ID K0NK52_DESTT Unreviewed; 473 AA.
AC K0NK52;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:CCK80283.1};
GN OrderedLocusNames=TOL2_C21220 {ECO:0000313|EMBL:CCK80283.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80283.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK80283.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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; FO203503; CCK80283.1; -; Genomic_DNA.
DR RefSeq; WP_014957595.1; NC_018645.1.
DR AlphaFoldDB; K0NK52; -.
DR STRING; 651182.TOL2_C21220; -.
DR KEGG; dto:TOL2_C21220; -.
DR PATRIC; fig|651182.5.peg.2518; -.
DR HOGENOM; CLU_035527_1_0_7; -.
DR OMA; LIVCNEK; -.
DR OrthoDB; 9806359at2; -.
DR Proteomes; UP000007347; Chromosome.
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; 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:ARBA00023134};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CCK80283.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000313|EMBL:CCK80283.1}.
FT DOMAIN 4..287
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 473 AA; 53013 MW; 844D523984F509C6 CRC64;
MIIPVILAGG SGTRLWPLSR ELYPKQLINI YNEHTMLQNT VLRLEGLEML GSPIVVCNEE
HRFMTAEQLR NIEIEPNAII LEPVGRNTAP AIALAALKAM ENSDDPILLV LPADHVIEKI
ADFHAAIKAG LEYAKKDNLI TFGIIPDSPE TGYGYIKKGA VLETDTGAAT IEKFVEKPDL
DTARKYLKSG SYCWNSGMFM FRASAIIKEL EAHAPDIMMP CKEVISTGVQ DLDFFRLSLD
GFKNIESESI DYAVMEKTFK GIVIPFEAGW NDLGSFDALW QTGKKDEDLN VIKGDVLTHD
VKESYIKSES SLIAAVGIEK FVIVETKDAI LVSPRDRVQD VKKIVKQLKD HNREESVTHR
KVYRPWGSYE TIDIEARFQV KRITVKPGAK LSLQKHFHRA EHWTVVSGSA IVTKGKKQIL
LKEDESTYIS LGTAHRLENP GKIPLELIEV QSGSYLGEDD IVRFDDVYGR KES
//