ID B1B4K4_ECOLX Unreviewed; 485 AA.
AC B1B4K4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:BAG11843.1};
OS Escherichia coli O55:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=244320 {ECO:0000313|EMBL:BAG11843.1};
RN [1] {ECO:0000313|EMBL:BAG11901.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WC416 {ECO:0000313|EMBL:BAG11901.1};
RA Iguchi A., Ooka T., Ogura Y., Asadulghani, Nakayama K., Frankel G.,
RA Hayashi T.;
RT "Genomic comparison of the O-antigen biosynthesis gene clusters of
RT Escherichia coli O55 strains belonging to three distinct lineages.";
RL Microbiology (Mosc.) 154:559-570(2008).
RN [2] {ECO:0000313|EMBL:BAG11843.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TB182A {ECO:0000313|EMBL:BAG11843.1};
RA Leopold S.R., Magrini V.J., Holt N.J., Shaikh N., Mardis E.R., Cagno J.R.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "The Emergence and Radiations of a Pathogen: High Resolution, Pan-
RT Chromosomal Analysis of the Evolution of Escherichia coli O157:H7 and
RT O157:H-.";
RL Submitted (AUG-2008) 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; AB453015; BAG11843.1; -; Genomic_DNA.
DR EMBL; AB353132; BAG11901.1; -; Genomic_DNA.
DR RefSeq; WP_001281069.1; NZ_CP039837.1.
DR OMA; VTHINYR; -.
DR UniPathway; UPA00126; UER00930.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; 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, ECO:0000313|EMBL:BAG11843.1}.
FT DOMAIN 8..295
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 485 AA; 54622 MW; 9FBC6480358C9443 CRC64;
MSDKSFIAVV MAGGTGSRLW PLSRELYPKQ FLKIGGELSL LQSTLNRLSK LSFDAPLVIT
NDNHRFIVAE QLRQMNQLSG NIILEPCGKN TAPAIALAAF SALKRDKNKD PILLVLAADH
IIKNEEAFCE AIKSAMFMAE EDKIVTFGII PTYAETGYGY INIGARVESN IEVDNAHFYV
AKKFVEKPER ELAEKYFSSK KYLWNSGMFM FKASVFLSEL KKYRPDIFEV CEEAISASSK
DLDFIRLPER MFEKCPSESI DFAVMENTKR CVVCPVDIGW SDVGSWQSLW ELSDKSPSGD
VCKGDTLTYN TKNNYIYSDS ALVAAVGVEN IVIVQTKDAV LVANKSEVQD VKKIVDLLKK
NNRTEHVTHR EVFRPWGKFD SIDQGDRYTV KKIVVKPGEG LSLRMHHHRS EHWIVLSGTA
KVILEGTEKL ITVNESIYIP LGASYSLENP GVIPLILIEV SSGDYLGEDD IVRQKERYKK
KINHE
//
