ID A0A210RWL8_9BURK Unreviewed; 430 AA.
AC A0A210RWL8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B6A14_06230 {ECO:0000313|EMBL:OWF65396.1};
OS Polynucleobacter hirudinilacicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1743166 {ECO:0000313|EMBL:OWF65396.1, ECO:0000313|Proteomes:UP000196880};
RN [1] {ECO:0000313|EMBL:OWF65396.1, ECO:0000313|Proteomes:UP000196880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-EgelM1-30-B4 {ECO:0000313|EMBL:OWF65396.1,
RC ECO:0000313|Proteomes:UP000196880};
RA Hahn M.W.;
RT "New species Polynucleobacter sp. MWH-EgelM1-30-B4.";
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:OWF65396.1}.
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DR EMBL; NAIA01000003; OWF65396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A210RWL8; -.
DR OrthoDB; 5714774at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000196880; 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 32..421
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT BINDING 32
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 57
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 118
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 430 AA; 47807 MW; E31F7E0711D371D7 CRC64;
MNAIVDLPKD HAGLVGKNIP IYKERGQREV FCGLTGIIWL HRKIQDAFFL VVGSRTCAHL
VQSAAGVMIF AEPRFATAII DDRDLAGIAD AHEELDRVVK ALLARRPDIK MLFLVGSCPS
EVIKLDLSRA AQRLNKEFLN HCRILSYSGS GIETTFTQGE DACLASLVNE IPKPTAVGEK
KLLVVGCLPD VVEDQFQRLF TELGIGQVSF FPPKNSQQKI EIDGNTQYLL AQPFLAETAR
LIEERGAKRI SAPFPFGVEG TTAWLKAAAN EWGITSPHFE QVTQARIERA RKSLARYLPM
LENKSISFFP DSQLEIPLAR FLSQECGMKV LEIGTPYLHK QHLEAELELL PEHSRIVEGQ
DVEKQLDRCR SDKPDIVVCG LGLANPLEAE GITTKWSIEL VFSPVHGYEQ AADLAELFAR
PLNRSMRLAA
//
