BCHN_RHOCB
ID BCHN_RHOCB Reviewed; 424 AA.
AC P26164; D5ANS6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 112.
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, ECO:0000269|PubMed:18358835};
GN Name=bchN {ECO:0000255|HAMAP-Rule:MF_00352};
GN OrderedLocusNames=RCAP_rcc00665;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8385667; DOI=10.1128/jb.175.8.2414-2422.1993;
RA Burke D.H., Alberti M., Hearst J.E.;
RT "bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and
RT identification of the third subunit of light-independent
RT protochlorophyllide reductase in bacteria and plants.";
RL J. Bacteriol. 175:2414-2422(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=SB1003 / CB1029;
RX PubMed=10811655; DOI=10.1074/jbc.m002904200;
RA Fujita Y., Bauer C.E.;
RT "Reconstitution of light-independent protochlorophyllide reductase from
RT purified bchL and bchN-bchB subunits. In vitro confirmation of nitrogenase-
RT like features of a bacteriochlorophyll biosynthesis enzyme.";
RL J. Biol. Chem. 275:23583-23588(2000).
RN [4]
RP CHARACTERIZATION.
RA Fujita Y.;
RL Unpublished observations (JUL-2001).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18358835; DOI=10.1016/j.febslet.2008.03.018;
RA Nomata J., Ogawa T., Kitashima M., Inoue K., Fujita Y.;
RT "NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is
RT the catalytic component containing oxygen-tolerant Fe-S clusters.";
RL FEBS Lett. 582:1346-1350(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BCHB SUBUNIT AND
RP 4FE-4S CLUSTER, FUNCTION, SUBUNIT, COFACTOR, REACTION MECHANISM, AND
RP MUTAGENESIS OF PHE-25; CYS-26; CYS-51 AND CYS-112.
RX PubMed=20400946; DOI=10.1038/nature08950;
RA Muraki N., Nomata J., Ebata K., Mizoguchi T., Shiba T., Tamiaki H.,
RA Kurisu G., Fujita Y.;
RT "X-ray crystal structure of the light-independent protochlorophyllide
RT reductase.";
RL Nature 465:110-114(2010).
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 ECO:0000269|PubMed:18358835, ECO:0000269|PubMed:20400946}.
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 ECO:0000269|PubMed:18358835};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00352,
CC ECO:0000269|PubMed:20400946};
CC Note=Binds 1 [4Fe-4S] cluster per heterodimer (PubMed:20400946). The
CC cluster is bound at the heterodimer interface by residues from both
CC subunits (PubMed:20400946). {ECO:0000255|HAMAP-Rule:MF_00352,
CC ECO:0000269|PubMed:20400946};
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 (PubMed:20400946). {ECO:0000255|HAMAP-Rule:MF_00352,
CC ECO:0000269|PubMed:20400946}.
CC -!- INTERACTION:
CC P26164; P26163: bchB; NbExp=3; IntAct=EBI-9017544, EBI-9017546;
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC Rule:MF_00352}.
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DR EMBL; Z11165; CAA77526.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84430.1; -; Genomic_DNA.
DR PIR; B49851; B49851.
DR RefSeq; WP_013066409.1; NC_014034.1.
DR PDB; 3AEK; X-ray; 2.30 A; A/C=2-424.
DR PDB; 3AEQ; X-ray; 2.90 A; A/C=2-424.
DR PDB; 3AER; X-ray; 2.80 A; A/C=2-424.
DR PDB; 3AES; X-ray; 2.50 A; A/C=2-424.
DR PDB; 3AET; X-ray; 2.91 A; A/C=2-424.
DR PDB; 3AEU; X-ray; 2.90 A; A/C=2-424.
DR PDBsum; 3AEK; -.
DR PDBsum; 3AEQ; -.
DR PDBsum; 3AER; -.
DR PDBsum; 3AES; -.
DR PDBsum; 3AET; -.
DR PDBsum; 3AEU; -.
DR AlphaFoldDB; P26164; -.
DR SMR; P26164; -.
DR DIP; DIP-59277N; -.
DR IntAct; P26164; 1.
DR STRING; 272942.RCAP_rcc00665; -.
DR EnsemblBacteria; ADE84430; ADE84430; RCAP_rcc00665.
DR GeneID; 31489611; -.
DR KEGG; rcp:RCAP_rcc00665; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_037170_0_0_5; -.
DR OMA; ISCVAWL; -.
DR OrthoDB; 363662at2; -.
DR BioCyc; MetaCyc:MON-13269; -.
DR BRENDA; 1.3.7.7; 5381.
DR UniPathway; UPA00671; -.
DR EvolutionaryTrace; P26164; -.
DR Proteomes; UP000002361; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome.
FT CHAIN 1..424
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208596"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000269|PubMed:20400946"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000269|PubMed:20400946"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 25
FT /note="F->A: Retains 50% activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 26
FT /note="C->A: Does not form heterotetramers."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 51
FT /note="C->A: Does not form heterotetramers."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 112
FT /note="C->A: Does not form heterotetramers."
FT /evidence="ECO:0000269|PubMed:20400946"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3AEQ"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:3AEK"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3AEK"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3AER"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:3AEK"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:3AEK"
SQ SEQUENCE 424 AA; 45830 MW; C90C75233802834D CRC64;
MSLDSPTFGC TDSPVRRERG QKAVFCGLTS IVWLHRKMQD AFFLVVGSRT CAHLLQAAAG
VMIFAEPRFG TAVLEEQDLA GLADAHKELD REVAKLLERR PDIRQLFLVG SCPSEVLKLD
LDRAAERLSG LHAPHVRVYS YTGSGLDTTF TQGEDTCLAA MVPTLDTTEA AELIVVGALP
DVVEDQCLSL LTQLGVGPVR MLPARRSDIE PAVGPNTRFI LAQPFLGETT GALERRGAKR
IAAPFPFGEE GTTLWLKAVA DAYGVSAEKF EAVTAAPRAR AKKAIAAHLE TLTGKSLFMF
PDSQLEIPLA RFLARECGMK TTEIATPFLH KAIMAPDLAL LPSNTALTEG QDLEAQLDRH
EAINPDLTVC GLGLANPLEA KGHATKWAIE LVFTPVHFYE QAGDLAGLFS RPLRRRALLN
GGAA
