ID J0J057_HELPX Unreviewed; 472 AA.
AC J0J057;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=HPNQ4228_0263 {ECO:0000313|EMBL:EJB31260.1};
OS Helicobacter pylori NQ4228.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992025 {ECO:0000313|EMBL:EJB31260.1, ECO:0000313|Proteomes:UP000004299};
RN [1] {ECO:0000313|EMBL:EJB31260.1, ECO:0000313|Proteomes:UP000004299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NQ4228 {ECO:0000313|EMBL:EJB31260.1,
RC ECO:0000313|Proteomes:UP000004299};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJB31260.1}.
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DR EMBL; AKNT01000001; EJB31260.1; -; Genomic_DNA.
DR RefSeq; WP_000694805.1; NZ_AKNT01000001.1.
DR AlphaFoldDB; J0J057; -.
DR PATRIC; fig|992025.3.peg.263; -.
DR Proteomes; UP000004299; Unassembled WGS sequence.
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:EJB31260.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EJB31260.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJB31260.1}.
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 472 AA; 53720 MW; 210E27C353A2197C CRC64;
MKIKNILLSG GSGKRLWPLS RSLYPKQFLK LFDHKSLFEL SFKRNASLVD ETLIVCNEKH
YFLALEEIEN EIQNKSVGFL LESLSKNTAN AISLSTLMSD KEDLLIVTPS DHLIKDFQAY
ENAMKKAINL AQKGFLVTFG VSIDKPNTEF GYIESPNGLD VKRFIEKPSL EKAIEFQKSG
GFYFNSGMFV FQAGVFLDEL KKHAPTILRG CERAFESLEN AYFFENKIAR LSEKSMQDLE
DVSVDIALMQ QSHKIKMVEL NAKWSDLGNF NALFEEAANE PKENVSLNQT PIFAKESANN
LVFSHKVSAL LGVEDLAIID TKDALLIAHK DKAKDLKALV SEIETHNQEL LQTHTKVYRP
WGSYEVLHES GCYKVKILEV KPNARLSLQK HFHRSEHWVV ISGMASVELD HKMFELQANE
STYIPKNTLH RLANYGKIPL IIIEVQVGEY VGEDDIVRVD DDFNRQNQKN LI
//
