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Database: UniProt
Entry: V2UNJ0_9GAMM
LinkDB: V2UNJ0_9GAMM
Original site: V2UNJ0_9GAMM 
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
//
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