BCHR_CHLTE
ID BCHR_CHLTE Reviewed; 456 AA.
AC Q8KCU0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Bacteriochlorophyllide d C-12(1)-methyltransferase {ECO:0000303|PubMed:17586634};
DE EC=2.1.1.331 {ECO:0000269|PubMed:17586634};
GN Name=bchR {ECO:0000303|PubMed:17586634};
GN OrderedLocusNames=CT1320 {ECO:0000312|EMBL:AAM72550.2};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000312|Proteomes:UP000001007};
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, PATHWAY, AND COFACTOR.
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000312|Proteomes:UP000001007};
RX PubMed=17586634; DOI=10.1128/jb.00519-07;
RA Gomez Maqueo Chew A., Frigaard N.U., Bryant D.A.;
RT "Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are
RT essential for adaptation to low light in Chlorobaculum tepidum.";
RL J. Bacteriol. 189:6176-6184(2007).
CC -!- FUNCTION: Involved in the biosynthesis of the major light-harvesting
CC pigment bacteriochlorophyll c (BChlc), which confers a significant
CC competitive advantage to green sulfur bacteria living at limiting red
CC and near-infrared light intensities. BchR is a methyltransferase that
CC adds a single methyl group to the methyl carbon at the C-12(1) position
CC of 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d to yield 8,12-
CC diethyl-3-vinylbacteriochlorophyllide d. {ECO:0000269|PubMed:17586634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d + S-
CC adenosyl-L-methionine = 8,12-diethyl-3-vinylbacteriochlorophyllide d
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49168,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90963, ChEBI:CHEBI:90964; EC=2.1.1.331;
CC Evidence={ECO:0000269|PubMed:17586634};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000305};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000305|PubMed:17586634}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce
CC bacteriochlorophyll c (BChlc) that is not methylated at C-12(1) and
CC show a growth rate that decreases to 53% of that of the wild-type at
CC low light intensity. Double mutants lacking both bchR and bchQ produce
CC bacteriochlorophyll c (BChlc) that is not methylated at C-8(2) and C-
CC 12(1), and show a growth rate that decreases to 41% of that of the
CC wild-type at low light intensity. {ECO:0000269|PubMed:17586634}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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; AE006470; AAM72550.2; -; Genomic_DNA.
DR RefSeq; NP_662208.1; NC_002932.3.
DR AlphaFoldDB; Q8KCU0; -.
DR SMR; Q8KCU0; -.
DR STRING; 194439.CT1320; -.
DR EnsemblBacteria; AAM72550; AAM72550; CT1320.
DR KEGG; cte:CT1320; -.
DR PATRIC; fig|194439.7.peg.1202; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_021572_5_1_10; -.
DR OMA; PQPMLGI; -.
DR OrthoDB; 973846at2; -.
DR BioCyc; MetaCyc:MON-19704; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR034497; Bacteriochlorophyll_C12_MT.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00414; bacteriochlorophyll_C12_methyl; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..456
FT /note="Bacteriochlorophyllide d C-12(1)-methyltransferase"
FT /id="PRO_0000444472"
FT DOMAIN 178..405
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 52245 MW; 7B6450092D7D43BE CRC64;
MSLTNGVAPS LEKLAAEQKS RKKWLLVQPK SQTSMMVDSG AVSMPLNLIM VATLASKYFD
VTFLDERTGD TIPQDFSGYD VVAITSRTLN AKNAYRIGDR AKAQGKIVLI GGVHPTMLTD
EASLHCTSVI YGEIESVWEE LAIDIFRGKM KSVYKASNLK PMTTMTPPDF SFALNSPHAK
KYSQLIPILA TKGCPVGCSF CTTPTVYGKS FRYREIDLVL DEMRAHQERL GKKKVRFSFM
DDNISFRPKY FMELLEGMAK LGVRWNANIS MNFLQKPEVA ELAGRSGCEL MSIGFESLNP
DILKSMNKGS NRLQNYEAVV SNLHKHKIAI QGYFIFGFDD DSEKSFQATY DFIMQNRIEF
PVFSLLTPFP GTPYFEEMKD RVRHFDWDKY DTYHYMFEPK KLGGEKLLEN FIKLQREVYK
GSAIMKRMQG KPLNWVWFVN FLMNRFTRKL TPEMYL
