ID A0A0R0CT36_9GAMM Unreviewed; 469 AA.
AC A0A0R0CT36;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=cpsB {ECO:0000313|EMBL:KRG69618.1};
GN ORFNames=ABB29_09105 {ECO:0000313|EMBL:KRG69618.1};
OS Pseudoxanthomonas dokdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG69618.1, ECO:0000313|Proteomes:UP000052052};
RN [1] {ECO:0000313|EMBL:KRG69618.1, ECO:0000313|Proteomes:UP000052052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG69618.1,
RC ECO:0000313|Proteomes:UP000052052};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG69618.1}.
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DR EMBL; LDJL01000009; KRG69618.1; -; Genomic_DNA.
DR RefSeq; WP_057658318.1; NZ_LDJL01000009.1.
DR AlphaFoldDB; A0A0R0CT36; -.
DR STRING; 344882.ABB29_09105; -.
DR PATRIC; fig|344882.3.peg.3179; -.
DR OrthoDB; 9806359at2; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000052052; Unassembled WGS sequence.
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 ECO:0000313|EMBL:KRG69618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRG69618.1}.
FT DOMAIN 6..284
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 312..462
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 469 AA; 51385 MW; 7EBAFE161B5A2CE4 CRC64;
MSPLLPVILS GGSGTRLWPL SREAYPKQFL PLVGDDTMLQ ATWKRVSGIA GLAPIVVANE
EHRFMAAEQL RECSVKPLAL ILEPMGRNTA PAITVAALQA LKSNEDAILL VLPSDHVIRD
EAAFHAAVEV AARAAEEGKL VTFGIKPASP EVGYGYIKAD GNTGAMPVEE FVEKPDLQTA
RMYLESGNYY WNSGMFLFKA SRYLAEVEKL QPAILSACRE ALDKAQADTD FVRLDPDAFA
NSPNDSIDYA IMEKTDAATV VPMDAGWSDV GSWSALWEIS DKDATGNAHH GDVIEVDCHD
TYAYGSKLIA MVGLNDVVVV ETDDAVMVGH RDRIQEVKEV VARIKRDGRS EASAHRKVYR
PWGAYDSIDN GDRFQVKRIT VKPGASLSLQ MHHHRAEHWI VVSGTAKVTR GDESILLTEN
QSTYIPLGVT HRLDNPGKLP LELIEVQSGS YLGEDDIVRF DDVYGRVGS
//