ID V8R955_9PSED Unreviewed; 483 AA.
AC V8R955;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=PMO01_04210 {ECO:0000313|EMBL:ETF08198.1};
OS Pseudomonas moraviensis R28-S.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395516 {ECO:0000313|EMBL:ETF08198.1};
RN [1] {ECO:0000313|EMBL:ETF08198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R28-S {ECO:0000313|EMBL:ETF08198.1};
RX PubMed=24558233;
RA Hunter S.S., Yano H., Loftie-Eaton W., Hughes J., De Gelder L.,
RA Stragier P., De Vos P., Settles M.L., Top E.M.;
RT "Draft Genome Sequence of Pseudomonas moraviensis R28-S.";
RL Genome Announc. 2:e00035-14(2014).
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:ETF08198.1}.
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DR EMBL; AYMZ01000003; ETF08198.1; -; Genomic_DNA.
DR RefSeq; WP_024011673.1; NZ_CM002330.1.
DR AlphaFoldDB; V8R955; -.
DR GeneID; 75527917; -.
DR PATRIC; fig|1395516.4.peg.860; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_6; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000024771; Chromosome.
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:ETF08198.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETF08198.1}.
FT DOMAIN 3..285
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 314..464
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 483 AA; 53843 MW; 173FEBCA901E0ED7 CRC64;
MIPVILSGGS GSRLWPLSRK QFPKQFLALT GEHTLFQQTL ERLVFEGMDT PIVVCNKEHR
FIVNEQLAAR NLECQRILME PFGRNTSPAV ALTAMMLVNE GRDELMLVLP ADHVLEDQKA
LQRALALATV AAENGEMVLF GVPATKPETG YGYIKSTADS LLPEGVSRVS HFVEKPDVKR
ATEYVESGGY YWNSGMFLFR ASRFLEELKK HDPDIYDTCL LTLERSQQDA DTITFDEATF
ACCPDNSIDY SVMEKTQRAC VVPLTAGWSD VGCWSSLWEV NEKDANGNVS KGDVVIQDSK
NCMIHGNGKL VSVIGLENIV VVETKDAMMI AHKDKVQGVK QMVNTLNAQG RSETQNHCEV
YRPWGSYDSV DMGGRFQVKH ISVKPGACLS LQMHHHRAEH WIVVSGTAEV TCDENVFLLT
ENQSTYIPIA SVHRLRNPGK IPLEIIEVQS GSYLGEDDIE RFEDIYGRST PIERGVSVKT
IAQ
//