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Database: UniProt
Entry: Q9ZN23_HELPJ
LinkDB: Q9ZN23_HELPJ
Original site: Q9ZN23_HELPJ 
ID   Q9ZN23_HELPJ            Unreviewed;       470 AA.
AC   Q9ZN23;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 111.
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:AAD05624.1};
GN   OrderedLocusNames=jhp_0037 {ECO:0000313|EMBL:AAD05624.1};
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963 {ECO:0000313|EMBL:AAD05624.1, ECO:0000313|Proteomes:UP000000804};
RN   [1] {ECO:0000313|EMBL:AAD05624.1, ECO:0000313|Proteomes:UP000000804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824 {ECO:0000313|Proteomes:UP000000804};
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(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   -!- 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; AE001439; AAD05624.1; -; Genomic_DNA.
DR   PIR; C71981; C71981.
DR   RefSeq; WP_000694964.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZN23; -.
DR   KEGG; hpj:jhp_0037; -.
DR   PATRIC; fig|85963.30.peg.1002; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Isomerase {ECO:0000313|EMBL:AAD05624.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..279
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"
SQ   SEQUENCE   470 AA;  53325 MW;  87D4739773608D50 CRC64;
     MKIKNVLLSG GSGKRLWPLS RSLYPKQFLK LFDHKSLFEL SFKRNASLVD ETLIVCNEKH
     YFLALEEIKN EIKNKSVGFL LESLSKNTAN AIALSALMSD KEDLLIVTPS DHLIKDFQAY
     ENAIKKAINL AQKGFLVTFG ISIEKPNTEF GYIESPNGLD VKRFIEKPSL EKAIEFQKSG
     GFYFNSGMFV FQAGVFLDEL KKHAPTILKG CERAFESLEN THFFEQKIAR LSEKSMQDLE
     DMSIDIALMQ QSHKIKMVEL NAKWSDLGNF NALFEEAANG TKENVSLNQT PIFAKESTNN
     LVFSHKVSAL LGVEDLAIID TKDALLVAHK DKAKDLKALV SEIETHNQEL LQTHTKVYRP
     WGSYEVLHES GCYKVKILEV KPNARLSLQK HFHRSEHWVV ISGMASVELD HQSFELQANE
     STYIPKNTLH RLANYGKIPL IIIEVQVGEY VGEDDIVRVD DDFNRQNQNA
//
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