PIMA_MYCLE
ID PIMA_MYCLE Reviewed; 374 AA.
AC O07147;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=ML0452;
GN ORFNames=MLCL581.14c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; Z96801; CAB09632.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29960.1; -; Genomic_DNA.
DR PIR; D86965; D86965.
DR RefSeq; NP_301406.1; NC_002677.1.
DR RefSeq; WP_010907730.1; NC_002677.1.
DR AlphaFoldDB; O07147; -.
DR SMR; O07147; -.
DR STRING; 272631.ML0452; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; CAC29960; CAC29960; CAC29960.
DR KEGG; mle:ML0452; -.
DR PATRIC; fig|272631.5.peg.795; -.
DR Leproma; ML0452; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_1_11; -.
DR OMA; VCPYSWD; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000000806; 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 Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Phosphatidyl-myo-inositol mannosyltransferase"
FT /id="PRO_0000080301"
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 374 AA; 40273 MW; 3B42B37D8A23C917 CRC64;
MRIGMICPYS FDVPGGVQSH VLQLAEVMRA RGQQVRVLAP ASPDVSLPEY VVSAGRAIPI
PYNGSVARLQ FSPAVHSRVR RWLVDGDFDV LHLHEPNAPS LSMWALRVAE GPIVATFHTS
TTKSLTLSVF QGVLRPWHEK IIGRIAVSDL ARRWQMEALG SDAVEIPNGV NVDSLSSAPQ
LAGYPRLGKT VLFLGRYDEP RKGMSVLLDA LPGVMECFDD VQLLIVGRGD EEQLRSQAGG
LVEHIRFLGQ VDDAGKAAAM RSADVYCAPN IGGESFGIVL VEAMAAGTPV VASDLDAFRR
VLRDGEVGHL VPAGDSAALA DALVALLRND VLRERYVAAG AEAVRRYDWS VVASQIMRVY
ETVATSGSKV QVAS
