ID   A2CCX3_PROM3            Unreviewed;       484 AA.
AC   A2CCX3;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   Name=manC {ECO:0000313|EMBL:ABM79333.1};
GN   OrderedLocusNames=P9303_26031 {ECO:0000313|EMBL:ABM79333.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM79333.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM79333.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM79333.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = GDP-alpha-D-mannose
CC         + diphosphate; 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:ARBA00047343};
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; CP000554; ABM79333.1; -; Genomic_DNA.
DR   RefSeq; WP_011827177.1; NC_008820.1.
DR   AlphaFoldDB; A2CCX3; -.
DR   STRING; 59922.P9303_26031; -.
DR   KEGG; pmf:P9303_26031; -.
DR   HOGENOM; CLU_035527_1_0_3; -.
DR   BioCyc; PMAR59922:G1G80-2279-MONOMER; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:TreeGrafter.
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   FunFam; 3.90.550.10:FF:000046; Mannose-1-phosphate guanylyltransferase (GDP); 1.
DR   FunFam; 2.60.120.10:FF:000032; Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR049577; GMPP_N.
DR   InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR   InterPro; IPR001538; Man6P_isomerase-2_C.
DR   InterPro; IPR054566; ManC/GMP-like_b-helix.
DR   InterPro; IPR051161; Mannose-6P_isomerase_type2.
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; PF22640; ManC_GMP_beta-helix; 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:ABM79333.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002274};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABM79333.1}.
FT   DOMAIN          8..293
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          302..355
FT                   /note="MannoseP isomerase/GMP-like beta-helix"
FT                   /evidence="ECO:0000259|Pfam:PF22640"
FT   DOMAIN          362..473
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   484 AA;  53627 MW;  E30D339521DA3979 CRC64;
     MATPPLIPVI LCGGTGTRLW PLSRASYPKQ YWALSGSSEE TLLQQTQQRL KGIEGLSAPL
     LICNEEHRFI VAEQMRQIDV EPNAILLEPM GRNTAPAVTV AALQATERGE DPLLLVLAAD
     HVIRDATQFR HVIEAGRIPA EAGRLVTFGI VPTAPETGYG YIEAAESFGN GEPKALPIAR
     FVEKPDRIAA EQFLANGCFT WNSGMFMFKA SAILSELERL SPEVVSCCRA ALEQEVPDLD
     FLRLEREAFA KCPNVAIDVA VMEKTELGTV LPLDAGWSDV GSWSALWDTT DRDLNGNVLR
     GHVIAESSRN CYLRSEHRLV VGLGVEDLVV VETDDAVLIA NRSQAQDVKT IVKQLEADGS
     PEGKAHRKIY RPWGHYTSVV KDSRWQVKRI ELKPGASLSL QMHHHRAEHW IVVKGTALVE
     KDGEKQLVGE NQSTYIPLGC KHRLTNPGRM PMELIEVQSG PYLCEDDIVR FEDRYGRNES
     VIVN
//