PIMA_MYCTO
ID PIMA_MYCTO Reviewed; 378 AA.
AC P9WMZ4; L0TD24; O06204; Q8VJF2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Phosphatidyl-myo-inositol mannosyltransferase {ECO:0000250|UniProtKB:A0QWG6};
DE EC=2.4.1.345 {ECO:0000250|UniProtKB:A0QWG6};
DE AltName: Full=Alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0QWG6};
DE AltName: Full=GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase {ECO:0000250|UniProtKB:A0QWG6};
DE AltName: Full=Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase {ECO:0000305};
DE AltName: Full=Phosphatidylinositol alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0QWG6};
DE Short=PI alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0QWG6};
GN Name=pimA {ECO:0000250|UniProtKB:A0QWG6}; OrderedLocusNames=MT2685;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the biosynthesis of phosphatidyl-myo-inositol
CC mannosides (PIM) which are early precursors in the biosynthesis of
CC lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition
CC of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of
CC the carrier lipid phosphatidyl-myo-inositol (PI) to generate a
CC phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue
CC (PIM1). {ECO:0000250|UniProtKB:A0QWG6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + GDP-
CC alpha-D-mannose = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-
CC mannopyranosyl-(1<->6)-D-myo-inositol] + GDP + H(+);
CC Xref=Rhea:RHEA:47368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58189, ChEBI:CHEBI:87673;
CC EC=2.4.1.345; Evidence={ECO:0000250|UniProtKB:A0QWG6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WMZ5};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000250|UniProtKB:A0QWG6}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0QWG6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0QWG6};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A0QWG6}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:A0QWG6}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK47001.1; -; Genomic_DNA.
DR PIR; A70571; A70571.
DR RefSeq; WP_003413478.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMZ4; -.
DR SMR; P9WMZ4; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; AAK47001; AAK47001; MT2685.
DR GeneID; 45426613; -.
DR KEGG; mtc:MT2685; -.
DR PATRIC; fig|83331.31.peg.2895; -.
DR HOGENOM; CLU_009583_2_1_11; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-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; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase; Virulence.
FT CHAIN 1..378
FT /note="Phosphatidyl-myo-inositol mannosyltransferase"
FT /id="PRO_0000427216"
FT BINDING 9
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 16
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 18
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 62..63
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 68
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 196
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 201..202
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 251..253
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 256
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 274..278
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 282
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT SITE 118
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
SQ SEQUENCE 378 AA; 40445 MW; 637B8E8467717F1A CRC64;
MRIGMICPYS FDVPGGVQSH VLQLAEVMRT RGHLVSVLAP ASPHAALPDY FVSGGRAVPI
PYNGSVARLR FGPATHRKVK KWLAHGDFDV LHLHEPNAPS LSMLALNIAE GPIVATFHTS
TTKSLTLTVF QGILRPMHEK IVGRIAVSDL ARRWQMEALG SDAVEIPNGV DVDSFASAAR
LDGYPRQGKT VLFLGRYDEP RKGMAVLLDA LPKVVQRFPD VQLLIVGHGD ADQLRGQAGR
LAAHLRFLGQ VDDAGKASAM RSADVYCAPN TGGESFGIVL VEAMAAGTAV VASDLDAFRR
VLRDGEVGHL VPVDPPDLQA AALADGLIAV LENDVLRERY VAAGNAAVRR YDWSVVASQI
MRVYETVAGS GAKVQVAS
