GenomeNet

Database: UniProt
Entry: Q9HU22
LinkDB: Q9HU22
Original site: Q9HU22 
ID   Q9HU22_PSEAE            Unreviewed;       293 AA.
AC   Q9HU22; Q7AYQ9;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   02-JUN-2021, entry version 136.
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=rmlA {ECO:0000313|EMBL:AAG08548.1};
GN   OrderedLocusNames=PA5163 {ECO:0000313|EMBL:AAG08548.1};
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG08548.1, ECO:0000313|Proteomes:UP000002438};
RN   [1] {ECO:0007829|PDB:1FXO, ECO:0007829|PDB:1FZW}
RP   X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH GLUCOSE-1-PHOSPHATE
RP   AND TTP.
RX   PubMed=11118200; DOI=10.1093/emboj/19.24.6652;
RA   Blankenfeldt W., Asuncion M., Lam J.S., Naismith J.H.;
RT   "The structural basis of the catalytic mechanism and regulation of glucose-
RT   1-phosphate thymidylyltransferase (RmlA).";
RL   EMBO J. 19:6652-6663(2000).
RN   [2] {ECO:0000313|EMBL:AAG08548.1, ECO:0000313|Proteomes:UP000002438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA   Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA   Hancock R.E., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3] {ECO:0007829|PDB:3ZLK, ECO:0007829|PDB:3ZLL}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RX   PubMed=23138692; DOI=10.1021/CB300426U;
RA   Alphey M.S., Pirrie L., Torrie L.S., Boulkeroua W.A., Gardiner M.,
RA   Sarkar A., Maringer M., Oehlmann W., Brenk R., Scherman M.S., McNeil M.,
RA   Rejzek M., Field R.A., Singh M., Gray D., Westwood N.J., Naismith J.H.;
RT   "Allosteric competitive inhibitors of the glucose-1-phosphate
RT   thymidylyltransferase (RmlA) from Pseudomonas aeruginosa.";
RL   ACS Chem. Biol. 8:387-396(2013).
RN   [4] {ECO:0007829|PDB:6T37, ECO:0007829|PDB:6T38}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RA   Xiao G., Alphey M.S., Tran F., Westwood N.J., Naismith J.H.;
RT   "Potent Allosteric Inhibitors of Pseudomonas aeruginosa Glucose-1-phosphate
RT   Thymidylyltransferase (RmlA).";
RL   Submitted (OCT-2019) to the PDB data bank.
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; AE004091; AAG08548.1; -; Genomic_DNA.
DR   PIR; D83000; D83000.
DR   RefSeq; NP_253850.1; NC_002516.2.
DR   RefSeq; WP_003105518.1; NZ_QZGE01000002.1.
DR   PDB; 1FXO; X-ray; 1.66 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1FZW; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1G0R; X-ray; 1.87 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1G1L; X-ray; 1.77 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1G23; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1G2V; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-293.
DR   PDB; 1G3L; X-ray; 2.70 A; A/B/C/D=1-293.
DR   PDB; 3ZLK; X-ray; 1.95 A; A/B/C/D=1-293.
DR   PDB; 3ZLL; X-ray; 2.00 A; A/B/C/D=1-293.
DR   PDB; 4ARW; X-ray; 2.20 A; A/B/C/D=1-293.
DR   PDB; 4ASJ; X-ray; 2.25 A; A/B/C/D=1-293.
DR   PDB; 4ASY; X-ray; 2.30 A; A/B/C/D=1-293.
DR   PDB; 4B2W; X-ray; 2.36 A; A/B/C/D=1-293.
DR   PDB; 4B2X; X-ray; 1.70 A; A/B/C/D=1-293.
DR   PDB; 4B3U; X-ray; 1.80 A; A/B/C/D=1-293.
DR   PDB; 4B42; X-ray; 2.50 A; A/B/C/D=1-293.
DR   PDB; 4B4B; X-ray; 2.10 A; A/B/C/D=1-293.
DR   PDB; 4B4G; X-ray; 2.50 A; A/B/C/D=1-293.
DR   PDB; 4B4M; X-ray; 2.35 A; A/B/C/D=1-293.
DR   PDB; 4B5B; X-ray; 2.06 A; A/B/C/D=1-293.
DR   PDB; 5FTS; X-ray; 2.20 A; A/B/C/D=1-293.
DR   PDB; 5FTV; X-ray; 2.21 A; A/B/C/D=1-293.
DR   PDB; 5FU0; X-ray; 1.90 A; A/B/C/D=1-293.
DR   PDB; 5FU8; X-ray; 2.20 A; A/B/C/D=1-293.
DR   PDB; 5FUH; X-ray; 1.60 A; A/B/C/D=1-293.
DR   PDB; 5FYE; X-ray; 2.40 A; A/B/C/D=1-293.
DR   PDB; 6T37; X-ray; 2.08 A; A/B/C/D=1-293.
DR   PDB; 6T38; X-ray; 2.15 A; A/B/C/D=1-293.
DR   PDB; 6TQG; X-ray; 2.45 A; A/B/C/D=1-293.
DR   PDBsum; 1FXO; -.
DR   PDBsum; 1FZW; -.
DR   PDBsum; 1G0R; -.
DR   PDBsum; 1G1L; -.
DR   PDBsum; 1G23; -.
DR   PDBsum; 1G2V; -.
DR   PDBsum; 1G3L; -.
DR   PDBsum; 3ZLK; -.
DR   PDBsum; 3ZLL; -.
DR   PDBsum; 4ARW; -.
DR   PDBsum; 4ASJ; -.
DR   PDBsum; 4ASY; -.
DR   PDBsum; 4B2W; -.
DR   PDBsum; 4B2X; -.
DR   PDBsum; 4B3U; -.
DR   PDBsum; 4B42; -.
DR   PDBsum; 4B4B; -.
DR   PDBsum; 4B4G; -.
DR   PDBsum; 4B4M; -.
DR   PDBsum; 4B5B; -.
DR   PDBsum; 5FTS; -.
DR   PDBsum; 5FTV; -.
DR   PDBsum; 5FU0; -.
DR   PDBsum; 5FU8; -.
DR   PDBsum; 5FUH; -.
DR   PDBsum; 5FYE; -.
DR   SMR; Q9HU22; -.
DR   BindingDB; Q9HU22; -.
DR   DrugBank; DB03723; 2'-Deoxy-Thymidine-Beta-L-Rhamnose.
DR   DrugBank; DB03751; 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose.
DR   DrugBank; DB02843; alpha-D-glucose-1-phosphate.
DR   DrugBank; DB04272; Citric acid.
DR   DrugBank; DB04485; Thymidine.
DR   DrugBank; DB02452; Thymidine 5'-triphosphate.
DR   DrugBank; DB01643; Thymidine monophosphate.
DR   PaxDb; Q9HU22; -.
DR   PRIDE; Q9HU22; -.
DR   EnsemblBacteria; AAG08548; AAG08548; PA5163.
DR   GeneID; 879990; -.
DR   KEGG; pae:PA5163; -.
DR   PATRIC; fig|208964.12.peg.5411; -.
DR   PseudoCAP; PA5163; -.
DR   HOGENOM; CLU_029499_9_0_6; -.
DR   InParanoid; Q9HU22; -.
DR   OMA; GPYPMIY; -.
DR   PhylomeDB; Q9HU22; -.
DR   BRENDA; 2.7.7.24; 5087.
DR   EvolutionaryTrace; Q9HU22; -.
DR   PHI-base; PHI:7634; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; ISS:PseudoCAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; ISS:PseudoCAP.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; ISS:PseudoCAP.
DR   CDD; cd02538; G1P_TT_short; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; PTHR43532; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1FXO, ECO:0007829|PDB:1FZW};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotide-binding {ECO:0007829|PDB:1G2V};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:AAG08548.1}.
FT   DOMAIN          4..240
FT                   /note="NTP_transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   NP_BIND         10..15
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   NP_BIND         25..26
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   NP_BIND         82..87
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   NP_BIND         114..119
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   NP_BIND         219..220
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   REGION          161..162
FT                   /note="Glucose-1-phosphate binding"
FT                   /evidence="ECO:0007829|PDB:1G0R, ECO:0007829|PDB:1G23"
FT   BINDING         110
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   BINDING         111
FT                   /note="Glucose-1-phosphate"
FT                   /evidence="ECO:0007829|PDB:1G0R, ECO:0007829|PDB:1G23"
FT   BINDING         146
FT                   /note="Glucose-1-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0007829|PDB:1G0R, ECO:0007829|PDB:1G23"
FT   BINDING         172
FT                   /note="Glucose-1-phosphate; via carbonyl oxygen"
FT                   /evidence="ECO:0007829|PDB:1G0R, ECO:0007829|PDB:1G23"
FT   BINDING         251
FT                   /note="TTP; via amide nitrogen"
FT                   /evidence="ECO:0007829|PDB:1G2V"
FT   BINDING         255
FT                   /note="TTP"
FT                   /evidence="ECO:0007829|PDB:1G2V"
SQ   SEQUENCE   293 AA;  32457 MW;  1E249F4359DC0553 CRC64;
     MKRKGIILAG GSGTRLHPAT LAISKQLLPV YDKPMIYYPL STLMLAGIRE ILIISTPQDT
     PRFQQLLGDG SNWGLDLQYA VQPSPDGLAQ AFLIGESFIG NDLSALVLGD NLYYGHDFHE
     LLGSASQRQT GASVFAYHVL DPERYGVVEF DQGGKAISLE EKPLEPKSNY AVTGLYFYDQ
     QVVDIARDLK PSPRGELEIT DVNRAYLERG QLSVEIMGRG YAWLDTGTHD SLLEAGQFIA
     TLENRQGLKV ACPEEIAYRQ KWIDAAQLEK LAAPLAKNGY GQYLKRLLTE TVY
//
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