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Database: UniProt
Entry: A0A076HC51_9SYNE
LinkDB: A0A076HC51_9SYNE
Original site: A0A076HC51_9SYNE 
ID   A0A076HC51_9SYNE        Unreviewed;       486 AA.
AC   A0A076HC51;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:AII46708.1};
GN   ORFNames=KR49_09665 {ECO:0000313|EMBL:AII46708.1};
OS   Synechococcus sp. KORDI-49.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=585423 {ECO:0000313|EMBL:AII46708.1, ECO:0000313|Proteomes:UP000028589};
RN   [1] {ECO:0000313|EMBL:AII46708.1, ECO:0000313|Proteomes:UP000028589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-49 {ECO:0000313|EMBL:AII46708.1,
RC   ECO:0000313|Proteomes:UP000028589};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequences of Synechococcus sp. KORDI-49.";
RL   Submitted (JUN-2013) 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; CP006270; AII46708.1; -; Genomic_DNA.
DR   RefSeq; WP_043694290.1; NZ_CP006270.1.
DR   AlphaFoldDB; A0A076HC51; -.
DR   STRING; 585423.KR49_09665; -.
DR   KEGG; synr:KR49_09665; -.
DR   PATRIC; fig|585423.3.peg.1857; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_3; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000028589; Chromosome.
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:AII46708.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AII46708.1}.
FT   DOMAIN          8..292
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          323..473
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   486 AA;  53459 MW;  128CDB4C2DA62E32 CRC64;
     MAATPLIPVI LCGGTGTRLW PLSRASYPKQ YWALSGDGES TLLQQTQQRL NGLDGLGSPL
     LICNEDHRFI VAEQMRQIDV EPNAILLEPM GRNTAPAVTV AALQATADGA DPLLLVLAAD
     HVIRDASHFR AVVEAGRRPA EEGRLVTFGI VPTAPETGYG YIEAAQPFSG GPLQDVPIAR
     FVEKPDRATA ETFLSTGRFT WNSGMFLFRA SAMLAELERL SPEVVSCCRA ALEQDTADLD
     FLRLEREAFA KCPNIAIDVA VMEKTELGTV LPLDAGWSDV GSWSALWETS DRDGNGNVLQ
     GRVISEGSRN CYLRSEHRLV VGLGVENLVV VETDDAVLIA DRSRAQEIKK VVKQLEADGS
     PEGKAHRKIY RPWGHYTSVV ESSRWQVKRI SVKPGASLSL QMHHHRAEHW VVVRGTAVVE
     RDGEQQLLGE NQSTYIPLGC RHRLSNPGKI PVELIEVQSG TYLGEDDIVR FEDRYGRSDQ
     RIPVQS
//
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