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Database: UniProt
Entry: G2M740_HELPX
LinkDB: G2M740_HELPX
Original site: G2M740_HELPX 
ID   G2M740_HELPX            Unreviewed;       470 AA.
AC   G2M740;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=HPPN135_00205 {ECO:0000313|EMBL:AEN17755.1};
OS   Helicobacter pylori Puno135.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1055529 {ECO:0000313|EMBL:AEN17755.1, ECO:0000313|Proteomes:UP000008533};
RN   [1] {ECO:0000313|EMBL:AEN17755.1, ECO:0000313|Proteomes:UP000008533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puno135 {ECO:0000313|EMBL:AEN17755.1,
RC   ECO:0000313|Proteomes:UP000008533};
RA   Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H.,
RA   Berg D.E.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CP002982; AEN17755.1; -; Genomic_DNA.
DR   RefSeq; WP_000694825.1; NC_017379.1.
DR   AlphaFoldDB; G2M740; -.
DR   KEGG; heu:HPPN135_00205; -.
DR   PATRIC; fig|1055529.4.peg.39; -.
DR   HOGENOM; CLU_035527_1_0_7; -.
DR   Proteomes; UP000008533; Chromosome.
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: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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEN17755.1}.
FT   DOMAIN          4..278
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          311..461
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
FT   COILED          326..353
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   470 AA;  53209 MW;  79BB7C36CA976F92 CRC64;
     MKIKNILLSG GSGKRLWPLS RSLYPKQFLK LFGNESLFEL SFKRNASLVD ETLIVCNEKH
     YFLALEEIEN EIKNKSVGFL LESLSKNTAN AIALSALMSE REDLLIVTPS DHLIKDIQAY
     ENAIKKAIDL AQKGFLVTFG INIEKPNTEF GYIESPNGLD VKRFIEKPSL EKAIEFQKSG
     GFYFNSGMFV FQAGVFLDEL KKHAPIILKG CERAFESLER ASFFEKKIAR LSEKSMQDLE
     DVSVDIALMQ QSHKIKMVGL NAKWSDLGNF NALFEEVANE PKENVSLNQT PVFAKESQNN
     LVFSHKVSAL LGVENLAIID TKDALLIAHK DKAKDLKALV SEVEANNQEL LQTHTKVYRP
     WGSYEILHES GCYKVKILEV KPNARLSLQK HFHRSEHWVV ISGMASVELD HQSFELQANE
     STYIPKNTLH RLANYGKIPL TIIEVQVGEY VGEDDIVRVD DDFNRQNQGK
//
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