ID C1D5F6_LARHH Unreviewed; 289 AA.
AC C1D5F6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN Name=rfbA {ECO:0000313|EMBL:ACO75973.1};
GN OrderedLocusNames=LHK_02995 {ECO:0000313|EMBL:ACO75973.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75973.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO75973.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75973.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO75973.1; -; Genomic_DNA.
DR AlphaFoldDB; C1D5F6; -.
DR STRING; 557598.LHK_02995; -.
DR KEGG; lhk:LHK_02995; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_4; -.
DR Proteomes; UP000002010; 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 ECO:0000313|EMBL:ACO75973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003706}.
FT DOMAIN 4..240
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 289 AA; 31721 MW; 769EA4857D8F0548 CRC64;
MQRKGIILAG GSGTRLYPAT LAVSKQLLPI YDKPMIYYPL STLMLAQIRD VLIISTPQDT
PRFQSLLGDG SQWGMNLQYA VQPSPDGLAQ AFLIGADFLA GAPSALVLGD NIFYGHDFVR
LLTDAGRQHD GATVFAYHVQ DPERYGVVEF DAAGKALSIE EKPVRPKSGY AVTGLYFYDS
RVVDIAREVR PSPRGELEIT DVNNAYLRQG LLDVQTMGRG YAWLDTGTHE SMLEASQFIA
TVEKRQGLKV ACPEEIAYQA GWIDAEQVAA LAAPMQKNAY GQYLLRLLA
//
