ID B5IJF4_9CYAN Unreviewed; 311 AA.
AC B5IJF4;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=rfbA {ECO:0000313|EMBL:EDY39326.1};
GN ORFNames=CPCC7001_2206 {ECO:0000313|EMBL:EDY39326.1};
OS Cyanobium sp. PCC 7001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY39326.1, ECO:0000313|Proteomes:UP000003950};
RN [1] {ECO:0000313|EMBL:EDY39326.1, ECO:0000313|Proteomes:UP000003950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY39326.1,
RC ECO:0000313|Proteomes:UP000003950};
RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS990556; EDY39326.1; -; Genomic_DNA.
DR RefSeq; WP_006911244.1; NZ_DS990556.1.
DR AlphaFoldDB; B5IJF4; -.
DR STRING; 180281.CPCC7001_2206; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_3; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000003950; 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:EDY39326.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003950};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EDY39326.1}.
FT DOMAIN 21..255
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 311 AA; 33953 MW; FB79A10465E184BF CRC64;
MATRPWEHPP SDPDALTPQR KGIILAGGSG TRLHPITVGV SKQLLPVFDK PMIYYPLSTL
MLAGIREVLI ITTPTDQEAF QRLLGDGSRW GMTIAYAVQP SPDGLAQAFL IGERFLAGAP
AALVLGDNLF HGHDLIPQLQ GCNGQAAGAT VFAYPVRDPE RYGVVAFDGD GRVLSIEEKP
AQPRSRYAVT GLYFYDDSVV ERARRVVPSA RGELEITDLN RQYLEEGLLK VELMGRGMAW
LDTGTCDSLH EAGSYIRTLE HRQGLKVGCP EEVAWRMGWI DADQLAALAA PLRKSGYGEY
LLQVLETGHA G
//
