MDS_THEMA
ID MDS_THEMA Reviewed; 356 AA.
AC Q9WYJ4; G4FHS1; R4NYA7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=GDP-mannose:di-myo-inositol-1,3'-phosphate beta-1,2-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.361 {ECO:0000269|PubMed:19648237};
DE AltName: Full=MDIP synthase {ECO:0000303|PubMed:19648237};
GN Name=mds {ECO:0000303|PubMed:19648237};
GN OrderedLocusNames=TM_0359 {ECO:0000312|EMBL:AAD35446.1};
GN ORFNames=Tmari_0357 {ECO:0000312|EMBL:AGL49282.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=19648237; DOI=10.1128/jb.00598-09;
RA Rodrigues M.V., Borges N., Almeida C.P., Lamosa P., Santos H.;
RT "A unique beta-1,2-mannosyltransferase of Thermotoga maritima that uses di-
RT myo-inositol phosphate as the mannosyl acceptor.";
RL J. Bacteriol. 191:6105-6115(2009).
CC -!- FUNCTION: Catalyzes the transfer of the mannosyl group from GDP-mannose
CC to di-myo-inositol-1,3'-phosphate (DIP), producing mannosyl-di-myo-
CC inositol phosphate (MDIP). Can also use MDIP as an acceptor of a second
CC mannose residue, yielding di-mannosyl-di-myo-inositol phosphate
CC (MMDIP). Minor amounts of the tri-mannosylated form are also formed.
CC {ECO:0000269|PubMed:19648237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bis(myo-inositol) 1,3'-phosphate + GDP-alpha-D-mannose = 2-O-
CC (beta-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate + GDP + H(+);
CC Xref=Rhea:RHEA:59080, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:142886, ChEBI:CHEBI:142888;
CC Evidence={ECO:0000269|PubMed:19648237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(beta-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate + GDP-
CC alpha-D-mannose = 2-O-(beta-D-mannosyl-(1->2)-beta-D-mannosyl)-
CC bis(myo-inositol) 1,3'-phosphate + GDP + H(+); Xref=Rhea:RHEA:59084,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:142887, ChEBI:CHEBI:142888;
CC Evidence={ECO:0000269|PubMed:19648237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bis(myo-inositol) 1,3'-phosphate + 2 GDP-alpha-D-mannose = 2-
CC O-(beta-D-mannosyl-(1->2)-beta-D-mannosyl)-bis(myo-inositol) 1,3'-
CC phosphate + 2 GDP + 2 H(+); Xref=Rhea:RHEA:59076, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:142886,
CC ChEBI:CHEBI:142887; EC=2.4.1.361;
CC Evidence={ECO:0000269|PubMed:19648237};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19648237};
CC Note=Mg(2+) is required for maximal activity.
CC {ECO:0000269|PubMed:19648237};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 mM for DIP {ECO:0000269|PubMed:19648237};
CC KM=0.7 mM for GDP-mannose {ECO:0000269|PubMed:19648237};
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.
CC {ECO:0000269|PubMed:19648237};
CC -!- SIMILARITY: Belongs to the MDIP synthase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35446.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49282.1; -; Genomic_DNA.
DR PIR; G72386; G72386.
DR RefSeq; NP_228170.1; NC_000853.1.
DR RefSeq; WP_004083160.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYJ4; -.
DR SMR; Q9WYJ4; -.
DR STRING; 243274.THEMA_02920; -.
DR EnsemblBacteria; AAD35446; AAD35446; TM_0359.
DR EnsemblBacteria; AGL49282; AGL49282; Tmari_0357.
DR KEGG; tma:TM0359; -.
DR KEGG; tmm:Tmari_0357; -.
DR KEGG; tmw:THMA_0367; -.
DR PATRIC; fig|243274.17.peg.356; -.
DR eggNOG; COG0438; Bacteria.
DR InParanoid; Q9WYJ4; -.
DR OMA; PNTRHFE; -.
DR OrthoDB; 433560at2; -.
DR BRENDA; 2.4.1.361; 6331.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="GDP-mannose:di-myo-inositol-1,3'-phosphate beta-1,2-
FT mannosyltransferase"
FT /id="PRO_0000449821"
SQ SEQUENCE 356 AA; 41972 MW; 58B3A66B38ECDC98 CRC64;
MKIGFLSRWG ATCGVGMHAE ILAREFIRMG HEVVVFAPTE ESASKEVKYY KRTEAQDPEF
VKREIYTEVD NVTEEGWVKE EEILKENLDL LIIETFWRVP VKPLTRLIEK LKIPVISVFH
EANIFKAREV VKLPCDKIVV FDRRFYDEIL EFYEIPREKV EVISYPVMKP YDAEPERPVS
EDKFLFFSFG RQPVEEYCDF LNALKKLRKR FDNVHYWIIR SDGRVDYEAE WITQWQKRPT
VEKLYSYLKG SNVHLLPKGN TPNVVVSSTL YQIIASETPI VIRDSRFVET IETDVYGFGP
IVKYRNIHDL VHKLELLMLD RELVEDIKKE VRVFVEKYGG DKIAQEFLDL AKTITK
