PIMB_MYCTU
ID PIMB_MYCTU Reviewed; 385 AA.
AC P9WMZ3; 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 38.
DE RecName: Full=GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase {ECO:0000303|PubMed:19395496};
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:0000303|PubMed:19395496}; OrderedLocusNames=Rv2188c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN AC1PIM2 BIOSYNTHESIS, PATHWAY, AND NOMENCLATURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19395496; DOI=10.1128/jb.01729-08;
RA Mishra A.K., Batt S., Krumbach K., Eggeling L., Besra G.S.;
RT "Characterization of the Corynebacterium glutamicum deltapimB' deltamgtA
RT double deletion mutant and the role of Mycobacterium tuberculosis
RT orthologues Rv2188c and Rv0557 in glycolipid biosynthesis.";
RL J. Bacteriol. 191:4465-4472(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:19395496).
CC Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-
CC Man) to the position 6 of a phosphatidyl-myo-inositol bearing an alpha-
CC 1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol
CC bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2)
CC (PubMed:19395496). PimB also catalyzes the addition of a mannosyl
CC residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol
CC bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to
CC generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and
CC alpha-1,6-linked mannose residues (Ac1PIM2) (By similarity). The
CC addition of the second mannosyl residue by PimB preferentially occurs
CC before the acylation of the mannosyl residue transferred by PimA (By
CC similarity). Also able to transfer a mannosyl residue from GDP-Man to
CC the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction
CC is very slow (By similarity). {ECO:0000250|UniProtKB:A0R043,
CC ECO:0000269|PubMed:19395496}.
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:0000305|PubMed:19395496}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44965.1; -; Genomic_DNA.
DR PIR; F70937; F70937.
DR RefSeq; NP_216704.2; NC_000962.3.
DR RefSeq; WP_003411369.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; P9WMZ3; -.
DR SMR; P9WMZ3; -.
DR STRING; 83332.Rv2188c; -.
DR PaxDb; P9WMZ3; -.
DR DNASU; 887278; -.
DR GeneID; 887278; -.
DR KEGG; mtu:Rv2188c; -.
DR TubercuList; Rv2188c; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; FDAEQPF; -.
DR PhylomeDB; P9WMZ3; -.
DR BRENDA; 2.4.1.346; 3445.
DR BRENDA; 2.4.1.B74; 3445.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000030; F:mannosyltransferase activity; IDA:MTBBASE.
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..385
FT /note="GDP-mannose-dependent alpha-(1-6)-
FT phosphatidylinositol monomannoside mannosyltransferase"
FT /id="PRO_0000393733"
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
