ID Q1MPN9_LAWIP Unreviewed; 471 AA.
AC Q1MPN9;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=xanB {ECO:0000313|EMBL:CAJ55038.1};
GN OrderedLocusNames=LI0984 {ECO:0000313|EMBL:CAJ55038.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ55038.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ55038.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ55038.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ55038.1; -; Genomic_DNA.
DR RefSeq; WP_011527067.1; NC_008011.1.
DR AlphaFoldDB; Q1MPN9; -.
DR STRING; 363253.LI0984; -.
DR KEGG; lip:LI0984; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_7; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000002430; Chromosome.
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: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 Isomerase {ECO:0000313|EMBL:CAJ55038.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..284
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 315..465
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 471 AA; 52590 MW; 9BEF91168B326CA4 CRC64;
MNNIYPIILC GGSGTRLWPL SREYYPKQFI NFGSGTLFEN TLSCIASLRN VQNPIVVCNE
EHRFFVSKLL QQQNRVATII LEPEGKNTAP AIALGVSAVS ELESDPLILV LPSDHLIGSN
SIFHSAVMSG ISVAIEGHFV TFGVNPTGPE SGFGYLQYGQ EVSDGIFKIL NFTEKPSKAR
AKEFLALGNY AWNSGIFLFR ASTYLNELEL LAPQIFSACK QGWDERTQDP LGFFRPNSQK
FLQSPSGSID YVIMEKTEKL YMVKLETNWS DLGSWESFYN AEVHDSMGNV VSGDVIAQDT
ENCYLNSTQR LVCALGVKNI IVVETADAVL VVDRNQTQNV KNLLEQLRIS GRTESETHMR
VFRPWGSYET LFSSTGYKVK KITVSPGATL SLQLHQYRAE HWIVVYGIAN VTINKAEHIV
KVNQSIYIPV GVEHRLANYG EEPLEVIEVQ SGSYVGEDDI IRLEDVYGRT E
//
