ID A0A0N1AVR7_9SPHN Unreviewed; 437 AA.
AC A0A0N1AVR7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=bchN {ECO:0000256|HAMAP-Rule:MF_00352};
GN ORFNames=IP79_14290 {ECO:0000313|EMBL:KPF62021.1};
OS Porphyrobacter sp. AAP60.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF62021.1, ECO:0000313|Proteomes:UP000037996};
RN [1] {ECO:0000313|EMBL:KPF62021.1, ECO:0000313|Proteomes:UP000037996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP60 {ECO:0000313|EMBL:KPF62021.1,
RC ECO:0000313|Proteomes:UP000037996};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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 (BchN-BchB) 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; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000256|HAMAP-Rule:MF_00352}.
CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN
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:KPF62021.1}.
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DR EMBL; LJHV01000023; KPF62021.1; -; Genomic_DNA.
DR RefSeq; WP_054119954.1; NZ_LJHV01000023.1.
DR AlphaFoldDB; A0A0N1AVR7; -.
DR STRING; 1523423.IP79_14290; -.
DR PATRIC; fig|1523423.3.peg.1757; -.
DR OrthoDB; 5714774at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000037996; 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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
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 Bacteriochlorophyll biosynthesis {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}.
FT DOMAIN 39..427
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT BINDING 39
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 64
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 125
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 437 AA; 48188 MW; D6D270E948AE0263 CRC64;
MSPLAILDGC ATERAPATPA ASEQPRPVLR ERGQREVFCG LTGIIWLHRK MQDAFFLVVG
SRTCAHLLQS AAGVMIFAEP RFATAIMEER DLAGMVDAQD ELDRVVTRLL ERRPDIRTLF
LVGSCPSEVI KLDLAKAAQR LGAQYMPRVR ILNYSGSGIE TTFTQGEDAC LAALVPVMPA
LAADAPKELL IVGSLPDIVE DQFLRLFAEM GIAKVGCLPS RNARELPSVG ANTRYLLAQP
FLGDTAMALE GRGARRIEAL FPFGVEGTSD WLRSAAREFG IDAALVEKII APGRERARIA
LSKLRPQLEG KRITFLPDSQ LEVPLARYLQ DELGMELVEV GTPYLHRAHL ARELDRFGPQ
VRVSEGQHLE RQLDRVRADR PDITVCGLGL ANPLEGEGLT TKWAIELVFS PIHGFDQAAD
LAELFARPLR RRDMLEV
//
