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Database: UniProt
Entry: A0A254Q4F0_9BURK
LinkDB: A0A254Q4F0_9BURK
Original site: A0A254Q4F0_9BURK 
ID   A0A254Q4F0_9BURK        Unreviewed;       498 AA.
AC   A0A254Q4F0;
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=CBI30_09460 {ECO:0000313|EMBL:OWS70372.1};
OS   Polynucleobacter aenigmaticus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=1743164 {ECO:0000313|EMBL:OWS70372.1, ECO:0000313|Proteomes:UP000198104};
RN   [1] {ECO:0000313|EMBL:OWS70372.1, ECO:0000313|Proteomes:UP000198104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-K35W1 {ECO:0000313|EMBL:OWS70372.1,
RC   ECO:0000313|Proteomes:UP000198104};
RA   Hahn M.W.;
RT   "Polynucleobacter sp. MWH-K35W1 isolated from the permanently anoxic
RT   monimolimnion of a meromictic lake.";
RL   Submitted (MAY-2017) 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:OWS70372.1}.
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DR   EMBL; NGUO01000015; OWS70372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254Q4F0; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000198104; 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:OWS70372.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:OWS70372.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OWS70372.1}.
FT   DOMAIN          6..315
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          343..493
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   498 AA;  54711 MW;  9DA0D73DFB4F627D CRC64;
     MTQVTPVILC GGSGTRLWPL SRSGFPKQFL VLSGDDSSQS LFQQAVERIN AISSSHIQVG
     STLIVTNEDH RFLALDQLRD LKGIQATLLL EPSGRNTAPA LTLAAFQAKD GVGDQDGGSH
     DPILVITPAD QTVKNSKAFT KALQDCIAVV DADHSKKTIA ILGITPAAPE TGYGYIKRSA
     IKGTHGEYPV EQFVEKPDSK TAQAYLEDGN YLWNSGMFVL RASTWLAALK EFRPDIFGAT
     ETAWVGKTMD RSGQTPFVRP DPEIFKTIPS ESIDYAVIEK CPGSQFRVNM VELNAGWNDL
     GAWDAVWQVG KQDEQGNVTS GDILLANSKN SLVHASSRLV SAVGVENLII IETADAVMVA
     DRKNSQDVKH IVNQLEAQKR EEKNLHRKVA RPWGWYDSVD EGERFKVKRI QVKPGASLSL
     QMHHHRAEHW IVVKGTAEIT NGDQVITLTE NQSTYIPKGQ THRLANPGNT PLEIIEVQSG
     SYLGEDDIVR FEDTYGRS
//
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