ID F8KWL0_PARAV Unreviewed; 289 AA.
AC F8KWL0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:CCB85415.1};
GN OrderedLocusNames=PUV_04650 {ECO:0000313|EMBL:CCB85415.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB85415.1, ECO:0000313|Proteomes:UP000000495};
RN [1] {ECO:0000313|EMBL:CCB85415.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
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; FR872580; CCB85415.1; -; Genomic_DNA.
DR RefSeq; WP_013924372.1; NC_015702.1.
DR AlphaFoldDB; F8KWL0; -.
DR STRING; 765952.PUV_04650; -.
DR KEGG; puv:PUV_04650; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_0; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000000495; 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:CCB85415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:CCB85415.1}.
FT DOMAIN 3..239
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 289 AA; 32404 MW; 7C6CD017F52C5A9D CRC64;
MRKGIILAGG SGTRLYPLTA ALSKQLLPVY DKPMIYYPIS TLMLAGIREI LIISTPEDTP
RFQQLLGDGS QWGLDFHYAV QPHPGGLAQA FIIGKSFLQN QPCVLILGDN LFFGNELSQL
LKAAEEEKDG ATIFAYKVHN PQRYGVVEFD KDKRPKGIVE KPIVPKSRYA VTGLYFYDHQ
VCDIAADLKP SARGELEITD VNNYYLKQGT LHLEIFGRGI AWLDTGTFES LLEASVFIQT
IQHRQGVKIG CLEEIAYRMG YIPSIQLEKI AHAMRDSEYA SYLLELLDD
//
