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Database: UniProt
Entry: Q5UHD1_CITFR
LinkDB: Q5UHD1_CITFR
Original site: Q5UHD1_CITFR 
ID   Q5UHD1_CITFR            Unreviewed;       482 AA.
AC   Q5UHD1;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 57.
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:AAV34502.1};
OS   Citrobacter freundii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546 {ECO:0000313|EMBL:AAV34502.1};
RN   [1] {ECO:0000313|EMBL:AAV34502.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M1972 {ECO:0000313|EMBL:AAV34502.1};
RX   PubMed=15375135; DOI=10.1128/JB.186.19.6536-6543.2004;
RA   Samuel G., Hogbin J.P., Wang L., Reeves P.R.;
RT   "Relationships of the Escherichia coli O157, O111, and O55 O-antigen gene
RT   clusters with those of Salmonella enterica and Citrobacter freundii, which
RT   express identical O antigens.";
RL   J. Bacteriol. 186:6536-6543(2004).
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   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
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; AY730592; AAV34502.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5UHD1; -.
DR   UniPathway; UPA00126; UER00930.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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:ARBA00023134};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000313|EMBL:AAV34502.1}.
FT   DOMAIN          8..297
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          326..474
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   482 AA;  54362 MW;  44E13078BE5DD3FC CRC64;
     MSDAPLIPVI MAGGTGSRLW PLSRELYPKQ FLHLTEDNSL LQTTLLRLSS LSCKTPLVIS
     NEQHRFIVAE QLRQINQLHD NIILEPCGRN TAPAIALAAF SALKRNEKKE PLLLVLAADH
     VINESSAFCE AVKNSIPLAE DGHVVTFGII PEYAETGYGY IERGLPLEKN KSSGDSLFYH
     VNKFVEKPNR RLAEEYVSSG NHFWNSGMFL FKASTYLCEL KKYRPDIYDA CESAMSTSYH
     DLDFIRLSEE SFKGCPAESI DFAVMEKTEC CVVYPLNIGR SDVGSWQSLW NISEKTETGD
     VCKGDVLTYN TKNNYIYSDS TLVAAIGIED VVVIQTKDAI LVSKKSEVQN VKKIVDMLKH
     QNRTEHVTHR EVFRPWGKFD AIDQGDRYKV KKIIVKPGEG LSLRMHHHRS EHWIVLSGTA
     KVTLNNEIKL ITANESIYIP LGAVYSLENP GVIPLNLIEV SSGDYLGEDD MVRQKERYRN
     ED
//
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