BCHN_RUBGI
ID BCHN_RUBGI Reviewed; 427 AA.
AC Q9JPA2; I0HUJ8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE Short=DPOR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE Short=LI-POR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00352};
GN Name=bchN {ECO:0000255|HAMAP-Rule:MF_00352}; OrderedLocusNames=RGE_33460;
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=983917;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=11343129; DOI=10.1007/s002390010163;
RA Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA Nagashima K.V.P.;
RT "Horizontal transfer of the photosynthesis gene cluster and operon
RT rearrangement in purple bacteria.";
RL J. Mol. Evol. 52:333-341(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=22689232; DOI=10.1128/jb.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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:0000255|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:0000255|HAMAP-Rule:MF_00352};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00352};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00352}.
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC Rule:MF_00352}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB034704; BAA94059.1; -; Genomic_DNA.
DR EMBL; AP012320; BAL96685.1; -; Genomic_DNA.
DR PIR; T50906; T50906.
DR AlphaFoldDB; Q9JPA2; -.
DR SMR; Q9JPA2; -.
DR STRING; 983917.RGE_33460; -.
DR EnsemblBacteria; BAL96685; BAL96685; RGE_33460.
DR KEGG; rge:RGE_33460; -.
DR PATRIC; fig|983917.3.peg.3271; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_037170_0_0_4; -.
DR OMA; ISCVAWL; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000007883; Chromosome.
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 HAMAP; MF_00352; ChlN_BchN; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005970; Protochl_reductN.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
DR TIGRFAMs; TIGR01279; DPOR_bchN; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome.
FT CHAIN 1..427
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208597"
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00352"
SQ SEQUENCE 427 AA; 46770 MW; C667B09EFACD7506 CRC64;
MNAVIDIAPA PMQQGCGDAP VLHERGQREV FCGLAGIVWL HRKIQDAFFL VVGSRTCAHL
LQSAAGVMIF AEPRFATAII DDRDLAGLAD ANAELDRVVT RLLERRPDIK MLFLVGSCPS
EVIKLDLSRA AERLSRNFSP RVRILSYTGS GIDTTFTQGE DTCLAALVPE LPASEQRALM
VVGSIADIVE DQFRRVFDGL GIGPVHFFPA RHAGDMPPVG PGTRFVLAQP FLADTARALE
ARGARRLAAP FPFGAEGTTL WLQAIAREFN VEATKFVSVV GPRRERAARA LARHRTQLEG
RKVFFFPDSQ LEVPLARFLA REMGMVPVEV GTPYLHRQLV ASELALLPAG TPLSEGQDLE
RQLDRCRAAR PDIVVCGLGL ANPLEAEGLT TKWSIELVFT PVHGFDQAAD LAELFTRPLE
RRTRLVA
