ID M7PKF1_9GAMM Unreviewed; 466 AA.
AC M7PKF1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=MPL1_00030 {ECO:0000313|EMBL:EMR14340.1};
OS Methylophaga lonarensis MPL.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR14340.1, ECO:0000313|Proteomes:UP000012019};
RN [1] {ECO:0000313|EMBL:EMR14340.1, ECO:0000313|Proteomes:UP000012019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPL {ECO:0000313|EMBL:EMR14340.1,
RC ECO:0000313|Proteomes:UP000012019};
RX PubMed=23661481;
RA Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA Murrell J.C., Shouche Y.S.;
RT "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT (Non-Methane-Utilizing) Methylotroph.";
RL Genome Announc. 1:E00202-13(2013).
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:EMR14340.1}.
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DR EMBL; APHR01000001; EMR14340.1; -; Genomic_DNA.
DR RefSeq; WP_009725082.1; NZ_APHR01000001.1.
DR AlphaFoldDB; M7PKF1; -.
DR STRING; 1286106.MPL1_00030; -.
DR PATRIC; fig|1286106.3.peg.6; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000012019; 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 ECO:0000313|EMBL:EMR14340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012019};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMR14340.1}.
FT DOMAIN 3..282
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 311..461
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 466 AA; 52017 MW; F0E941F65E706429 CRC64;
MIPVILSGGT GSRLWPLSRK NKPKQFLNLF GEHSLFQETV LRLSGLDELQ PPMIICNENH
RFMVGDQLGE LGLSATEIIL EPHARNTAPA VTLAALRALE GADDPILLIL AADHVIKDVP
VFHAAIEDAL KLARQNHLVT FGIQADQPHT GYGYIESAEK GQAAKVVRFI EKPDLATAES
YLKAGNFYWN SGMFMFKASV FIEEMQKFAP EIVQACRAAL NNIRTDLDFT RLDAEAFQHC
PSDSVDYAVM EKTQQAMVVP LDAGWSDVGS WSSLWENHPH DEHGNVCIGD VVTESSRNCY
IHSENRLVTA IGVEDLIIVE THDAVMVLPK SRSQDVKTLV ERLNDESRSE ADVHRTCYRP
WGHYDSIDAG GRFQVKRITV KPGASLSLQM HYHRAEHWVV VSGTAEVTCN DEVTILSENQ
STYIPVGAVH RLSNPGRLPL ELIEVQSGSY LEEDDIIRIQ DNYNRQ
//
