PIMA_PROFC
ID PIMA_PROFC Reviewed; 381 AA.
AC D7GDZ9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Phosphatidyl-myo-inositol mannosyltransferase {ECO:0000303|PubMed:4295288};
DE EC=2.4.1.345 {ECO:0000305|PubMed:4295288};
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};
DE AltName: Full=Phosphatidylmyoinositol monomannoside {ECO:0000303|PubMed:4295288};
GN Name=pimA {ECO:0000250|UniProtKB:A0QWG6};
GN OrderedLocusNames=PFREUD_12400 {ECO:0000312|EMBL:CBL56760.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=754252;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4295288; DOI=10.1016/0006-291x(68)90714-6;
RA Brennan P., Ballou C.E.;
RT "Phosphatidylmyoinositol monomannoside in Propionibacterium shermanii.";
RL Biochem. Biophys. Res. Commun. 30:69-75(1968).
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:0000305|PubMed:4295288}.
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:0000305|PubMed:4295288};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WMZ5};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000305}.
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; FN806773; CBL56760.1; -; Genomic_DNA.
DR RefSeq; WP_013161134.1; NC_014215.1.
DR AlphaFoldDB; D7GDZ9; -.
DR SMR; D7GDZ9; -.
DR STRING; 754252.PFREUD_12400; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; CBL56760; CBL56760; PFREUD_12400.
DR GeneID; 61222097; -.
DR KEGG; pfr:PFREUD_12400; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_1_11; -.
DR OMA; VCPYSWD; -.
DR OrthoDB; 948440at2; -.
DR BioCyc; PFRE754252:PFREUD_RS06005-MON; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000000936; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043750; F:phosphatidylinositol alpha-mannosyltransferase activity; NAS: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; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Phosphatidyl-myo-inositol mannosyltransferase"
FT /id="PRO_0000438239"
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 69..70
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 75
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 204
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
FT BINDING 209..210
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 125
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:A0QWG6"
SQ SEQUENCE 381 AA; 40987 MW; 2014F501EA445324 CRC64;
MRVGLVCPYS FARPGGVQNH VLGLGGWLKE QGHDVSIIAP GQASRSLLAE TGLVPSEFVS
AGRAVPVTFN GSVARINFGV GPALKVKKWL DQGNFDVVHL HEPIAPTICL LALYLTDRPV
TATFHTATPE LTAIRFANRV LPRMVSRIDA AIAVSSEAAD VAHHYSGVNP VVIGNGIHLA
DYPLVRATSR WRGGEHPLIT FLGRYDEPRK GFEVLTAALP LVRATYPDLE VVVIGSGTAR
SVEGVRFLGG LDDEERNAWL GRSDIYIAPQ TGRESFGIVL LEAMACGAPV VAANLRAFLD
VLTDDEGLVG HTFRVGNSAS ASRAMLRSLS EPRDLRLERG RALAANYDWS VIGPQVVAMY
TVAGQNYATS RGIKNRELKG H
