BCHB_RHOCB
ID BCHB_RHOCB Reviewed; 525 AA.
AC P26163; D5ANS5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353, ECO:0000269|PubMed:18358835};
GN Name=bchB {ECO:0000255|HAMAP-Rule:MF_00353}; Synonyms=bchK;
GN OrderedLocusNames=RCAP_rcc00664;
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 PROTEIN SEQUENCE OF 1-6, AND 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RL Unpublished observations (JUL-2001).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 BCHN SUBUNIT;
RP SUBSTRATE AND 4FE-4S CLUSTER AND OF MUTANTS ALA-36 AND CYS-36, FUNCTION,
RP SUBUNIT, COFACTOR, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-36; CYS-95; ASP-274; MET-408 AND LEU-410.
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_00353,
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_00353,
CC ECO:0000269|PubMed:18358835};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00353,
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_00353,
CC ECO:0000269|PubMed:20400946};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
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_00353,
CC ECO:0000269|PubMed:20400946}.
CC -!- INTERACTION:
CC P26163; P26164: bchN; NbExp=3; IntAct=EBI-9017546, EBI-9017544;
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; Z11165; CAA77525.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84429.1; -; Genomic_DNA.
DR PIR; C49851; C49851.
DR RefSeq; WP_013066408.1; NC_014034.1.
DR PDB; 3AEK; X-ray; 2.30 A; B/D=1-525.
DR PDB; 3AEQ; X-ray; 2.90 A; B/D=1-525.
DR PDB; 3AER; X-ray; 2.80 A; B/D=1-525.
DR PDB; 3AES; X-ray; 2.50 A; B/D=1-525.
DR PDB; 3AET; X-ray; 2.91 A; B/D=1-525.
DR PDB; 3AEU; X-ray; 2.90 A; B/D=1-525.
DR PDBsum; 3AEK; -.
DR PDBsum; 3AEQ; -.
DR PDBsum; 3AER; -.
DR PDBsum; 3AES; -.
DR PDBsum; 3AET; -.
DR PDBsum; 3AEU; -.
DR AlphaFoldDB; P26163; -.
DR SMR; P26163; -.
DR DIP; DIP-59276N; -.
DR IntAct; P26163; 1.
DR STRING; 272942.RCAP_rcc00664; -.
DR EnsemblBacteria; ADE84429; ADE84429; RCAP_rcc00664.
DR GeneID; 31489610; -.
DR KEGG; rcp:RCAP_rcc00664; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_5; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR BioCyc; MetaCyc:MON-13270; -.
DR BRENDA; 1.3.1.33; 5381.
DR BRENDA; 1.3.7.7; 5381.
DR UniPathway; UPA00671; -.
DR EvolutionaryTrace; P26163; -.
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 Gene3D; 1.10.8.550; -; 1.
DR HAMAP; MF_00353; ChlB_BchB; 1.
DR InterPro; IPR013580; LI-POR_suB-like_C.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR042298; P-CP_red_C.
DR InterPro; IPR005969; Protochl_reductB.
DR InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR TIGRFAMs; TIGR01278; DPOR_BchB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..525
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219800"
FT REGION 433..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353,
FT ECO:0000269|PubMed:20400946"
FT BINDING 36
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 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 36
FT /note="D->A: Retains 13% activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 36
FT /note="D->C,S: Almost no enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 95
FT /note="C->A: Does not form heterotetramers."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 274
FT /note="D->A: Almost no enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 408
FT /note="M->A: Retains 85% activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT MUTAGEN 410
FT /note="L->A: Almost no enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20400946"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3AEK"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:3AEK"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3AEK"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 391..403
FT /evidence="ECO:0007829|PDB:3AEK"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:3AEK"
SQ SEQUENCE 525 AA; 57192 MW; 4322A6D9F535C3F5 CRC64;
MKLTLWTYEG PPHVGAMRVA TAMKDLQLVL HGPQGDTYAD LLFTMIERRN ARPPVSFSTF
EASHMGTDTA ILLKDALAAA HARYKPQAMA VALTCTAELL QDDPNGISRA LNLPVPVVPL
ELPSYSRKEN YGADETFRAL VRALAVPMER TPEVTCNLLG ATALGFRHRD DVAEVTKLLA
TMGIKVNVCA PLGASPDDLR KLGQAHFNVL MYPETGESAA RHLERACKQP FTKIVPIGVG
ATRDFLAEVS KITGLPVVTD ESTLRQPWWS ASVDSTYLTG KRVFIFGDGT HVIAAARIAA
KEVGFEVVGM GCYNREMARP LRTAAAEYGL EALITDDYLE VEKAIEAAAP ELILGTQMER
NIAKKLGLPC AVISAPVHVQ DFPARYAPQM GFEGANVLFD TWVHPLVMGL EEHLLTMFRE
DFEFHDAAGA SHHGGKAVAR EESPVAPADL APAATSDTPA APSPVVVTQA SGEIRWMPEA
ERELRKIPFF VRGKAKRNTE LYAAHKGVCD ITVETLYEAK AHYAR
