ID   A0A1G6THM9_9BURK        Unreviewed;       494 AA.
AC   A0A1G6THM9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=SAMN05192589_105153 {ECO:0000313|EMBL:SDD28529.1};
OS   Paracidovorax valerianellae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=187868 {ECO:0000313|EMBL:SDD28529.1, ECO:0000313|Proteomes:UP000198781};
RN   [1] {ECO:0000313|EMBL:SDD28529.1, ECO:0000313|Proteomes:UP000198781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16619 {ECO:0000313|EMBL:SDD28529.1,
RC   ECO:0000313|Proteomes:UP000198781};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMZC01000005; SDD28529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6THM9; -.
DR   STRING; 187868.SAMN05192589_105153; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000198781; 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:SDD28529.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SDD28529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198781};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDD28529.1}.
FT   DOMAIN          9..301
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          332..482
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   494 AA;  53990 MW;  72529B95F2354B0B CRC64;
     MTVAQPLLPV ILCGGSGTRL WPLSREAYPK QFLTLAGSRT LLQDTALRLQ GWAPEIGIAA
     DPILVCNTEH RFVAASQLLA VGIRKARVLL EPVGRNTAPA LTLAALQAGA EGHDPVMLAM
     PADHVVQDLL AFHAAVRRAF SIAEAGGLVT FAVVPDRPET GYGYMQCHPA GVEGPGIHRI
     ASFAEKPDAP TAQRYLDAGD YFWNSGLFMV RASQWIAAIR ACRPDILSAC ESAMQGAQRD
     LDFIRPDVSA FEACPSDSID YAVMERLPLM PEVGIPTFAV ALQAGWSDLG AWDALWKVLE
     RDGDGNATVG DALLENSENT LLMSTHRLVA GVGLDHIVVV ETPDAVLVAD KRRTQDVKHI
     VARLKQEGHA LAHHHRKVHR PWGWYDAIDS GERFQVKRIV VNPGARLSMQ MHYHRAEHWV
     VVRGTAEITN GDDTYLLAQN ESTFIPVGRR HRLANPGKTP LEIIEVQSGD YLGEDDIVRF
     DDIYGRSTNA EGLS
//