BCHN_CERS4
ID BCHN_CERS4 Reviewed; 428 AA.
AC Q9RFD4; Q3J176; Q9Z5D8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=RHOS4_18900;
GN ORFNames=RSP_0285;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Naylor G.W., Addlesee H.A., Gibson L.C.D., Hunter C.N.;
RT "The photosynthesis gene cluster of Rhodobacter sphaeroides.";
RL Photosyn. Res. 62:121-139(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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: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}.
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DR EMBL; AF195122; AAF24275.1; -; Genomic_DNA.
DR EMBL; AJ010302; CAB38725.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79458.1; -; Genomic_DNA.
DR PIR; T50731; T50731.
DR RefSeq; WP_002720449.1; NZ_CP030271.1.
DR RefSeq; YP_353359.1; NC_007493.2.
DR AlphaFoldDB; Q9RFD4; -.
DR SMR; Q9RFD4; -.
DR STRING; 272943.RSP_0285; -.
DR EnsemblBacteria; ABA79458; ABA79458; RSP_0285.
DR KEGG; rsp:RSP_0285; -.
DR PATRIC; fig|272943.9.peg.2229; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; ISCVAWL; -.
DR PhylomeDB; Q9RFD4; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002703; Chromosome 1.
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..428
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208598"
FT BINDING 29
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 54
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 115
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 CONFLICT 62
FT /note="A -> G (in Ref. 2; CAB38725)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..301
FT /note="Missing (in Ref. 2; CAB38725)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="S -> R (in Ref. 2; CAB38725)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="P -> A (in Ref. 2; CAB38725)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="P -> A (in Ref. 2; CAB38725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 46119 MW; B357968A7D3B60D5 CRC64;
MSLDLPPPPA RGCRSTEVLK ERGQREVFCG LTGIIWLHRK MQDAFFLVVG SRTCAHLLQS
AAGVMIFAEP RFGTAVLEEK DLAGLADANA ELDREVDRLL ARRPDIRQLF LVGSCPSEVI
KLDLHRAAER LSAHHGPAVR VYNFSGSGIE TTFTQGEDAC LASIVPTLPA TEARELLLVG
ALPDVVEDQA VSLLTQLGIG PVRCLPAHHA AEAPGVGPNT VFALVQPFLG DTHGALTRRG
ARHIAAPFPF GEEGTTLWLK AIADEFGVSA DTFEAVTAAP RARARKAVAA ASEGLRGKSV
FFLPDSQLEP SLARFLTREC GMSAVEVGTP FLHRGILGPD LDLIAEGPVL SEGQDVERQL
DRVRAARPDL TVCGLGLANP LEAEGFTTKW AIELVFTPVH FYEQAGDLAG LFSRPVRRRA
ILRREAAE
