MANC2_ECO57
ID MANC2_ECO57 Reviewed; 482 AA.
AC O85342;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Mannose-1-phosphate guanylyltransferase 2;
DE EC=2.7.7.13;
DE AltName: Full=GDP-mannose pyrophosphorylase 2;
DE Short=GMP 2;
DE Short=GMPP 2;
GN Name=manC2; Synonyms=manC; OrderedLocusNames=Z3195, ECs2836;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=O157:H7 / C664-1992 / EHEC;
RX PubMed=9673232; DOI=10.1128/iai.66.8.3545-3551.1998;
RA Wang L., Reeves P.R.;
RT "Organization of Escherichia coli O157 O antigen gene cluster and
RT identification of its specific genes.";
RL Infect. Immun. 66:3545-3551(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 O antigen. {ECO:0000269|PubMed:9673232}.
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 -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AF061251; AAC32348.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG57091.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36259.1; -; Genomic_DNA.
DR PIR; D90983; D90983.
DR PIR; G85828; G85828.
DR RefSeq; NP_310863.1; NC_002695.1.
DR RefSeq; WP_001278239.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; O85342; -.
DR SMR; O85342; -.
DR STRING; 155864.EDL933_3103; -.
DR EnsemblBacteria; AAG57091; AAG57091; Z3195.
DR EnsemblBacteria; BAB36259; BAB36259; ECs_2836.
DR GeneID; 912820; -.
DR KEGG; ece:Z3195; -.
DR KEGG; ecs:ECs_2836; -.
DR PATRIC; fig|386585.9.peg.2969; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_6; -.
DR OMA; IACVGMK; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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; Reference proteome; Transferase.
FT CHAIN 1..482
FT /note="Mannose-1-phosphate guanylyltransferase 2"
FT /id="PRO_0000194254"
SQ SEQUENCE 482 AA; 54270 MW; 0BB237825F6C4614 CRC64;
MSDAPIIAVV 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
