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Database: UniProt
Entry: A0A1I7EBL0_9RHOB
LinkDB: A0A1I7EBL0_9RHOB
Original site: A0A1I7EBL0_9RHOB 
ID   A0A1I7EBL0_9RHOB        Unreviewed;       473 AA.
AC   A0A1I7EBL0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=SAMN05216236_1604 {ECO:0000313|EMBL:SFU21311.1};
OS   Sedimentitalea nanhaiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Sedimentitalea.
OX   NCBI_TaxID=999627 {ECO:0000313|EMBL:SFU21311.1, ECO:0000313|Proteomes:UP000182466};
RN   [1] {ECO:0000313|EMBL:SFU21311.1, ECO:0000313|Proteomes:UP000182466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10959 {ECO:0000313|EMBL:SFU21311.1,
RC   ECO:0000313|Proteomes:UP000182466};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FPAW01000060; SFU21311.1; -; Genomic_DNA.
DR   RefSeq; WP_027260314.1; NZ_FPAW01000060.1.
DR   AlphaFoldDB; A0A1I7EBL0; -.
DR   STRING; 999627.SAMN05216236_1604; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000182466; 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:SFU21311.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SFU21311.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182466};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFU21311.1}.
FT   DOMAIN          4..282
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          318..468
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   473 AA;  50704 MW;  2A944E5573A6DDD0 CRC64;
     MITPVLLCGG SGTRLWPLSR KSYPKQFAAL IGDSTLFQAS AARLSGPDFA APMVLTNSDF
     RFIVTEQLAE VGVDPAAILI EPAGRNTAPA VLAAALWLQK SDPEALMLVA PSDHVVPDAA
     AFRAAVLAGV PAARAGQLVT FGIKPTHAET GYGYLELAED PGDFAARPLA LNRFVEKPDA
     ARAAEMLTAG NYLWNAGIFL FSVATIIAAF RAHAPDLVDP VQAAVDQGQP DLGFLRLAPE
     PWAQVDDISI DYAVMERADN LSVVPYAAGW SDLGGWDAVW RETGPDERGV ATAGNATALD
     CDDTLLRSED DALEVVGIGL RNIIAVAMPD AVLVADVSRA QDVKLAVAAL KAKQAKQAES
     FPKDHRPWGW FESLVIGERF QVKRIVVHPG AALSLQSHHH RSEHWIVVEG TARVTVDGAV
     KLVSENQSVY IPLGAVHRME NPGKVPMVLI EVQTGSYLGE DDIIRYEDVY ARS
//
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