ID Q1LAX4_CUPMC Unreviewed; 498 AA.
AC Q1LAX4;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=manC {ECO:0000313|EMBL:ABF12702.1};
GN OrderedLocusNames=Rmet_5843 {ECO:0000313|EMBL:ABF12702.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF12702.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF12702.1; -; Genomic_DNA.
DR RefSeq; WP_011518051.1; NC_007974.2.
DR AlphaFoldDB; Q1LAX4; -.
DR KEGG; rme:Rmet_5843; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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:ABF12702.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ABF12702.1}; Plasmid {ECO:0000313|EMBL:ABF12702.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABF12702.1}.
FT DOMAIN 14..314
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 343..493
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 498 AA; 54048 MW; D1A2646615175D9B CRC64;
MPVIQPVKRP VIQPVILAGG AGTRLWPLSR EQYPKQLLNL VANDTLLEAT AARLEGVAAR
TGRPAGVEAP QIVVCGEEHR FMVADMLKRK GKRARVVSEP CGRNTAPALT MAALHAMASA
GEGGDAVLVA TPADHSVTDS DAFRDAIAAA VLHAERGAIV TLGVRPTAPE TGFGYIRAAV
PVPPGGFLIE RFVEKPHLEL AQHYVDSGEY WWNCGIFVVL ASVWLKAVMQ LQPEMHARCC
AAYETGQPSE SGKDDVFRIG QEAFDTCPSD SIDYAVMEKL DGLRGIPGML VPMDAGWSDV
GSWAAIWDIA TKDNAGNAGR GRVLFDGASS CLAHSEGRLI ACVGVQDVVV VETADAVLVV
DKHHVQDVKN VVQRLRQEHG AEIVNHRKVH RPWGCYDSID HGDRFQVKRI VVEPGASLSL
QMHYHRAEHW VVVRGTARVT CGETTSILTE NQSTYIPIGT LHRLENPGKT PLEIIEVQSG
AYLGEDDIVR VEDNYGRK
//
