RMLA_SINFN
ID RMLA_SINFN Reviewed; 286 AA.
AC P55464;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable 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; OrderedLocusNames=NGR_a03560; ORFNames=y4gH;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; U00090; AAB91682.1; -; Genomic_DNA.
DR RefSeq; NP_443870.1; NC_000914.2.
DR RefSeq; WP_010875370.1; NC_000914.2.
DR AlphaFoldDB; P55464; -.
DR SMR; P55464; -.
DR STRING; 394.NGR_a03560; -.
DR PRIDE; P55464; -.
DR EnsemblBacteria; AAB91682; AAB91682; NGR_a03560.
DR KEGG; rhi:NGR_a03560; -.
DR PATRIC; fig|394.7.peg.364; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_5; -.
DR OMA; RRNWIDA; -.
DR OrthoDB; 1004719at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Probable glucose-1-phosphate thymidylyltransferase"
FT /id="PRO_0000208003"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 31205 MW; 2FD7BFF7575914F2 CRC64;
MKGIILAGGS GTRLHPMTLV MSKQILPVYD KPMIFYPLTT LMLAGIREIL IISTPHHMPL
FQALLGDGSQ WGISLRYAVQ PSPNGLAQAY VIGADFVAGS PSCLILGDNI YFGHGLQGLL
QQAAALQQGA TIFAYHVNDP ERYGVVEFDE GMNALSIEEK PAAPKSTWAV TGLYFYDSEV
VDIAANLKPS ARGEYEITDV NRIYLERGKL KVAVLGRGYA WLDTGTPDSL LEAAEFVRTL
EKRQAFKVAC PEEVALAMGF ISVEEFARIA ERAGKGDYGA YLRRLA