ID A0A257R636_9PROT Unreviewed; 422 AA.
AC A0A257R636;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=bchN {ECO:0000256|HAMAP-Rule:MF_00352};
GN ORFNames=B7Z76_05780 {ECO:0000313|EMBL:OYV56415.1};
OS Acidiphilium sp. 20-67-58.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1970291 {ECO:0000313|EMBL:OYV56415.1, ECO:0000313|Proteomes:UP000216756};
RN [1] {ECO:0000313|EMBL:OYV56415.1, ECO:0000313|Proteomes:UP000216756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20-67-58 {ECO:0000313|EMBL:OYV56415.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYV56415.1}.
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DR EMBL; NCAS01000011; OYV56415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257R636; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000216756; 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 25..410
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT BINDING 25
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 50
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 111
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 422 AA; 45286 MW; 26EDCA717EA355A8 CRC64;
MSACTTSPAA PPAIIAERGQ REVFCGLTGI VWLHRRIQDA FFLVVGSRTC AHLLQSAAGV
MIFAEPRFAT AIIEERDLAG RADLDDELDR VATRLIARRP DIRLLFLVGS CPSEVIRLDL
GRAAARLEER FGRSPRVLAY SGSGIGTTFT EGEDACLSAL VPTLAPAPGP ATRLLVVGAL
ADVVEDQFRR LFAALGIATV DFLPARRADA MPPVGPFTRY VLAQPFLGET ATALERRGAV
QIAAPCPLGA EGTRLWFESI AAAFGIDPAH VDGVLSLPVR RATAALAAPR ARLAGRRVFL
FPDSQLEIPL ARFLARECGM ILTEVGTPFL NRRLMAPDLA LLPADAQLAE GQDVARQLDR
CRAARPDLVV CGLGLANPLE AEGFATKWSI ELVFSPIQGF EQAADLAALF ARPLARRALL
EV
//
