ID   MANC9_ECOLX             Reviewed;         471 AA.
AC   P37753; P82273;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Mannose-1-phosphate guanylyltransferase;
DE            EC=2.7.7.13;
DE   AltName: Full=GDP-mannose pyrophosphorylase;
DE            Short=GMP;
DE            Short=GMPP;
GN   Name=manC; Synonyms=rfbM, rfbM1;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O9:K30:H12 / E69;
RX   PubMed=7515042; DOI=10.1128/jb.176.11.3126-3139.1994;
RA   Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N.,
RA   Whitfield C.;
RT   "Cloning and analysis of duplicated rfbM and rfbK genes involved in the
RT   formation of GDP-mannose in Escherichia coli O9:K30 and participation of
RT   rfb genes in the synthesis of the group I K30 capsular polysaccharide.";
RL   J. Bacteriol. 176:3126-3139(1994).
RN   [2]
RP   GENE NAME.
RX   PubMed=9004408; DOI=10.1016/s0966-842x(97)82912-5;
RA   Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D.,
RA   Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.;
RT   "Bacterial polysaccharide synthesis and gene nomenclature.";
RL   Trends Microbiol. 4:495-503(1996).
CC   -!- FUNCTION: Involved in GDP-mannose biosynthesis which serves as the
CC       activated sugar nucleotide precursor for mannose residues in cell
CC       surface polysaccharides. This enzyme participates in synthesis of the
CC       LPS O9 antigen.
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   -!- 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.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- MISCELLANEOUS: There are two duplicated genes for manB and manC in this
CC       E.coli strain.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; L27632; AAA21139.1; -; Genomic_DNA.
DR   EMBL; L27646; AAA21137.1; -; Genomic_DNA.
DR   PIR; I41251; I41251.
DR   PIR; I84556; I84556.
DR   AlphaFoldDB; P37753; -.
DR   SMR; P37753; -.
DR   STRING; 585034.ECIAI1_2104; -.
DR   UniPathway; UPA00126; UER00930.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
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   Pfam; PF01050; MannoseP_isomer; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01479; GMP_PMI; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Lipopolysaccharide biosynthesis; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..471
FT                   /note="Mannose-1-phosphate guanylyltransferase"
FT                   /id="PRO_0000194259"
FT   VARIANT         161
FT                   /note="V -> L"
SQ   SEQUENCE   471 AA;  52628 MW;  F3A8394550384F79 CRC64;
     MLLPVIMAGG TGSRLWPMSR ELYPKQFLRL FGQNSMLQET ITRLSGLEVH EPMVICNEEH
     RFLVAEQLRQ LNKLSSNIIL EPVGRNTAPA IALAALQATR HGDDPLMLVL AADHIINNQP
     VFHDAIRVAE QYADEGHLVT FGIVPNAPET GYGYIQRGVA VTDSAHTPYQ VARFVEKPDR
     ERAGAYLASG EYYWNSGMFM FRAKKYLSEL AKFRPDILEA CQAAVNAADN GSDFISIPHD
     IFCECPDESV DYAVMEKTAD AVVVGLDADW SDVGSWSALW EVSPKDGQGN VLSGDAWVHN
     SENCYINSDE KLVAAIGVEN LVIVSTKDAV LVMNRERSQD VKKAVEFLKQ NQRTEYKRHR
     EIYRPWGRCD VVVQTPRFNV NRITVKPGGA FSMQMHHHRA EHWVILAGTG QVTVNGKQFL
     LSENQSTFIP IGAEHCLENP GCIPLEVLEI QSGSYLGEDD IIRIKDQYGR C