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Database: UniProt
Entry: W9DN73_METTI
LinkDB: W9DN73_METTI
Original site: W9DN73_METTI 
ID   W9DN73_METTI            Unreviewed;       464 AA.
AC   W9DN73;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=MettiDRAFT_0863 {ECO:0000313|EMBL:ETA67439.1};
OS   Methanolobus tindarius DSM 2278.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA67439.1, ECO:0000313|Proteomes:UP000019483};
RN   [1] {ECO:0000313|EMBL:ETA67439.1, ECO:0000313|Proteomes:UP000019483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA67439.1,
RC   ECO:0000313|Proteomes:UP000019483};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (AUG-2013) 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}.
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:ETA67439.1}.
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DR   EMBL; AZAJ01000001; ETA67439.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9DN73; -.
DR   STRING; 1090322.MettiDRAFT_0863; -.
DR   Proteomes; UP000019483; 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:ETA67439.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ETA67439.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETA67439.1}.
FT   DOMAIN          8..276
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          307..456
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   464 AA;  53145 MW;  3DA593B90CFF8655 CRC64;
     MTGDETIKSI ILAGGSGTRL WPLSRELYPK QFLKIEDVSL FQETILRCLQ ISEISEIYVV
     TNELHKYFVI GQIEELGYEI PRDNILLEPE GKNTLPAIYY GITEIQKVHG NSMVAVFSSD
     HKLDKSAMET IKNARQLSSE HLVTFGILPK SPHTGYGYIK PGDKLNIGYK VSEFREKPDY
     KDAEKYISEG CLWNSGMFLF STELFLNEVA LYASDVKDSF ESSNNIQDIF ENVPNISIDY
     GIMEKSSKVA VVELNHKWSD LGNFNALYEE LNKDEKGNCV LECEQLLLNS KNNFIYSSPE
     KLVSTIDIND LIVVDTSDAL MICPRQSCEK VKDIVNVLKQ RNDERVNLHE TVYRPWGSYT
     LLEKSKKHKI KNISVLPGKK LSLQLHHHRS EHWVIVKGIA CVENNEDKYF LRQGESTFIR
     AGMKHRLSNP GKLPLEIIEV QLGEYVEEDD IIRYDDEYGR VKKT
//
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