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Database: UniProt
Entry: B8EI62_METSB
LinkDB: B8EI62_METSB
Original site: B8EI62_METSB 
ID   B8EI62_METSB            Unreviewed;       470 AA.
AC   B8EI62;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   OrderedLocusNames=Msil_1595 {ECO:0000313|EMBL:ACK50544.1};
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK50544.1, ECO:0000313|Proteomes:UP000002257};
RN   [1] {ECO:0000313|EMBL:ACK50544.1, ECO:0000313|Proteomes:UP000002257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC   {ECO:0000313|Proteomes:UP000002257};
RX   PubMed=20472789; DOI=10.1128/JB.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK50544.1; -; Genomic_DNA.
DR   RefSeq; WP_012590614.1; NC_011666.1.
DR   AlphaFoldDB; B8EI62; -.
DR   STRING; 395965.Msil_1595; -.
DR   KEGG; msl:Msil_1595; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_5; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000002257; Chromosome.
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:ACK50544.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ACK50544.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACK50544.1}.
FT   DOMAIN          6..285
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;  51606 MW;  7B28254CAA11A4BF CRC64;
     MPKILPVIMC GGSGTRVWPE SRESLPKQFI SLVGTRSTFQ MAAEILKDPV FENPIVISNH
     DYRFLVSEQL AEIKREARIV LEPVRRDSAP AVAVAAELAA QLGPETVVAL LAADHVVQDT
     KGFVELCKQA AEAAALGYIV TLGIKPTEPA TGYGYIKTGK PVSLDGAVLK VAGFVEKPDA
     ATAEKYIAEN YLWNSGNFFF RADVMQAELQ KFAPAVAEAA AAAVAAAKQD LNFLVLDKDA
     FSAAPKISID YAVMERTDKA AVVPADIGWS DVGNWAAVWD LSDRDEFGNS TRGNGVVMNA
     SNVHIRSDDF LTTVVGVDNV IVVTTQDAVL VLNKACGDQV KQLVDRLKAE GRPEALQHKR
     SYRPWGYYQS VDNGARYQVK RIVVKPGQRL SLQKHFHRAE HWIVVRGTAE VTRDSEVIFV
     HENESIYLPI GCTHRMTNPG RIDLELIEVQ TGSYLGEDDI IRIEDIYNRG
//
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