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Database: UniProt
Entry: A0A0C1J007_9RHOB
LinkDB: A0A0C1J007_9RHOB
Original site: A0A0C1J007_9RHOB 
ID   A0A0C1J007_9RHOB        Unreviewed;       472 AA.
AC   A0A0C1J007;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=cpsB {ECO:0000313|EMBL:KIC41332.1};
GN   ORFNames=RA27_10680 {ECO:0000313|EMBL:KIC41332.1};
OS   Ruegeria sp. ANG-R.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC41332.1, ECO:0000313|Proteomes:UP000031318};
RN   [1] {ECO:0000313|Proteomes:UP000031318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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:KIC41332.1}.
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DR   EMBL; JWLJ01000003; KIC41332.1; -; Genomic_DNA.
DR   RefSeq; WP_039539015.1; NZ_JWLJ01000003.1.
DR   AlphaFoldDB; A0A0C1J007; -.
DR   STRING; 1577903.RA27_10680; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000031318; 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: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:KIC41332.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIC41332.1}.
FT   DOMAIN          4..277
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          314..464
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   472 AA;  51741 MW;  E083CD5B909E9606 CRC64;
     MIQPIILAGG SGTRLWPVSR KSYPKQFVEL DGDNSLFQKT VERVAEPGFS APLIVTGEDY
     RFIAQQQLAD VDAEKSELIV EPVGRNTAAA VLAAALRYKE EPETILLVLP SDHAIEDVSA
     FRRTMVRAEK TAKRGKIVTF GIKPDHAATG FGYLRVAGGY QGALLISTFA EKPDAQTAKV
     MLESGDWLWN AGMFMFRVDT VLKAFEAHAP EMSAPVEAAV ALGQKDLGFY RLDQNAFFRC
     PSLSFDHAVM EHVEKGVVAF ELDCGWSDLG SWKSVKDQGQ LDEGANVTSG NSTAIDCRDS
     LLRSENPDIK LVGLGLKDIV AVATDDGILV ADMSHSAEVG KVVDALRNEG SDQAEMFRRC
     HRPWGYYETL SLGSRFQVKR IMVLPGAKLS LQSHMHRAEH WVVVSGSATV TVGDRVSLLS
     ENESTYIPLG AVHRLENPGK LPLHLIEVQS GCYLGEDDIV RYEDIYDRVA VA
//
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