CHLN_TETOB
ID CHLN_TETOB Reviewed; 560 AA.
AC Q1KVX6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE Short=DPOR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE Short=LI-POR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00352};
GN Name=chlN {ECO:0000255|HAMAP-Rule:MF_00352};
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 NB-protein (ChlN-ChlB) is the
CC catalytic component of the complex. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00352};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00352};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00352}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC Rule:MF_00352}.
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DR EMBL; DQ396875; ABD48230.1; -; Genomic_DNA.
DR RefSeq; YP_635948.1; NC_008101.1.
DR AlphaFoldDB; Q1KVX6; -.
DR SMR; Q1KVX6; -.
DR GeneID; 4099815; -.
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 HAMAP; MF_00352; ChlN_BchN; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005970; Protochl_reductN.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01279; DPOR_bchN; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid.
FT CHAIN 1..560
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000324039"
FT REGION 173..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
SQ SEQUENCE 560 AA; 63976 MW; 94115EE94AA7A885 CRC64;
MTILLEEKEK LTFECETGNY HTFCPISCVS WLYQKIEDSF FLVIGTKTCG YFLQNALGVM
IFAEPRYAMA ELEESDISAK LNDYKELKRL CFQIKEDRNP SVIVWIGTCT TEIIKMDLEG
MAPELERELG IPIVVARANG LDYAFTQGED TVLAAMAQRC PSLPLNVEEK SQNSLFNQSS
NSPENLKTLN TKKDTFQNST ENSKTFSAEK KKTQNPFEFF KSLEEFFPSF SIQNNKKETI
LSKNSFVPFV EVEKNMYPLE SSENSKAESF YHLLREGEQT NQNSELVKPK LVLFGSLPNT
VATQLKLELN RQGIEISGWL PSTRYSDLPI LDTNTYVCGV NPFLSRTATT LMRRRKCKLI
SAPFPIGPDG TKAWIEKICS IYGKKPIGLE ERETKIWEGL EDSLKLVRGK SVFFMGDNLL
EISLARFLIR CGMIVYEIGI PYLDQRFQAA ELALLEKTCF EMNVPVPRIV EKPDNYYQIS
RIRELQPDLV ITGMAHANPL EARNITTKWS VEFTFAQIHG FTNAREILDL VTRPLRRNQN
INSFSEFFGS TTSTFVQNQF
