ID K2KKG7_HELPX Unreviewed; 470 AA.
AC K2KKG7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=OUS_0315 {ECO:0000313|EMBL:EKE96246.1};
OS Helicobacter pylori R056a.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145118 {ECO:0000313|EMBL:EKE96246.1, ECO:0000313|Proteomes:UP000006748};
RN [1] {ECO:0000313|EMBL:EKE96246.1, ECO:0000313|Proteomes:UP000006748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R056a {ECO:0000313|EMBL:EKE96246.1,
RC ECO:0000313|Proteomes:UP000006748};
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:EKE96246.1}.
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DR EMBL; AMOY01000003; EKE96246.1; -; Genomic_DNA.
DR RefSeq; WP_000694798.1; NZ_AMOY01000003.1.
DR AlphaFoldDB; K2KKG7; -.
DR PATRIC; fig|1145118.3.peg.312; -.
DR Proteomes; UP000006748; 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:EKE96246.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EKE96246.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKE96246.1}.
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 470 AA; 53273 MW; D835D4AF11689844 CRC64;
MKIKNILLSG GSGKRLWPLS RSLYPKQFLK LFDHKSLFEL SFKRNASLVD ETLIVCNEKH
YFLALEEIEN EIKNKSVGFL LESLSKNTAN AIALSALMSE REDLLIVTPS DHLIKDLQAY
ENAIKKAINL AQKGFLVTFG VSIDKPNTEF GYIESPNGLD VKRFIEKPSL EKAIEFQKSG
GFYFNSGMFV FQAGVFLDEL KKHAPTILKG CERAFESLEN THFFEQKIAR LSEKSMQDLE
DVSVDIALMQ QSHKIKMVGL NAKWSDLGNF NALFEEVANE SKENVSLNQT PVFAKESANN
LVFSHKVSAL LGVENLAVID TKDALLIAHK DKAKDLKALV SEIEMHNQEL LQTHTKVYRP
WGSYEVLHES GCYKVKILEV KPNARLSLQK HFHRSEHWVV ISGMASVELD HQSFELQANE
STYIPKNTLH RLANYGKIPL IIIEVQVGEY VGEDDIVRVD DDFNRQNQNA
//
