PIMB_MYCTO
ID PIMB_MYCTO Reviewed; 385 AA.
AC P9WMZ2; L0T936; O53522; Q7D7D7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase {ECO:0000250|UniProtKB:A0R043};
DE EC=2.4.1.346 {ECO:0000250|UniProtKB:A0R043};
DE AltName: Full=Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase {ECO:0000250|UniProtKB:A0R043};
DE AltName: Full=Alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0R043};
DE Short=Alpha-ManT {ECO:0000250|UniProtKB:A0R043};
DE AltName: Full=Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase {ECO:0000305};
DE AltName: Full=Phosphatidylinositol alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0R043};
DE Short=PI alpha-mannosyltransferase {ECO:0000250|UniProtKB:A0R043};
GN Name=pimB {ECO:0000250|UniProtKB:A0R043}; OrderedLocusNames=MT2243;
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 6 of
CC a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue
CC (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and
CC alpha-1,6-linked mannose residues (Ac1PIM2). PimB also catalyzes the
CC addition of a mannosyl residue from GDP-Man to the position 6 of
CC phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose
CC residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol
CC bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2). The
CC addition of the second mannosyl residue by PimB preferentially occurs
CC before the acylation of the mannosyl residue transferred by PimA. Also
CC able to transfer a mannosyl residue from GDP-Man to the position 6 of a
CC phosphatidyl-myo-inositol (PI), but this reaction is very slow.
CC {ECO:0000250|UniProtKB:A0R043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-
CC (1<->6)-D-myo-inositol] + GDP-alpha-D-mannose = a 2,6-O-bis(alpha-D-
CC mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + GDP + H(+);
CC Xref=Rhea:RHEA:52440, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:87673, ChEBI:CHEBI:136624;
CC EC=2.4.1.346; Evidence={ECO:0000250|UniProtKB:A0R043};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-
CC mannopyranosyl-(1<->6)-D-myo-inositol] + GDP-alpha-D-mannose = 2-O-
CC (alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-
CC myo-inositol + GDP + H(+); Xref=Rhea:RHEA:52444, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:88053,
CC ChEBI:CHEBI:136625; EC=2.4.1.346;
CC Evidence={ECO:0000250|UniProtKB:A0R043};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000250|UniProtKB:A0R043}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK46529.1; -; Genomic_DNA.
DR PIR; F70937; F70937.
DR RefSeq; WP_003411369.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMZ2; -.
DR SMR; P9WMZ2; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; AAK46529; AAK46529; MT2243.
DR KEGG; mtc:MT2243; -.
DR PATRIC; fig|83331.31.peg.2419; -.
DR HOGENOM; CLU_009583_2_5_11; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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; PF13439; Glyco_transf_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; Virulence.
FT CHAIN 1..385
FT /note="GDP-mannose-dependent alpha-(1-6)-
FT phosphatidylinositol monomannoside mannosyltransferase"
FT /id="PRO_0000427217"
FT BINDING 205
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 210
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 262
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 299
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
SQ SEQUENCE 385 AA; 41220 MW; BCFF90D320F5D4E0 CRC64;
MSRVLLVTND FPPRRGGIQS YLGEFVGRLV GSRAHAMTVY APQWKGADAF DDAARAAGYR
VVRHPSTVML PGPTVDVRMR RLIAEHDIET VWFGAAAPLA LLAPRARLAG ASRVLASTHG
HEVGWSMLPV ARSVLRRIGD GTDVVTFVSS YTRSRFASAF GPAASLEYLP PGVDTDRFRP
DPAARAELRK RYRLGERPTV VCLSRLVPRK GQDTLVTALP SIRRRVDGAA LVIVGGGPYL
ETLRKLAHDC GVADHVTFTG GVATDELPAH HALADVFAMP CRTRGAGMDV EGLGIVFLEA
SAAGVPVIAG NSGGAPETVQ HNKTGLVVDG RSVDRVADAV AELLIDRDRA VAMGAAGREW
VTAQWRWDTL AAKLADFLRG DDAAR
