BCHU_CHLTE
ID BCHU_CHLTE Reviewed; 338 AA.
AC Q8KGE0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Bacteriochlorophyllide d C-20 methyltransferase {ECO:0000303|PubMed:15090495};
DE EC=2.1.1.333 {ECO:0000305|PubMed:15090495, ECO:0000305|PubMed:16797589};
DE AltName: Full=Bacteriochlorophyllide d MTase {ECO:0000303|PubMed:16797589};
GN Name=bchU {ECO:0000303|PubMed:15090495};
GN OrderedLocusNames=CT0028 {ECO:0000312|EMBL:AAM71276.1};
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;
RX PubMed=15090495; DOI=10.1128/jb.186.9.2558-2566.2004;
RA Maresca J.A., Gomez Maqueo Chew A., Ponsati M.R., Frigaard N.U.,
RA Ormerod J.G., Bryant D.A.;
RT "The bchU gene of Chlorobium tepidum encodes the c-20 methyltransferase in
RT bacteriochlorophyll c biosynthesis.";
RL J. Bacteriol. 186:2558-2566(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF HIS-150; TYR-246 AND HIS-290, ACTIVE SITE, REACTION
RP MECHANISM, AND SUBUNIT.
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=16797589; DOI=10.1016/j.jmb.2006.05.057;
RA Wada K., Yamaguchi H., Harada J., Niimi K., Osumi S., Saga Y., Oh-Oka H.,
RA Tamiaki H., Fukuyama K.;
RT "Crystal structures of BchU, a methyltransferase involved in
RT bacteriochlorophyll c biosynthesis, and its complex with S-
RT adenosylhomocysteine: implications for reaction mechanism.";
RL J. Mol. Biol. 360:839-849(2006).
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 (PubMed:15090495). Catalyzes the
CC methylation at the C-20 position of the cyclic tetrapyrrole chlorin of
CC bacteriochlorophyll d (BChld) to produce bacteriochlorophyll c (BChlc)
CC using S-adenosylmethionine (SAM) as a methyl source (PubMed:15090495,
CC PubMed:16797589). {ECO:0000269|PubMed:15090495,
CC ECO:0000269|PubMed:16797589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a bacteriochlorophyllide d + S-adenosyl-L-methionine = a
CC bacteriochlorophyllide c + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:49180, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90955, ChEBI:CHEBI:90965;
CC EC=2.1.1.333; Evidence={ECO:0000305|PubMed:15090495,
CC ECO:0000305|PubMed:16797589};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000305|PubMed:15090495}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16797589}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce only
CC bacteriochlorophyll d (BChld). {ECO:0000269|PubMed:15090495}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AE006470; AAM71276.1; -; Genomic_DNA.
DR RefSeq; NP_660934.1; NC_002932.3.
DR RefSeq; WP_010931722.1; NC_002932.3.
DR PDB; 1X19; X-ray; 2.27 A; A=1-338.
DR PDB; 1X1A; X-ray; 2.60 A; A=1-338.
DR PDB; 1X1B; X-ray; 2.60 A; A=1-338.
DR PDB; 1X1C; X-ray; 2.85 A; A=1-338.
DR PDB; 1X1D; X-ray; 2.70 A; A=1-338.
DR PDBsum; 1X19; -.
DR PDBsum; 1X1A; -.
DR PDBsum; 1X1B; -.
DR PDBsum; 1X1C; -.
DR PDBsum; 1X1D; -.
DR AlphaFoldDB; Q8KGE0; -.
DR SMR; Q8KGE0; -.
DR STRING; 194439.CT0028; -.
DR EnsemblBacteria; AAM71276; AAM71276; CT0028.
DR KEGG; cte:CT0028; -.
DR PATRIC; fig|194439.7.peg.27; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_005533_4_0_10; -.
DR OMA; VEFGCFK; -.
DR OrthoDB; 1213908at2; -.
DR BioCyc; MetaCyc:MON-19713; -.
DR BRENDA; 2.1.1.333; 1345.
DR UniPathway; UPA00671; -.
DR EvolutionaryTrace; Q8KGE0; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0036069; P:light-dependent bacteriochlorophyll biosynthetic process; IDA:UniProtKB.
DR GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR014088; C20_MeTrfase_CrtF.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02716; C20_methyl_CrtF; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..338
FT /note="Bacteriochlorophyllide d C-20 methyltransferase"
FT /id="PRO_0000444474"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16797589"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:16797589,
FT ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B,
FT ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16797589"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:16797589,
FT ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B,
FT ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:16797589,
FT ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B,
FT ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D"
FT BINDING 227..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:16797589,
FT ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B,
FT ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D"
FT BINDING 242..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:16797589,
FT ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B,
FT ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D"
FT BINDING 290
FT /ligand="a bacteriochlorophyll d"
FT /ligand_id="ChEBI:CHEBI:81553"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:16797589"
FT MUTAGEN 150
FT /note="H->A: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16797589"
FT MUTAGEN 246
FT /note="Y->F: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16797589"
FT MUTAGEN 290
FT /note="H->A: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16797589"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1X19"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1X19"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:1X19"
FT TURN 263..267
FT /evidence="ECO:0007829|PDB:1X1D"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1X1B"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1X19"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:1X19"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1X19"
SQ SEQUENCE 338 AA; 37935 MW; B7589CB49DCCD898 CRC64;
MSNNDLLNYY HRANELVFKG LIEFSCMKAA IELDLFSHMA EGPKDLATLA ADTGSVPPRL
EMLLETLRQM RVINLEDGKW SLTEFADYMF SPTPKEPNLH QTPVAKAMAF LADDFYMGLS
QAVRGQKNFK GQVPYPPVTR EDNLYFEEIH RSNAKFAIQL LLEEAKLDGV KKMIDVGGGI
GDISAAMLKH FPELDSTILN LPGAIDLVNE NAAEKGVADR MRGIAVDIYK ESYPEADAVL
FCRILYSANE QLSTIMCKKA FDAMRSGGRL LILDMVIDDP ENPNFDYLSH YILGAGMPFS
VLGFKEQARY KEILESLGYK DVTMVRKYDH LLVQAVKP
