UMAA_MYCTU
ID UMAA_MYCTU Reviewed; 286 AA.
AC Q6MX39; I6Y3U9; L0T6S0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=S-adenosylmethionine-dependent methyltransferase UmaA {ECO:0000305};
DE Short=SAM-dependent methyltransferase UmaA {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN Name=umaA {ECO:0000303|PubMed:23435098, ECO:0000312|EMBL:CCP43202.1};
GN OrderedLocusNames=Rv0469 {ECO:0000312|EMBL:CCP43202.1};
GN ORFNames=LH57_02505 {ECO:0000312|EMBL:AIR13191.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION AS A METHYLTRANSFERASE, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=23435098; DOI=10.1515/hsz-2013-0126;
RA Meena L.S., Chopra P., Vishwakarma R.A., Singh Y.;
RT "Biochemical characterization of an S-adenosyl-l-methionine-dependent
RT methyltransferase (Rv0469) of Mycobacterium tuberculosis.";
RL Biol. Chem. 394:871-877(2013).
CC -!- FUNCTION: Methyltransferase that modifies short-chain fatty acids. In
CC vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-
CC methionine (SAM) to the double bond of phospholipid-linked oleic acid
CC to produce tuberculostearic acid (10-methylstearic-acid or TSA).
CC {ECO:0000269|PubMed:23435098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23435098}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43202.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR13191.1; -; Genomic_DNA.
DR RefSeq; WP_003900153.1; NZ_NVQJ01000002.1.
DR RefSeq; YP_177729.1; NC_000962.3.
DR PDB; 7L9U; X-ray; 1.55 A; A=1-286.
DR PDB; 7LXI; X-ray; 1.95 A; A=1-286.
DR PDB; 7MCJ; X-ray; 1.80 A; A/B=1-286.
DR PDBsum; 7L9U; -.
DR PDBsum; 7LXI; -.
DR PDBsum; 7MCJ; -.
DR AlphaFoldDB; Q6MX39; -.
DR SMR; Q6MX39; -.
DR STRING; 83332.Rv0469; -.
DR PaxDb; Q6MX39; -.
DR PRIDE; Q6MX39; -.
DR DNASU; 886286; -.
DR GeneID; 886286; -.
DR KEGG; mtu:Rv0469; -.
DR PATRIC; fig|83332.111.peg.513; -.
DR TubercuList; Rv0469; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_3_0_11; -.
DR OMA; FMRFIGQ; -.
DR PhylomeDB; Q6MX39; -.
DR PHI-base; PHI:3633; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR003333; Mycolic_cyclopropane_synthase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid metabolism; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..286
FT /note="S-adenosylmethionine-dependent methyltransferase
FT UmaA"
FT /id="PRO_0000434597"
FT ACT_SITE 268
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 32..33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 67..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 93..98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 122..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:7L9U"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:7L9U"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:7L9U"
FT HELIX 255..273
FT /evidence="ECO:0007829|PDB:7L9U"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:7L9U"
SQ SEQUENCE 286 AA; 33096 MW; C24CF30BE40CDC89 CRC64;
MTELRPFYEE SQSIYDVSDE FFSLFLDPTM AYTCAYFERE DMTLEEAQNA KFDLALDKLH
LEPGMTLLDI GCGWGGGLQR AIENYDVNVI GITLSRNQFE YSKAKLAKIP TERSVQVRLQ
GWDEFTDKVD RIVSIGAFEA FKMERYAAFF ERSYDILPDD GRMLLHTILT YTQKQMHEMG
VKVTMSDVRF MKFIGEEIFP GGQLPAQEDI FKFAQAADFS VEKVQLLQQH YARTLNIWAA
NLEANKDRAI ALQSEEIYNK YMHYLTGCEH FFRKGISNVG QFTLTK
