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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//