ID A0A2C6ZD78_9PROT Unreviewed; 477 AA.
AC A0A2C6ZD78;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=CR162_03690 {ECO:0000313|EMBL:PHK96441.1};
OS Pseudoroseomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1335062 {ECO:0000313|EMBL:PHK96441.1, ECO:0000313|Proteomes:UP000223527};
RN [1] {ECO:0000313|EMBL:PHK96441.1, ECO:0000313|Proteomes:UP000223527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YW11 {ECO:0000313|EMBL:PHK96441.1,
RC ECO:0000313|Proteomes:UP000223527};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) 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}.
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:PHK96441.1}.
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DR EMBL; PDNU01000003; PHK96441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6ZD78; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000223527; Unassembled WGS sequence.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000313|EMBL:PHK96441.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:PHK96441.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PHK96441.1}.
FT DOMAIN 11..293
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 322..472
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
FT COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 477 AA; 51817 MW; 10F7FEF928080A9F CRC64;
MADTGQQRIV PVVLCGGTGS RLWPLSREGF PKQFWPLLSQ HSMLQETANR AVGPSFASLL
VIANQDHRFL VAEQLREARI ENPRIVLEPT ARNSAPAIAA AALLAHEEDT QSVLWLMPAD
AAIADTAAMH AALGKAAEAA RAGRIVTFGM KPTAPETGYG YIEAGEPLEG LEGVAAVARF
VEKPDAGTAA RFLAGGQHLW NSGMFVATAA TLLAELERLA PDLLAAVRGA VEGATRDLDF
IRLDPAAFAR APDISIDYAV MEKTSHAAVV PADIGWSDVG SWAALWEVSS KDAAGNATQG
PVELYQARNC YVRTEGILTG VVGLEDAVVV VTDDAVLAMH RDRAQDVKKL LEQLKAANRK
EATEHRRMYR PWGHYEGLIK GDRFQVKKIS VKPGAKLSLQ KHFHRAEHWV VVAGTAIVER
DAERIMLREN ESIYLPLGCV HRMENPGMIP LTLIEVQSGS YLGEDDIVRF EDTYGRA
//
