MANC7_ECOLX
ID MANC7_ECOLX Reviewed; 464 AA.
AC P37741;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 98.
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;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O7:K1 / VW187;
RX PubMed=7677991; DOI=10.1128/jb.175.1.148-158.1993;
RA Marolda C.L., Valvano M.A.;
RT "Identification, expression, and DNA sequence of the GDP-mannose
RT biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187
RT (Escherichia coli O7:K1).";
RL J. Bacteriol. 175:148-158(1993).
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 O7 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 -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AF125322; AAC27538.1; -; Genomic_DNA.
DR PIR; C40630; C40630.
DR RefSeq; WP_000097982.1; NZ_UIJD01000062.1.
DR AlphaFoldDB; P37741; -.
DR SMR; P37741; -.
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..464
FT /note="Mannose-1-phosphate guanylyltransferase"
FT /id="PRO_0000194258"
SQ SEQUENCE 464 AA; 52611 MW; D1133D2D2B22E024 CRC64;
MSSPLIPVIL SGGNGTRLWP LSREEYPKQF LKLTDSISML QSTISRLDSL NTSSPVVICN
ELHRFIVAEQ LRHLNKLDNN IILEPSGRNT APAICIAALI LKMKHPNENP LMLVLPADHS
VKKVKTFCNT IKSAIPFAEA GNLVSFGIKP THPETGYGYI QKGKVLSDSD IYEVSEVRTF
VEKPNLKTAE SFIEKDEYYW NSGMYLFSVE RYLQELSLYR PDIVKVCQET VKNIHYDMDF
IRLDDKIFRN CPQESIDYAV MEKTKDAVVA TMDIGWNDVG AWSSLWELGK KDSSGNVITG
DIVCHETENS YIYTESGLVA TIGIQDLVII HTKDSLLVSR RDSVQNVKNI VQHLDLSGRK
EHKEHREVFK SWGRCDSIDS SEKYHYQVKR ITVNPSENYR CNYIITVRNI GVVVMGIAKL
TVAEEIKILK ENESVYIPAG IKHSLKILDN TTCVNRSLDR FLSC