ID A0A1Q8J2N0_9BURK Unreviewed; 471 AA.
AC A0A1Q8J2N0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=BTH42_03410 {ECO:0000313|EMBL:OLL33170.1};
OS Burkholderia sp. SRS-W-2-2016.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL33170.1, ECO:0000313|Proteomes:UP000186182};
RN [1] {ECO:0000313|Proteomes:UP000186182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA Chauhan A.;
RL Submitted (DEC-2016) 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:OLL33170.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSDV01000012; OLL33170.1; -; Genomic_DNA.
DR RefSeq; WP_075296102.1; NZ_MSDV01000012.1.
DR AlphaFoldDB; A0A1Q8J2N0; -.
DR STRING; 1926878.BTH42_03410; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000186182; 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: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:OLL33170.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:OLL33170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186182};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OLL33170.1}.
FT DOMAIN 4..284
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 316..466
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 471 AA; 51669 MW; BB3C28826F5C2428 CRC64;
MLIPVILSGG AGTRLWPVSR EGYPKPFMKL ADGDSLLFKT YRRAAAATGT DAEILTVTNR
EYYFMSKDEL ALAKPAQAGA FLLEPAGRNT APAVAMAAHC IAAKHGRDAL MLVLSADHLI
QDQARFEAAV EAAVSLAQQD HLVTFGIVPS APETGFGYIE AGAPLGSGKQ VLRFVEKPNV
ETAREYIEAG NFYWNSGMFC FKAGTILDEI SRNAPDVATT VEACWASMPH DGAMLEIPSQ
SFSQVPDISI DYAVMERSDK VAVVPADFGW SDIGSWVAVR ELSTPDADNN RTTGEAIFVD
SSNTYVHSQN RMVATVGVEN LMIIDTPDAL LVAHPDKAQD VKKVVARLKK QDHEAYKLHR
TVTRPWGTYT VLEEGTRFKI KRIVVKPGAS LSLQLHHHRS EHWIVVSGMA KVVNGERDIF
VSTNESTYIP AGHKHRLENP GVLDLVMIEV QSGEYLGEDD IVRFEDIYGR Q
//
