ID Q121H6_POLSJ Unreviewed; 470 AA.
AC Q121H6;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN OrderedLocusNames=Bpro_4942 {ECO:0000313|EMBL:ABE46816.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OG Plasmid pPol360 {ECO:0000313|Proteomes:UP000001983}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46816.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000317; ABE46816.1; -; Genomic_DNA.
DR RefSeq; WP_011485800.1; NC_007949.1.
DR AlphaFoldDB; Q121H6; -.
DR KEGG; pol:Bpro_4942; -.
DR HOGENOM; CLU_035527_1_0_4; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000001983; Plasmid pPol360.
DR GO; GO:0005525; F:GTP binding; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ABE46816.1}; Plasmid {ECO:0000313|EMBL:ABE46816.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE46816.1}.
FT DOMAIN 4..283
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 315..465
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 470 AA; 51746 MW; D4E1DE6E9B31E63F CRC64;
MLIPVILCGG AGSRLWPVSR ELHPKPFMRL ADGQSLLQKA FQRGAHLPGV KEILTVTNRE
LFFKTEDEYR PVNPRGLLTS FLLEPFGRNT AAAVAAAALQ VQRTHGDGAV LLVLPADHLI
ADQAAFADAV VQARALAEQG RVVTFGIRPE GPETGFGYIE AEGHDVKRFV EKPDLETARQ
YLASGRYWWN SGMFCFTAGA MLAELEQHCP RILAAARKCL EQSRTATGKG LQQTELDAES
FAEVPDDSID YAVMEKTRRI SMVPCALGWS DIGSWTAVGE LSEADGCGNR VQGHALMHDT
TDCYIQSQDR LVGTVGVADL IIIDTPDALL VANRHSSQNV KQIYAQLKTL GHDAHKVHRT
VHRPWGTYTV LEEGPQFKIK RIEVKPGAAL SLQMHHHRSE HWIVVSGTAS IVNGEQDILL
LTNQSTYIPA GHKHRLINPG VIDLVMIEVQ SGAYLGEDDI VRFEDDYGRV
//
