BCHQ_CHLTE
ID BCHQ_CHLTE Reviewed; 451 AA.
AC Q8KBK9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Bacteriochlorophyllide d C-8(2)-methyltransferase {ECO:0000303|PubMed:17586634};
DE EC=2.1.1.332 {ECO:0000269|PubMed:17586634};
GN Name=bchQ {ECO:0000303|PubMed:17586634};
GN OrderedLocusNames=CT1777 {ECO:0000312|EMBL:AAM72998.1};
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, AND PATHWAY.
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. BchQ is a methyltransferase that
CC adds two consecutive methyl groups to the ethyl carbon at the C-8(2)
CC position of 8,12-diethyl-3-vinylbacteriochlorophyllide d to yield 12-
CC ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d.
CC {ECO:0000269|PubMed:17586634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8,12-diethyl-3-vinylbacteriochlorophyllide d + S-adenosyl-L-
CC methionine = 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49172, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90964,
CC ChEBI:CHEBI:90966; EC=2.1.1.332;
CC Evidence={ECO:0000269|PubMed:17586634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d + S-
CC adenosyl-L-methionine = 12-ethyl-8-isobutyl-3-
CC vinylbacteriochlorophyllide d + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:49176, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90966, ChEBI:CHEBI:90967;
CC EC=2.1.1.332; Evidence={ECO:0000269|PubMed:17586634};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00780};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|PROSITE-ProRule:PRU00780};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000305|PubMed:17586634}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00780}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce
CC bacteriochlorophyll c (BChlc) that is not methylated at C-8(2) and show
CC a growth rate that decreases to 60% of that of the wild-type at low
CC 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}.
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DR EMBL; AE006470; AAM72998.1; -; Genomic_DNA.
DR RefSeq; NP_662656.1; NC_002932.3.
DR AlphaFoldDB; Q8KBK9; -.
DR SMR; Q8KBK9; -.
DR STRING; 194439.CT1777; -.
DR DNASU; 1008134; -.
DR EnsemblBacteria; AAM72998; AAM72998; CT1777.
DR KEGG; cte:CT1777; -.
DR PATRIC; fig|194439.7.peg.1611; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_021572_5_1_10; -.
DR OMA; VIRWWRA; -.
DR OrthoDB; 973846at2; -.
DR BioCyc; MetaCyc:MON-19705; -.
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:0031419; F:cobalamin binding; IEA:InterPro.
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; IPR034498; Bacteriochlorophyll_C8_MT.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00307; bacteriochlorophyll_C8_methylt; 1.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 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..451
FT /note="Bacteriochlorophyllide d C-8(2)-methyltransferase"
FT /id="PRO_0000444473"
FT DOMAIN 1..118
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT DOMAIN 148..377
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 451 AA; 51737 MW; 2F00AF40A0FCC563 CRC64;
MDDDSNQKPL FHMALGVLTS LTPPQHHIEL VDEHFHDKIN YDGDYDMVGI TSRTIEATRA
YEIADEFRKR GKTVVLGGLH ISFNPEEAAA HADCIVVGEA DNLWTTLLDD VANNRLKERY
DSKDFPPVKA ITPLDYARIA KASKRTKVDG TKSIPIYVTR GCPFNCSFCV TPNFTGKQYR
VQDPKLLKHQ IEEAKKYFFK ANGKNSKPWF MLTDENLGIN KKKLWESLDL LKECDITFSV
FLSINFLEDP TTVKKLVDAG CNFVLAGLES IKQSTLEAYN KGHVNSAEKY SKIIEDCRKA
GLNIQGNFLF NPAIDTFEDI DELVQFVKKN HIFMPIFQII TPYPGTQMYH EYRESGLITI
EDWEKYNALH LVIKSDRYEP LLFQYKVLKS YVEVYTWKEI LLRTLYNPRK LINLVTSIAF
KKHLAAQLKA FERNHKMNPA MLSGVKPVMN G
