ID A2W030_9BURK Unreviewed; 550 AA.
AC A2W030;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=BCPG_03685 {ECO:0000313|EMBL:EAY65326.1};
OS Burkholderia cenocepacia PC184.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY65326.1, ECO:0000313|Proteomes:UP000053735};
RN [1] {ECO:0000313|EMBL:EAY65326.1, ECO:0000313|Proteomes:UP000053735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC184 {ECO:0000313|EMBL:EAY65326.1,
RC ECO:0000313|Proteomes:UP000053735};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., White J.,
RA Larson L., Alvarado L., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA LiPuma J., Lory S.;
RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184).";
RL Submitted (DEC-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; CH482378; EAY65326.1; -; Genomic_DNA.
DR AlphaFoldDB; A2W030; -.
DR HOGENOM; CLU_035527_1_0_4; -.
DR Proteomes; UP000053735; 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:EAY65326.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EAY65326.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAY65326.1}.
FT DOMAIN 70..366
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 395..545
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 550 AA; 59611 MW; 75A5B209A9A219AC CRC64;
MRGGYPPLGP VLLSIYFMLQ RQALTSTVES VIMNAPAVVA ETRHSSSAAP AAGTPAAGMP
AVGTRLAVQP VILAGGSGTR LWPMSRERFP KQLIGLLGDH SLLQSTALRL DGLTADYPLN
DDVLIVCGED HRFTTAEQLR LTARNATIML EPLGRDTAPA LTLAALRLVA NGNDAVMTVM
PADHAVADLP RFHAAVAAGV HCAAQGKIAT MGIVPKHAET GYGYIRVGAP LGDAGTGTLD
VRRLDRFVEK PHLELAQQYV ASGEYWWNSG IFIVRASVWL NAIRQLEPAI YAACEQAVAQ
GKEDGDFFRV DRDAFAASPS NSIDYAVMEP LASQPQLCES VVVPLDAGWS DVGSWDAIWQ
ISPKDESGNV GRGHVLFEGA DSTFAHSESR LVACVGTQNL VVVETPDAVL VADKSRVQDV
KKIVGHIKAR QGTEATDHRK VHRPWGHYDS VDTGERFQVK RIVVKPGAQL SLQMHHHRAE
HWIVVRGTAR ITRGDETFLL SENESTYIPL GVSHRLENPG KMPLELIEVQ SGAYLGEDDI
VRFDDTYGRQ
//
