIKQDR
NPSVIVWIGT CTTEIIKMDL EGMAPNIEKE IQIPIVVARA NGLDYAFTQG EDTVLAALAQ
RCPTVPAQLN RRGETPSTLP DGEKNSSTLE GAKPLLHSGN KQPSLVLFGS VPNTVATQLS
NELKLQGITV NGWLPAQRYN ELPVLNENTY VCGINPFLSR TATTLMRRKK CKLIGAPFPI
GPDGTRCWIE KICSVLNINP NNLLERETNI WNNLEEYLKL IQGKSVFFMG DNLLEISLAR
FLIRCGMIVY EIGIPYLDKR FQACELTLLK QTCIEMKVPM PRIVEKPDNY NQIQRIRELK
PDLVITGLSL ANPLEARGIT TKWSVEFTFS QIHGFTNARD ILELVTRPIR RNTNLTSLGW
NTLVLK


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