ID D1Z268_METPS Unreviewed; 357 AA.
AC D1Z268;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000313|EMBL:BAI62790.1};
GN Name=rfbA {ECO:0000313|EMBL:BAI62790.1};
GN OrderedLocusNames=MCP_2718 {ECO:0000313|EMBL:BAI62790.1};
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI62790.1, ECO:0000313|Proteomes:UP000001882};
RN [1] {ECO:0000313|Proteomes:UP000001882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC {ECO:0000313|Proteomes:UP000001882};
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT paludicola, the first cultivated representative of the order
RT Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001851};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC Evidence={ECO:0000256|ARBA:ARBA00000731};
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
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DR EMBL; AP011532; BAI62790.1; -; Genomic_DNA.
DR AlphaFoldDB; D1Z268; -.
DR STRING; 304371.MCP_2718; -.
DR KEGG; mpd:MCP_2718; -.
DR PATRIC; fig|304371.9.peg.2783; -.
DR eggNOG; arCOG00667; Archaea.
DR InParanoid; D1Z268; -.
DR OMA; FTWLDTG; -.
DR OrthoDB; 15372at2157; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000001882; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04189; G1P_TT_long; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR InterPro; IPR005908; G1P_thy_trans_l.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR03992; Arch_glmU; 1.
DR NCBIfam; TIGR01208; rmlA_long; 1.
DR PANTHER; PTHR42883; GLUCOSE-1-PHOSPHATE THYMIDYLTRANSFERASE; 1.
DR PANTHER; PTHR42883:SF2; ZGC:136439; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:BAI62790.1}.
FT DOMAIN 2..237
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 357 AA; 38412 MW; 7AC615AF6F136C10 CRC64;
MKGLVLSGGS GTRLRPLTHT GPKQLIPVAN KPVLQYVIED LRDAGITDIG VILGNNGKEQ
VIAELKDGKQ YGVNITYVEQ GAPLGIAHAV QCARDFMGDD DFIVYLGDNM LKDGVKGLVD
DFAEGQYDAA ISLQAVANPR QFGVAELDKQ GRVVGLEEKP KVPKSNYALV GVYLFTPVIF
DMIRQIKPSW RNELEITDAI QKLLDNKYKV RSHIVSGWWK DTGKPEDILD VNRLVLDELK
PLVEGMVEEG ASVAGRVSLG KNSVIRSGCV IRGPVVIGKD CTIEAGAYIG PYTAVGDGCT
VKGAYVESSV LMAGCSVSCE NRIVDSLIGK NAIIASANND LPKGTRLIVG ENSFLKI
//