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Database: UniProt
Entry: A0A2G1MDH3_9RHOB
LinkDB: A0A2G1MDH3_9RHOB
Original site: A0A2G1MDH3_9RHOB 
ID   A0A2G1MDH3_9RHOB        Unreviewed;       481 AA.
AC   A0A2G1MDH3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, 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=CJ301_15180 {ECO:0000313|EMBL:PHP26712.1};
OS   Limimaricola cinnabarinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1125964 {ECO:0000313|EMBL:PHP26712.1, ECO:0000313|Proteomes:UP000221860};
RN   [1] {ECO:0000313|EMBL:PHP26712.1, ECO:0000313|Proteomes:UP000221860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XM1 {ECO:0000313|EMBL:PHP26712.1,
RC   ECO:0000313|Proteomes:UP000221860};
RA   Ma R., Wang J., Wang Q., Ma Z., Li J., Chen L.;
RT   "Draft Genome Sequence of Loktanella cinnabarina Strain XM1, Isolated from
RT   Coastal Surface Water.";
RL   Submitted (AUG-2017) 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:PHP26712.1}.
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DR   EMBL; NQWH01000030; PHP26712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1MDH3; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000221860; 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:PHP26712.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:PHP26712.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PHP26712.1}.
FT   DOMAIN          6..291
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          326..476
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   481 AA;  51836 MW;  F224EE6164DE1605 CRC64;
     MTTITPVLLC GGSGTRLWPL SRKSYPKQFV PLMGEETLFQ ASARRLHGRG LGPDGDLGFA
     SPLVLTNADF RFIVTEQLGL AGIDPRAVLI EPEGRNTAPA ILAAASYLVA SDPEAVMLVA
     PSDHVVPDAA SFYAAVAQGL GPVREGRLVT FGIAPTHAET GYGYLELEGP VDDGAPQPLT
     RFVEKPDLGR AEDMLASGNF LWNAGIFMAR AADMVAAFRE HGPEILGPVE AALAQAKTDL
     GFLRLDPASW ATAPDISIDY AVMEKAPNLS VVPFSGEWSD LGGWDAVWRE SGPDESGVVT
     SQGATAIDCR DTLLRSESDR LEIVGIGLEN VMAIAMNDAV LVADMSRAQD VKKAVEALKA
     KQSPQATAFP KDHRPWGWFE SLVIGGRFQV KRIMVHPGAA LSLQSHHHRS EHWIVVEGTA
     RVTIDDEVKL VTENQSVYVP LGAVHRMENP GKVPMVLIEV QTGAYVGEDD IVRYEDVYAR
     N
//
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