PIMB_MYCS2
ID PIMB_MYCS2 Reviewed; 382 AA.
AC A0R043; I7GBP8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase {ECO:0000303|PubMed:19638342};
DE EC=2.4.1.346 {ECO:0000269|PubMed:19638342};
DE AltName: Full=Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase {ECO:0000303|PubMed:19638342};
DE AltName: Full=Alpha-mannosyltransferase {ECO:0000303|PubMed:19638342};
DE Short=Alpha-ManT {ECO:0000303|PubMed:19638342};
DE AltName: Full=Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase {ECO:0000305};
DE AltName: Full=Phosphatidylinositol alpha-mannosyltransferase {ECO:0000303|PubMed:19638342};
DE Short=PI alpha-mannosyltransferase {ECO:0000303|PubMed:19638342};
GN Name=pimB {ECO:0000303|PubMed:10531370};
GN OrderedLocusNames=MSMEG_4253, MSMEI_4154;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION.
RX PubMed=10531370; DOI=10.1074/jbc.274.44.31625;
RA Schaeffer M.L., Khoo K.H., Besra G.S., Chatterjee D., Brennan P.J.,
RA Belisle J.T., Inamine J.M.;
RT "The pimB gene of Mycobacterium tuberculosis encodes a mannosyltransferase
RT involved in lipoarabinomannan biosynthesis.";
RL J. Biol. Chem. 274:31625-31631(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RX PubMed=19638342; DOI=10.1074/jbc.m109.030593;
RA Guerin M.E., Kaur D., Somashekar B.S., Gibbs S., Gest P., Chatterjee D.,
RA Brennan P.J., Jackson M.;
RT "New insights into the early steps of phosphatidylinositol mannoside
RT biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium
RT smegmatis.";
RL J. Biol. Chem. 284:25687-25696(2009).
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) (PubMed:10531370,
CC PubMed:19638342). Catalyzes the addition of a mannosyl residue from
CC GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo-
CC inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate
CC phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked
CC mannose residues (Ac1PIM2) (PubMed:19638342). 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)
CC (PubMed:19638342). The addition of the second mannosyl residue by PimB
CC preferentially occurs before the acylation of the mannosyl residue
CC transferred by PimA. Also able to transfer a mannosyl residue from GDP-
CC Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this
CC reaction is very slow (PubMed:19638342). {ECO:0000269|PubMed:10531370,
CC ECO:0000269|PubMed:19638342}.
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:0000269|PubMed:19638342};
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:0000269|PubMed:19638342};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000305|PubMed:19638342}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP40611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; CP000480; ABK74170.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40611.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_888531.1; NC_008596.1.
DR AlphaFoldDB; A0R043; -.
DR SMR; A0R043; -.
DR STRING; 246196.MSMEI_4154; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PRIDE; A0R043; -.
DR EnsemblBacteria; ABK74170; ABK74170; MSMEG_4253.
DR EnsemblBacteria; AFP40611; AFP40611; MSMEI_4154.
DR KEGG; msg:MSMEI_4154; -.
DR KEGG; msm:MSMEG_4253; -.
DR PATRIC; fig|246196.19.peg.4174; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; FDAEQPF; -.
DR BRENDA; 2.4.1.346; 3512.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043750; F:phosphatidylinositol alpha-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA: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; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Virulence.
FT CHAIN 1..382
FT /note="GDP-mannose-dependent alpha-(1-6)-
FT phosphatidylinositol monomannoside mannosyltransferase"
FT /id="PRO_0000393735"
FT BINDING 200
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 205
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 257
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
FT BINDING 294
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q8NNK8"
SQ SEQUENCE 382 AA; 41407 MW; 938A199444B1BA4D CRC64;
MLLVTNDFPP RRGGIQSYLE AFVGELVRTH ELTVYAPKWK GAEEYDEKAA RSGYRVVRHP
TTLMLPEPTV ASRMKRLIGE HDIETVWFGA AAPLALLGPL ARRAGARRIV ASTHGHEVGW
SMLPVARTAL RRIGNDADVV TFVSRYTRSR FASAFGPSAA LEHLPPGVDT DRFAPDPDAR
ARMRERYGLG DRPVVVCLSR LVPRKGQDML IRALPELRRR VPDTALAIVG GGPYLETLQR
MASDLGVAEH VVFTRGIPAE ELPAHHAMAD VFAMPCRTRG AGLDVEGLGI VYLEASACGV
PVVAGRSGGA PETVLDGKTG TVVDGTDVDA ITTAVGDLLA DPRRAAAMGV AGRHWALDNW
QWRTRGARLA ELLSGRREAR QA
