ID I0QV29_9GAMM Unreviewed; 470 AA.
AC I0QV29;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=SPM24T3_08759 {ECO:0000313|EMBL:EIC85152.1};
OS Serratia sp. M24T3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC85152.1, ECO:0000313|Proteomes:UP000011072};
RN [1] {ECO:0000313|EMBL:EIC85152.1, ECO:0000313|Proteomes:UP000011072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC85152.1,
RC ECO:0000313|Proteomes:UP000011072};
RX PubMed=22740681; DOI=10.1128/JB.00670-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT Disease Nematode Bursaphelenchus xylophilus.";
RL J. Bacteriol. 194:3764-3764(2012).
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
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:EIC85152.1}.
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DR EMBL; AJHJ01000007; EIC85152.1; -; Genomic_DNA.
DR RefSeq; WP_009636352.1; NZ_AJHJ01000007.1.
DR AlphaFoldDB; I0QV29; -.
DR STRING; 932213.SPM24T3_08759; -.
DR PATRIC; fig|932213.3.peg.1769; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000011072; 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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIC85152.1}.
FT DOMAIN 4..287
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; 52990 MW; B73E4DD061440F61 CRC64;
MLLPVIMAGG TGSRLWPMSR ELYPKQFLRL HSKNSMLQET VLRLDDLEVR EPVVICNDEH
RFLVAEQLRQ IKKLSNNIIL EPVGRNTAPA IALAALNAIK DGDDPVMLVL AADHVINNVE
KFHEVVEKAI PFASKNSLVT FGIVPTGPET GYGYIQRGES IGELDEGYQV KCFVEKPDSA
TAETYIASGE YYWNSGMFMF RAKKYLEELE KFRPDIYEAC KKSLHDLPDG MDFITVDKEA
FSLCPDDSVD YAVMEKTRNA MVVPLDAGWS DVGSWSALWE VNEKDEQNNA LTGDVFLHNT
HDCYINTDEK MVAAVGVQNL VIVNTKDALL VVDKSKVQDV KKVVEYLKTN LRSEYKHHRD
IYRPWGKSDL VVAENRFNVN RVTVNPGGKL STQMHHHRAE HWIILAGTAQ VTISDNTFLL
TENQSTFIPI GSVHTLENPG KIPLEILEVR SGSYLGNDDV IRIKDHYGRN
//
