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Database: UniProt
Entry: Q549S0_ECOLX
LinkDB: Q549S0_ECOLX
Original site: Q549S0_ECOLX 
ID   Q549S0_ECOLX            Unreviewed;       460 AA.
AC   Q549S0;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
DE   Flags: Fragment;
GN   Name=manC {ECO:0000313|EMBL:AAT35783.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:AAT35783.1};
RN   [1] {ECO:0000313|EMBL:AAT35783.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=O34 {ECO:0000313|EMBL:AAT35783.1};
RX   PubMed=9603891;
RA   Lai V., Wang L., Reeves P.R.;
RT   "Escherichia coli clone Sonnei (Shigella sonnei) had a chromosomal O-
RT   antigen gene cluster prior to gaining its current plasmid-borne O-antigen
RT   genes.";
RL   J. Bacteriol. 180:2983-2986(1998).
RN   [2] {ECO:0000313|EMBL:AAT35783.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=O34 {ECO:0000313|EMBL:AAT35783.1};
RA   Jensen S., Lai V., Wang L., Reeves P.R.;
RL   Submitted (MAY-2004) 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   -!- 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; AF053597; AAT35783.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q549S0; -.
DR   UniPathway; UPA00126; UER00930.
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: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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..276
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          305..455
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAT35783.1"
SQ   SEQUENCE   460 AA;  51166 MW;  8A39CCCAE8AFED2B CRC64;
     LWPLSRVLYP KQFLCLKGDL TMLQTTICRL NGVECESPVV ICNEQHRFIV AEQLRQLNKL
     TENIILEPAG RNTAPAIALA ALAAKRHSPE SDPLMLVLAA DHVIADEDAF RAAVRNAMPY
     AEAGKLVTFG IVPDLPETGY GYIRRGEVSA GEQDTVAFEV AQFVEKPNLE TAQAYVASGE
     YYWNSGMFLF RAGRYLEELK KYRPDILDAC EKAMSAVDPD LDFIRVDEEA FLACPEESVD
     YAVMERTADA VVVPMDAGWS DVGSWSSLWE ISAHTAEGNV CHGDVINHKT ENSYVYAESG
     LVTTVGVKDL VVVQTKDAVL IADRNAVQDV KKVVEQIKAD GRHEHRVHRE VYRPWGKYDS
     IDAGDRYQVK RITVKPGEGL SVQMHHHRAE HWVVVAGTAK VTIDGDIKLL GENESIYIPL
     GATHCLENPG KIPLDLIEVR SGSYLEEDDV VRFADRYGRV
//
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