ID A0A1L9QL26_9CYAN Unreviewed; 467 AA.
AC A0A1L9QL26;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:0000256|HAMAP-Rule:MF_00352};
GN ORFNames=BI308_22190 {ECO:0000313|EMBL:OJJ18407.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ18407.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ18407.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ18407.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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: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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00352}.
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
CC Rule:MF_00352}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJJ18407.1}.
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DR EMBL; MLAW01000055; OJJ18407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9QL26; -.
DR STRING; 1925591.BI308_22190; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000183940; Unassembled WGS sequence.
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 PIRSF; PIRSF000162; P_chlorophyll_rd; 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}; Reference proteome {ECO:0000313|Proteomes:UP000183940}.
FT DOMAIN 24..444
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00352"
SQ SEQUENCE 467 AA; 53048 MW; BE11E6C2E13BAAB9 CRC64;
MTVAQPETSA LNFECETGNY HTFCPISCVA WLYQKIEDSF FLVIGTKTCG YFLQNAMGVM
IFAEPRYAMA ELEEGDISAK LNDYEELKRL CEQIKRDRNP SVIVWIGTCT TEIIKMDLEG
LAPKLEAEIG IPIVVARANG LDYAFTQGED TVLAAMAARC PKTVEQPEEK EERNAIQRLL
TFGKKKEEVA QEESEYVNHP PLVLFGSVPD PIVTQLTLEL KRHGIKVSGW LPAKRYTELP
VLEEGYYVSG VNPFLSRTAT TLMRRRKCKL IGAPFPIGPD GTRAWIEKIC SVFNIEPKGL
AEREQQIWES VEDYLQLVRG KSVFFMGDNL LEISQARFLI RCGMIVHEIG IPYMDKRYQG
AELALLEKTC QEMGAPLPNI VEKPDNYNQI QRIYDLQPDL VITGMAHANP MEARGINTKW
SVEFTFAQIH GFTNTRDILE LVTRPLRRNN NLKDLGWEKL VKEEARV
//
