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Database: UniProt
Entry: Q9S5F9_ECOLX
LinkDB: Q9S5F9_ECOLX
Original site: Q9S5F9_ECOLX 
ID   Q9S5F9_ECOLX            Unreviewed;       472 AA.
AC   Q9S5F9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=manC {ECO:0000313|EMBL:BAA77733.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:BAA77733.1};
RN   [1] {ECO:0000313|EMBL:BAA77733.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=184 {ECO:0000313|EMBL:BAA77733.1};
RX   PubMed=10222209; DOI=10.1006/mpat.1998.0253;
RA   Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
RT   "Analysis of the genes responsible for the O-antigen synthesis in
RT   enterohaemorrhagic Escherichia coli O157.";
RL   Microb. Pathog. 26:235-247(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC         alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58409; EC=2.7.7.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001083};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC       {ECO:0000256|ARBA:ARBA00006115, ECO:0000256|RuleBase:RU004190}.
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DR   EMBL; AB008676; BAA77733.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S5F9; -.
DR   UniPathway; UPA00126; UER00930.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd02213; cupin_PMI_typeII_C; 1.
DR   CDD; cd02509; GDP-M1P_Guanylyltransferase; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR049577; GMPP_N.
DR   InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR   InterPro; IPR001538; Man6P_isomerase-2_C.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR01479; GMP_PMI; 1.
DR   PANTHER; PTHR46390; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46390:SF1; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF01050; MannoseP_isomer; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:BAA77733.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAA77733.1}.
FT   DOMAIN          1..286
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          316..464
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   472 AA;  53273 MW;  41A9C1A8D722F8B7 CRC64;
     MAGGTGSRLW PLSRELYPKQ FLQLSGDNTL LQTTLLRLSG LSCQKPLVIT NEQHRFVVAE
     QLREINKLNG NIILEPCGRN TAPAIAISAF HALKRNPQED PLLLVLAADH VIAKESVFCD
     AIKNATPIAN QGKIVTFGII PEYAETGYGY IERGELSVPL QGHENTGFYY VNKFVEKPNR
     ETAELYMTSG NHYWNSGIFM FKASVYLEEL RKFRPDIYNV CEQVASSSYI DLDFIRLSKE
     QFQDCPAESI DFAVMEKTEK CVVCPVDIGW SDVGSWQSLW DISLKSKTGD VCKGDILTYD
     TKNNYIYSES ALVAAIGIED MVIVQTKDAV LVSKKSDVQH VKKIVEMLKL QQRTEYISHR
     EVFRPWGKFD SIDQGERYKV KKIIVKPGEG LSLRMHHHRS EHWIVLSGTA KVTLGDKTKL
     VTANESIYIP LGAAYSLENP GIIPLNLIEV SSGDYLGEDD IIRQKERYKH ED
//
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