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Database: UniProt
Entry: Q11L65_CHESB
LinkDB: Q11L65_CHESB
Original site: Q11L65_CHESB 
ID   Q11L65_CHESB            Unreviewed;       471 AA.
AC   Q11L65;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   OrderedLocusNames=Meso_0456 {ECO:0000313|EMBL:ABG61860.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG61860.1};
RN   [1] {ECO:0000313|EMBL:ABG61860.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG61860.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; CP000390; ABG61860.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11L65; -.
DR   STRING; 266779.Meso_0456; -.
DR   KEGG; mes:Meso_0456; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_5; -.
DR   OrthoDB; 9806359at2; -.
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:ABG61860.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..287
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          316..466
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   471 AA;  51692 MW;  F6F9AB7535B42843 CRC64;
     MTVTPIIISG GAGSRLWPLS RDAHPKPFIE LPDGTSLISR TYGRAARLQG VERIVTVTNR
     DLLFLTADVY AASDAPRRSN GYLLEPFGRD TAAAVALATL HVNEAEGPDA VLLVLPADHL
     IADEDAFAEA VGKAVEMAQT GRIVTFGIVP ERAETGYGYI EAKGGRVLRF VEKPDAKKAA
     DYVASGRFYW NSGMFCFPAR TMLEAMEAHC PEVLVGARAA YRAARKFNAD DREVFEIDRD
     SFAATPAISL DYAVMEKAEN VGCIALDCGW SDIGSWSAVA ELTPADENGN RLRGEVLLED
     TSNSFVHSEH RLVGLVGVSD LLVVDTPDAL LVAHKEKAQE VKRLFNRLKE QGHHAAKLHC
     TAHRPWGTYT VLEEGDRFKI KRIEVKPGAR LSLQAHHHRS EHWVVVSGTA KIVNGDQEIL
     LATNQSTYIP CGFKHRLENP GILPLVLIEV QSGDYLGEDD IIRFDDVYGR N
//
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