ID H1KSR1_METEX Unreviewed; 296 AA.
AC H1KSR1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=MetexDRAFT_5674 {ECO:0000313|EMBL:EHP86957.1};
OS Methylorubrum extorquens DSM 13060.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP86957.1, ECO:0000313|Proteomes:UP000004382};
RN [1] {ECO:0000313|EMBL:EHP86957.1, ECO:0000313|Proteomes:UP000004382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP86957.1,
RC ECO:0000313|Proteomes:UP000004382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., Pirttila A.,
RA Frank C., Woyke T.J.;
RT "The draft genome of Methylobacterium extorquens DSM 13060.";
RL Submitted (SEP-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP86957.1}.
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DR EMBL; AGJK01000286; EHP86957.1; -; Genomic_DNA.
DR RefSeq; WP_003605848.1; NZ_AGJK01000286.1.
DR AlphaFoldDB; H1KSR1; -.
DR GeneID; 72990078; -.
DR PATRIC; fig|882800.3.peg.5507; -.
DR Proteomes; UP000004382; Unassembled WGS sequence.
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:EHP86957.1};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EHP86957.1}.
FT DOMAIN 2..237
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 296 AA; 32831 MW; 0A4A1B3F4E2D2D02 CRC64;
MKGIVLAGGS GTRLHPATLA INKQLLPVYD KPMIYYPISV LMLAGIREIL VISSPEHLGN
YQRLLGTGEQ FGVTFTYAVQ PRPEGLAQAF IIGRDFVGSD DVALVLGDNL FFGNGMSDLL
AKARTRKSGA TVFAYHVDHP EAYGVVTLDE SGRPLRLVEK PQTPESPWAV TGLYFYDNQV
LDIAAEVKPS DRGELEITSV NQAYLERGQL HVERMSRGYA WLDTGTHDSL LEAGEFVRVL
QRRQGLQVAC LEEIAYLQGF IGREQLQARG ELFAKTSYGQ NLLRLAREGR RADQDF
//
