ID U4RIH4_HELPX Unreviewed; 493 AA.
AC U4RIH4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=N204_04420 {ECO:0000313|EMBL:EPZ97945.1};
OS Helicobacter pylori UM085.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1352344 {ECO:0000313|EMBL:EPZ97945.1, ECO:0000313|Proteomes:UP000016853};
RN [1] {ECO:0000313|EMBL:EPZ97945.1, ECO:0000313|Proteomes:UP000016853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM085 {ECO:0000313|EMBL:EPZ97945.1,
RC ECO:0000313|Proteomes:UP000016853};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(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:EPZ97945.1}.
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DR EMBL; AUSP01000008; EPZ97945.1; -; Genomic_DNA.
DR AlphaFoldDB; U4RIH4; -.
DR PATRIC; fig|1352344.3.peg.567; -.
DR Proteomes; UP000016853; 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:EPZ97945.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..305
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 334..484
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 493 AA; 55712 MW; BA4223FB9D302307 CRC64;
MTQKCPIKNA IITLKKESLT RKLMKIKNIL LSGGSGKRLW PLSRSLYPKQ FLKLFGNESL
FKLSFKRNAS LVDETLIVCN EKHYFLALEE IESEIKNKSV GFLLESLSKN TANAIALSAL
MSEREDLLIV TPSDHLIKDI QAYENAMKKA IDLAQKGFLV TFGINIEKPN TEFGYIESPN
GLDVKRFIEK PSLEKAIEFQ KSGGFYFNSG MFVFQAGVFL DELKKHAPTI LKGCERAFES
LKRASFLGKA VARLNTESMQ DLEDVSVDIA LMQQSHKIKM VGLNAKWSDL GNFNALFEEV
ANDLKENVSL NQTPIFAKES QNNLVFSHKV SALLGVENLA IIDTKDALLI AHKDKAKDLK
ALVSEVETNN QELLQTHTKV YRPWGSYEVL HESGCYKVKI LEVKPNARLS LQKHFHRSEH
WVVISGMASV ELDRQSFELQ ANESTYIPKN TLHRLANYGK IPLIIIEVQV GEYVGEDDIV
RVDDDFNRQN QGK
//
