RFBF_BACSU
ID RFBF_BACSU Reviewed; 254 AA.
AC O06486; Q797B2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable glucose-1-phosphate cytidylyltransferase;
DE EC=2.7.7.33;
DE AltName: Full=CDP-glucose pyrophosphorylase;
GN Name=yfnH; OrderedLocusNames=BSU07270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9141694; DOI=10.1099/00221287-143-4-1317;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "A 23.4 kb segment at the 69 degrees-70 degrees region of the Bacillus
RT subtilis genome.";
RL Microbiology 143:1317-1320(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the transfer of a CMP moiety from CTP to glucose 1-
CC phosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + CTP + H(+) = CDP-D-glucose +
CC diphosphate; Xref=Rhea:RHEA:18213, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58660; EC=2.7.7.33;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate cytidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; D86418; BAA20117.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12546.1; -; Genomic_DNA.
DR PIR; C69815; C69815.
DR RefSeq; NP_388608.1; NC_000964.3.
DR RefSeq; WP_003244408.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O06486; -.
DR SMR; O06486; -.
DR STRING; 224308.BSU07270; -.
DR PaxDb; O06486; -.
DR PRIDE; O06486; -.
DR EnsemblBacteria; CAB12546; CAB12546; BSU_07270.
DR GeneID; 938779; -.
DR KEGG; bsu:BSU07270; -.
DR PATRIC; fig|224308.179.peg.789; -.
DR eggNOG; COG1208; Bacteria.
DR InParanoid; O06486; -.
DR OMA; YGAHHIK; -.
DR PhylomeDB; O06486; -.
DR BioCyc; BSUB:BSU07270-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047343; F:glucose-1-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd02524; G1P_cytidylyltransferase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR013446; G1P_cyt_trans.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..254
FT /note="Probable glucose-1-phosphate cytidylyltransferase"
FT /id="PRO_0000389445"
FT BINDING 6..10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 254 AA; 28671 MW; 4674B3D79CAEADED CRC64;
MKAVILCGGK GTRMSEVTND IPKPLAMIGG KPILWHIMKI YQYYGVNEFI LLLGYKGEKI
KEYFLDYEWK HNSLTLDSST GEVQMLGQPE TWKITFLETG VDTLTAGRIL QAKDYIGDET
FLLTYGDGLA NINLFHLISY HQTKGAAATV TGIDKVSQFG TLTVEDGMAK TFSEKTSSDG
IINGGFFVLS PKVFDYLPKD GNTMFEDEPL KNLAKDGELA VYRHYGFWTA IDTYKNLLEV
NKMWNQGQQV WKVW
