ID V2UNJ0_9GAMM Unreviewed; 161 AA.
AC V2UNJ0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461};
DE Flags: Fragment;
GN ORFNames=P255_02195 {ECO:0000313|EMBL:ESK50220.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK50220.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK50220.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK50220.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005125}.
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004781}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000256|ARBA:ARBA00010480}.
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:ESK50220.1}.
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DR EMBL; AYEU01000007; ESK50220.1; -; Genomic_DNA.
DR AlphaFoldDB; V2UNJ0; -.
DR HOGENOM; CLU_029499_9_1_6; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000018418; Unassembled WGS sequence.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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 Reference proteome {ECO:0000313|Proteomes:UP000018418};
KW Transferase {ECO:0000313|EMBL:ESK50220.1}.
FT DOMAIN 7..160
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT NON_TER 161
FT /evidence="ECO:0000313|EMBL:ESK50220.1"
SQ SEQUENCE 161 AA; 17523 MW; 5BC259BAD5EFD7AB CRC64;
MSQIKRKGII LAGGSGTRLY PITMGTSKQL LPIYDKPMIY YPLSVLMLAG ISEILIISTP
EDLPNFEKLL GTGEELGIKL SYKVQPSPDG LAQAFILGEE FIGQDNVCLI LGDNIFYGQS
FSQQLKRASA QTSGATVFGY YVNDPERFGV VEFDSTGKAI S
//