CHLN_PROMA
ID CHLN_PROMA Reviewed; 418 AA.
AC Q7VD37;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Pro_0546;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99591.1; -; Genomic_DNA.
DR RefSeq; NP_874939.1; NC_005042.1.
DR RefSeq; WP_011124700.1; NC_005042.1.
DR PDB; 2YNM; X-ray; 2.10 A; C=1-418.
DR PDBsum; 2YNM; -.
DR AlphaFoldDB; Q7VD37; -.
DR SMR; Q7VD37; -.
DR IntAct; Q7VD37; 1.
DR STRING; 167539.Pro_0546; -.
DR EnsemblBacteria; AAP99591; AAP99591; Pro_0546.
DR GeneID; 54199913; -.
DR KEGG; pma:Pro_0546; -.
DR PATRIC; fig|167539.5.peg.561; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_037170_0_0_3; -.
DR OMA; ISCVAWL; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000001420; 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..418
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000324008"
FT BINDING 17
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 42
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 103
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 4..9
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 258..283
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 393..410
FT /evidence="ECO:0007829|PDB:2YNM"
SQ SEQUENCE 418 AA; 46199 MW; 02458DD9AD581EE5 CRC64;
MSGSTLLKET GPREVFCGLT SIVWLHRRMP DAFFLVVGSR TCAHLIQSAA GVMIFAEPRF
GTAILEERDL AGLADAHEEL DRVVKSLLKR RPEIRTLFLV GSCPSEVIKI DLSRAAERLS
SQFNGQVRIL NYSGSGIETT FTQGEDGALK ALVPLMPSSQ EEQLLLAGTL ANPVEDRLKT
IFNRLGIQKV ESFPPRESTK LPAIGPGTKV LLAQPYLTDT ARELKDRGAE ILQAPFPLGV
EGSQLWIEAA ANAFKIKKTL VDATLEPLIT RAHKALKPYV EQLSGKKLFL LPESQLEIPL
ARFLSNECGM KLIEVGVPYL NREMMGPELD LLPQNTRIVE GQHVEKQLDR VREHHPDLVV
CGMGLANPLE AEGISTKWSI EMVFSPIHGI DQASDLAELF ARPLHRQNLL NKKTLEAV
