ID A0A0N1N4T2_9PROT Unreviewed; 492 AA.
AC A0A0N1N4T2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=GLUCOINTEAF2_0202375 {ECO:0000313|EMBL:KPH87015.1};
OS Komagataeibacter intermedius AF2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH87015.1, ECO:0000313|Proteomes:UP000031553};
RN [1] {ECO:0000313|EMBL:KPH87015.1, ECO:0000313|Proteomes:UP000031553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF2 {ECO:0000313|EMBL:KPH87015.1,
RC ECO:0000313|Proteomes:UP000031553};
RA Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J., Gonzalez-Garcia L.N.,
RA Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2, Isolated
RT from Kombucha Tea.";
RL Submitted (JUL-2015) 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:KPH87015.1}.
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DR EMBL; JUFX02000168; KPH87015.1; -; Genomic_DNA.
DR RefSeq; WP_048883812.1; NZ_JUFX02000168.1.
DR AlphaFoldDB; A0A0N1N4T2; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000031553; Unassembled WGS sequence.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KPH87015.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPH87015.1}.
FT DOMAIN 23..308
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 338..487
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 492 AA; 54857 MW; 3E81536A2BC518D9 CRC64;
MTFMTATDVT VSTPEPRNRT ITPVILSGGT GTRLWPVSRA SHPKQFWALA SSRTMIGETL
QRATGTAFAP PIVVCNNAHR FLVAEQLREN GCEDGRIILE PAVRNTAAAI AAAALLAAQD
DPETLLWIMA ADAVFRYPER LPAVLEKAMT VAREGYIVTF GMKPDVPETG YGYIRLGAPL
RPGDADDNVY RVARFIEKPD RLRATEMLNE GGYLWNSGMF LAPASVILAE LKRHEPDVLE
NVRHALLHSE SDLTFRRLET ASFMRCPNVS IDYAVMERTD RAVVIPADLG WSDIGNWNAL
WELGDKDATG NVVVGDVVLE QSHNCYVRSE GMLTAVAGLT DIVLVVTSDA VLAIHRDYAQ
DVSALVSQLK MAKRTEAEIH NRCYRPWGFY EGLIQGERFQ VKRIVVYPGQ KLSLQKHFHR
AEHWVVVSGT AIVTRNEEKL MLQENESVYL PLGCMHRLEN PGRIPLTLIE VQSGPYLGED
DIVRFEDTYG RQ
//
