MDS_AQUAE
ID MDS_AQUAE Reviewed; 356 AA.
AC O67214;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=GDP-mannose:di-myo-inositol-1,3'-phosphate beta-1,2-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.361 {ECO:0000250|UniProtKB:Q9WYJ4};
DE AltName: Full=MDIP synthase {ECO:0000303|PubMed:19648237};
GN Name=mds {ECO:0000303|PubMed:19648237};
GN OrderedLocusNames=aq_1141 {ECO:0000312|EMBL:AAC07179.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=VF5;
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) (PubMed:19648237). Can also use MDIP as an
CC acceptor of a second mannose residue, yielding di-mannosyl-di-myo-
CC inositol phosphate (MMDIP) (By similarity).
CC {ECO:0000250|UniProtKB:Q9WYJ4, 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:0000250|UniProtKB:Q9WYJ4};
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:0000250|UniProtKB:Q9WYJ4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9WYJ4};
CC -!- SIMILARITY: Belongs to the MDIP synthase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07179.1; -; Genomic_DNA.
DR PIR; C70398; C70398.
DR RefSeq; NP_213778.1; NC_000918.1.
DR RefSeq; WP_010880716.1; NC_000918.1.
DR AlphaFoldDB; O67214; -.
DR STRING; 224324.aq_1141; -.
DR EnsemblBacteria; AAC07179; AAC07179; aq_1141.
DR KEGG; aae:aq_1141; -.
DR PATRIC; fig|224324.8.peg.889; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_778299_0_0_0; -.
DR InParanoid; O67214; -.
DR OMA; PNTRHFE; -.
DR OrthoDB; 433560at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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_0000449820"
SQ SEQUENCE 356 AA; 41994 MW; D9DFF77F4288B7D7 CRC64;
MNVGIFSRWN ATCGVSLHAE MIGRELLRRG YPITVFAPYL ESASRWWHHK LIRPDEEYVV
RCYEELSPDG KEGKIDIEKV LEREIDFLIV ESYEKLPYKD VEKLVKILKD KGIPSIAIIH
EGDYEDIRYT DMNIFEKVCV FDERYVKEVL KDRVSEEKVE IIPYPCYPVR EGSREFAEDG
VIKFFSFGRQ PKEEYCPYIE GLKVFKRDFP NVKYRIVRAM EPLKIFEDFV EQEERILDYE
EIVKELHSAD FHLLPKGNTK RVVVSSTLYQ VLGTLTLTVV PDNRFFETLP HGEEAPVIFY
RDVLELVKEL KKASADEEYR KKIRENASKF VEENSVERIT DRFENLINSI LVKNVH
