ID   PIMC_MYCTA              Reviewed;         381 AA.
AC   A5U3B9; Q7D807; Q9RLP4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol dimannoside mannosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase;
DE   AltName: Full=Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase;
DE   AltName: Full=Phosphatidylinositol alpha-mannosyltransferase;
DE            Short=PI alpha-mannosyltransferase;
GN   Name=pimC; OrderedLocusNames=MRA_1768.2; ORFNames=MRA_1768B;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RX   PubMed=10531227; DOI=10.1128/iai.67.11.5768-5774.1999;
RA   Brosch R., Philipp W., Stavropoulos E., Colston M.J., Cole S.T.,
RA   Gordon S.V.;
RT   "Genomic analysis reveals variation between Mycobacterium tuberculosis
RT   H37Rv and the attenuated M. tuberculosis H37Ra.";
RL   Infect. Immun. 67:5768-5774(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: Catalyzes the addition of a mannose residue from GDP-D-
CC       mannose to the position 6 of the alpha-1,6-linked mannose residue of
CC       the triacyl phosphatidylinositol dimannoside (Ac3PIM2) to generate
CC       triacyl phosphatidylinositol trimannoside (Ac3PIM3). {ECO:0000250}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ242907; CAB60070.1; -; Genomic_DNA.
DR   EMBL; CP000611; ABQ73519.1; -; Genomic_DNA.
DR   RefSeq; WP_003899004.1; NC_009525.1.
DR   AlphaFoldDB; A5U3B9; -.
DR   SMR; A5U3B9; -.
DR   STRING; 419947.MRA_1768B; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ABQ73519; ABQ73519; MRA_1768B.
DR   GeneID; 45425730; -.
DR   KEGG; mra:MRA_1768B; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_009583_10_1_11; -.
DR   OMA; VVCTTEF; -.
DR   UniPathway; UPA00949; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0043750; F:phosphatidylinositol alpha-mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13579; Glyco_trans_4_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT   CHAIN           1..381
FT                   /note="GDP-mannose-dependent alpha-(1-6)-
FT                   phosphatidylinositol dimannoside mannosyltransferase"
FT                   /id="PRO_0000393737"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            283
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  41289 MW;  58205FC1AE8AE5EE CRC64;
     MRVVQVANFY GPRSGGLRTA VDRLGAEYCA SGHEVFLIVP GARTERHLLR TGVVRITLPA
     KHIPYTGGYR AVMPGAVRTV LETLRPDALE VSDRLTLRSL GRWGREHGVT TVMISHERLD
     RFAGQLLPRR AAQKFADFAN ARTAANYDTV VCTTGFAREE FDRIGATNTV TVPLGVDLKT
     FHPRRRCARV RQHWATPTQI LLVHCGRLSV EKHADRSIDA LAALCDAGVD ARLVIAGEGP
     LRARLERKAT GLPIDFTGFI SDRHAVAGLL ASADVALAPG PHETFGLAAL ESLACGTPAV
     VSRTSALTEI ITADSGACAD NRPEAIAHAV RTIVSRPERH RRRCARRRAE IFTWQRAAAS
     MLATLGAMAV STRCGDTQDT A