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Database: UniProt
Entry: K0NK52_DESTT
LinkDB: K0NK52_DESTT
Original site: K0NK52_DESTT 
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
//
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