RMLA_MYCTU
ID RMLA_MYCTU Reviewed; 288 AA.
AC P9WH13; L0T524; P72017; Q797X3; Q7DA01;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE EC=2.7.7.24;
DE AltName: Full=dTDP-glucose pyrophosphorylase;
DE AltName: Full=dTDP-glucose synthase;
GN Name=rmlA; Synonyms=rfbA; OrderedLocusNames=Rv0334;
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 [GENOMIC DNA], FUNCTION AS A THYMIDYLYLTRANSFERASE, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9084178; DOI=10.1099/00221287-143-3-937;
RA Ma Y., Mills J.A., Belisle J.T., Vissa V., Howell M., Bowlin K.,
RA Scherman M.S., McNeil M.;
RT "Determination of the pathway for rhamnose biosynthesis in mycobacteria:
RT cloning, sequencing and expression of the Mycobacterium tuberculosis gene
RT encoding alpha-D-glucose-1-phosphate thymidylyltransferase.";
RL Microbiology 143:937-945(1997).
RN [2]
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 [3]
RP FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17784859; DOI=10.1111/j.1574-6968.2007.00890.x;
RA Qu H., Xin Y., Dong X., Ma Y.;
RT "An rmlA gene encoding d-glucose-1-phosphate thymidylyltransferase is
RT essential for mycobacterial growth.";
RL FEMS Microbiol. Lett. 275:237-243(2007).
RN [4]
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).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis. Involved in the
CC biosynthesis of the dTDP-L-rhamnose which is a component of the
CC critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which
CC connects the galactan region of arabinogalactan to peptidoglycan via a
CC phosphodiester linkage. {ECO:0000269|PubMed:17784859,
CC ECO:0000269|PubMed:9084178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:58601; EC=2.7.7.24;
CC Evidence={ECO:0000269|PubMed:9084178};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; U55242; AAB66657.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43064.1; -; Genomic_DNA.
DR PIR; G70527; G70527.
DR RefSeq; NP_214848.1; NC_000962.3.
DR RefSeq; WP_003401670.1; NZ_NVQJ01000026.1.
DR PDB; 6B5E; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-288.
DR PDB; 6B5K; X-ray; 1.60 A; A/B=1-288.
DR PDBsum; 6B5E; -.
DR PDBsum; 6B5K; -.
DR AlphaFoldDB; P9WH13; -.
DR SMR; P9WH13; -.
DR STRING; 83332.Rv0334; -.
DR PaxDb; P9WH13; -.
DR DNASU; 886568; -.
DR GeneID; 45424301; -.
DR GeneID; 886568; -.
DR KEGG; mtu:Rv0334; -.
DR TubercuList; Rv0334; -.
DR eggNOG; COG1209; Bacteria.
DR OMA; FTWLDTG; -.
DR PhylomeDB; P9WH13; -.
DR BRENDA; 2.7.7.24; 3445.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IMP:MTBBASE.
DR GO; GO:0046075; P:dTTP metabolic process; IDA:MTBBASE.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:MTBBASE.
DR CDD; cd02538; G1P_TT_short; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43532; PTHR43532; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01207; rmlA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="Glucose-1-phosphate thymidylyltransferase"
FT /id="PRO_0000395347"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6B5K"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6B5E"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6B5K"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:6B5K"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:6B5K"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:6B5K"
SQ SEQUENCE 288 AA; 31492 MW; 90873DE4C76E930C CRC64;
MRGIILAGGS GTRLYPITMG ISKQLLPVYD KPMIYYPLTT LMMAGIRDIQ LITTPHDAPG
FHRLLGDGAH LGVNISYATQ DQPDGLAQAF VIGANHIGAD SVALVLGDNI FYGPGLGTSL
KRFQSISGGA IFAYWVANPS AYGVVEFGAE GMALSLEEKP VTPKSNYAVP GLYFYDNDVI
EIARGLKKSA RGEYEITEVN QVYLNQGRLA VEVLARGTAW LDTGTFDSLL DAADFVRTLE
RRQGLKVSIP EEVAWRMGWI DDEQLVQRAR ALVKSGYGNY LLELLERN
