ID A0A1X1YBH8_9MYCO Unreviewed; 288 AA.
AC A0A1X1YBH8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00017654, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN Name=rmlA {ECO:0000313|EMBL:BBX98558.1};
GN ORFNames=AWC15_18690 {ECO:0000313|EMBL:ORW08415.1}, MLAC_38520
GN {ECO:0000313|EMBL:BBX98558.1};
OS Mycobacterium lacus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=169765 {ECO:0000313|EMBL:BBX98558.1, ECO:0000313|Proteomes:UP000466396};
RN [1] {ECO:0000313|EMBL:ORW08415.1, ECO:0000313|Proteomes:UP000193202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44577 {ECO:0000313|EMBL:ORW08415.1,
RC ECO:0000313|Proteomes:UP000193202};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBX98558.1, ECO:0000313|Proteomes:UP000466396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98558.1,
RC ECO:0000313|Proteomes:UP000466396};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBX98558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98558.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000256|RuleBase:RU003706}.
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:0000256|ARBA:ARBA00001095,
CC ECO:0000256|RuleBase:RU003706};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000256|ARBA:ARBA00010480, ECO:0000256|RuleBase:RU003706}.
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DR EMBL; AP022581; BBX98558.1; -; Genomic_DNA.
DR EMBL; LQPF01000060; ORW08415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1YBH8; -.
DR STRING; 169765.AWC15_18690; -.
DR KEGG; mlj:MLAC_38520; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000193202; Unassembled WGS sequence.
DR Proteomes; UP000466396; Chromosome.
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 InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01207; rmlA; 1.
DR PANTHER; PTHR43532; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43532:SF1; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 1; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU003706};
KW Metal-binding {ECO:0000256|RuleBase:RU003706};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706};
KW Reference proteome {ECO:0000313|Proteomes:UP000466396};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:BBX98558.1}.
FT DOMAIN 3..237
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 288 AA; 31357 MW; 4578D8B9947B98DD CRC64;
MRGIILAGGS GTRLHPITIG ISKQLLPVYD KPMVYYPLST LMMAGIRDIL VITTPHDAAG
FQRLLGDGTQ FGIDISYVTQ DSPDGLAQAF VLGANHIGTD SVALVLGDNI FYGPGLGTSL
SRFQTVSGGA IFAYWVANPS AYGVVEFGPD GMALSLEEKP ETPKSHYAVP GLYFYDNDVI
EIAKGLKKSA RGEYEITEVN QIYLNRGRLA VEVMARGTAW LDTGTFDSLL DASDFVRTLE
LRQGLKVSVP EEVAWRRGWI DDEQLAQRAR GLVKSGYGGY LLELLERS
//
