ID S9RCY3_9RHOB Unreviewed; 426 AA.
AC S9RCY3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=Salmuc_00111 {ECO:0000313|EMBL:EPX75985.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX75985.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX75985.1}.
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DR EMBL; APVH01000062; EPX75985.1; -; Genomic_DNA.
DR RefSeq; WP_020042513.1; NZ_KE557285.1.
DR AlphaFoldDB; S9RCY3; -.
DR STRING; 1123237.Salmuc_00111; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_037170_0_0_5; -.
DR OrthoDB; 5714774at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000015347; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000015347}.
FT DOMAIN 27..374
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 27
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 52
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 113
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 426 AA; 46234 MW; 694F927438DFD2C2 CRC64;
MSCAAAPETG CRNAPVLRER GQHEVFCGLT GIIWLHRKMQ DAFFLVVGSR TCAHLLQSAA
GVMIFAEPRF GTAILEETDL AGMADAQAEL EREVDRLLAR RGDIRQLFLV GSCPSEVIKL
DLARAAERLS ARYGPQVRVL NYSGSGIETT FTEGEDACLA AMVPALPETQ ARELLLVGAL
PDVVEDQALA LLAELGIGPV RVLPARRAED DCAIGPNTVF ALTQPFLGGT LAALERRGAR
HIPAPFPFGE EGTTLWLRAV AREFGVEPAR FDAVTQAPRA RARRAVARAS EGLKGRSVFF
FPDSQLEIPL ARFLTRECGM EAVEVAAPYI HRRVVGPDLD LLAEGPVLAE GQDVERQLDR
CRAARPDLTV CGLGLANPLE AEGLATKWAI ELVFTPVHFY EQAGDLAGLF SRPLRRRAAL
RLEAAE
//
