CHLN_THEVB
ID CHLN_THEVB Reviewed; 460 AA.
AC Q8DGH2;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; OrderedLocusNames=tll2345;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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 -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC Rule:MF_00352}.
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DR EMBL; BA000039; BAC09897.1; -; Genomic_DNA.
DR RefSeq; NP_683135.1; NC_004113.1.
DR RefSeq; WP_011058178.1; NC_004113.1.
DR PDB; 2XDQ; X-ray; 2.40 A; A=1-460.
DR PDBsum; 2XDQ; -.
DR AlphaFoldDB; Q8DGH2; -.
DR SMR; Q8DGH2; -.
DR STRING; 197221.22296073; -.
DR PRIDE; Q8DGH2; -.
DR EnsemblBacteria; BAC09897; BAC09897; BAC09897.
DR KEGG; tel:tll2345; -.
DR PATRIC; fig|197221.4.peg.2458; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; ISCVAWL; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00670; -.
DR EvolutionaryTrace; Q8DGH2; -.
DR Proteomes; UP000000440; Chromosome.
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 PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
DR TIGRFAMs; TIGR01279; DPOR_bchN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..460
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208602"
FT BINDING 22
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 47
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 107
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 STRAND 10..13
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 81..96
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 353..369
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 402..409
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2XDQ"
SQ SEQUENCE 460 AA; 51509 MW; 9D3ED2EAF8ED4774 CRC64;
MTVTAPNALN FECETGNYHT FCPISCVAWL YQKIEDSFFL VIGTKTCGYF LQNAMGVMIF
AEPRYAMAEL EEGDISAQLN DYEELKRLCL EIKRDRNPSV IVWIGTCTTE IIKMDLEGLA
PKLEAEIGIP IVVARANGLD YAFTQGEDTV LAAMAARCPT STAISDPEER NPIQRLLNFG
KKKEEVQAQS SQYHPHPPLV LFGSLPDPVV TQLTLELKKQ GIKVSGWLPA KRYTELPVID
EGYYVAGVNP FLSRTATTLI RRRKCQLITA PFPIGPDGTR TWIEQICATF GIQPQGLAER
EAETWQKLSD YLELVRGKSV FFMGDNLLEI SLARFLIRCG MRVLEIGIPY MDKRYQAAEL
ALLSQTCAEM GHPLPTIVEK PDNYNQLQRI KALQPDLVIT GMAHANPLEA RGISTKWSVE
FTFAQIHGFG NARDILELVT RPLRRNQALA GLGWQKLVAH
