PIMB_CORGL
ID PIMB_CORGL Reviewed; 381 AA.
AC Q8NNK8; Q6M3P7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase {ECO:0000303|PubMed:19395496};
DE EC=2.4.1.346 {ECO:0000305|PubMed:19395496};
DE AltName: Full=Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase {ECO:0000303|PubMed:19395496};
DE AltName: Full=Alpha-mannosyltransferase {ECO:0000303|PubMed:19395496};
DE Short=Alpha-ManT {ECO:0000303|PubMed:19395496};
DE AltName: Full=Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase {ECO:0000303|PubMed:19395496};
DE AltName: Full=Phosphatidylinositol alpha-mannosyltransferase {ECO:0000303|PubMed:19395496};
DE Short=PI alpha-mannosyltransferase {ECO:0000303|PubMed:19395496};
GN Name=pimB {ECO:0000303|PubMed:19395496}; OrderedLocusNames=Cgl2186, cg2400;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18421567; DOI=10.1007/s10482-008-9243-1;
RA Mishra A.K., Klein C., Gurcha S.S., Alderwick L.J., Babu P., Hitchen P.G.,
RA Morris H.R., Dell A., Besra G.S., Eggeling L.;
RT "Structural characterization and functional properties of a novel
RT lipomannan variant isolated from a Corynebacterium glutamicum pimB'
RT mutant.";
RL Antonie Van Leeuwenhoek 94:277-287(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18178556; DOI=10.1074/jbc.m707139200;
RA Lea-Smith D.J., Martin K.L., Pyke J.S., Tull D., McConville M.J.,
RA Coppel R.L., Crellin P.K.;
RT "Analysis of a new mannosyltransferase required for the synthesis of
RT phosphatidylinositol mannosides and lipoarbinomannan reveals two lipomannan
RT pools in corynebacterineae.";
RL J. Biol. Chem. 283:6773-6782(2008).
RN [5]
RP FUNCTION IN AC1PIM2 BIOSYNTHESIS, CATALYTIC ACTIVITY, PATHWAY, AND
RP NOMENCLATURE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP-MANNOSE, AND
RP MUTAGENESIS OF GLU-290 AND GLY-291.
RX PubMed=20843801; DOI=10.1074/jbc.m110.165407;
RA Batt S.M., Jabeen T., Mishra A.K., Veerapen N., Krumbach K., Eggeling L.,
RA Besra G.S., Futterer K.;
RT "Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside
RT synthesis: structural and mutational analysis of mannosyltransferase
RT Corynebacterium glutamicum PimB'.";
RL J. Biol. Chem. 285:37741-37752(2010).
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:18421567,
CC PubMed:18178556, PubMed:19395496). Catalyzes the addition of a mannosyl
CC residue from GDP-D-mannose (GDP-Man) to the position 6 of a
CC 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) (PubMed:18178556,
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:18178556, ECO:0000269|PubMed:18421567,
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:0000305|PubMed:19395496};
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:0000305|PubMed:19395496};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000305|PubMed:19395496}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC monoacylated phosphatidyl-myo-inositol dimannoside (Ac1PIM2) resulting
CC in the accumulation of Ac1PIM1, the absence of LAM and LM-A, and the
CC presence of LM-B. {ECO:0000269|PubMed:18178556,
CC ECO:0000269|PubMed:18421567}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; BA000036; BAB99579.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20527.1; -; Genomic_DNA.
DR RefSeq; NP_601390.1; NC_003450.3.
DR RefSeq; WP_011014943.1; NC_006958.1.
DR PDB; 3OKA; X-ray; 2.20 A; A/B=1-381.
DR PDB; 3OKC; X-ray; 2.40 A; A=1-381.
DR PDB; 3OKP; X-ray; 2.00 A; A=1-381.
DR PDBsum; 3OKA; -.
DR PDBsum; 3OKC; -.
DR PDBsum; 3OKP; -.
DR AlphaFoldDB; Q8NNK8; -.
DR SMR; Q8NNK8; -.
DR STRING; 196627.cg2400; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR KEGG; cgb:cg2400; -.
DR KEGG; cgl:Cgl2186; -.
DR PATRIC; fig|196627.13.peg.2123; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_5_11; -.
DR OMA; FDAEQPF; -.
DR BRENDA; 2.4.1.346; 960.
DR UniPathway; UPA00949; -.
DR EvolutionaryTrace; Q8NNK8; -.
DR PRO; PR:Q8NNK8; -.
DR Proteomes; UP000000582; 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 3D-structure; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..381
FT /note="GDP-mannose-dependent monoacylated alpha-(1-6)-
FT phosphatidylinositol monomannoside mannosyltransferase"
FT /id="PRO_0000393734"
FT BINDING 206
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000269|PubMed:20843801"
FT BINDING 211
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000269|PubMed:20843801"
FT BINDING 261
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000269|PubMed:20843801"
FT BINDING 298
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000269|PubMed:20843801"
FT MUTAGEN 290
FT /note="E->D: Reduces mannosyltransferase activity by more
FT than 95%, and weakens but do not abrogate binding of GDP-
FT mannose."
FT /evidence="ECO:0000269|PubMed:20843801"
FT MUTAGEN 291
FT /note="G->S: Reduces mannosyltransferase activity by more
FT than 95%."
FT /evidence="ECO:0000269|PubMed:20843801"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3OKP"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3OKP"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3OKP"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 345..362
FT /evidence="ECO:0007829|PDB:3OKP"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:3OKP"
SQ SEQUENCE 381 AA; 41328 MW; 99AECD1E156444DF CRC64;
MSASRKTLVV TNDFPPRIGG IQSYLRDFIA TQDPESIVVF ASTQNAEEAH AYDKTLDYEV
IRWPRSVMLP TPTTAHAMAE IIREREIDNV WFGAAAPLAL MAGTAKQAGA SKVIASTHGH
EVGWSMLPGS RQSLRKIGTE VDVLTYISQY TLRRFKSAFG SHPTFEHLPS GVDVKRFTPA
TPEDKSATRK KLGFTDTTPV IACNSRLVPR KGQDSLIKAM PQVIAARPDA QLLIVGSGRY
ESTLRRLATD VSQNVKFLGR LEYQDMINTL AAADIFAMPA RTRGGGLDVE GLGIVYLEAQ
ACGVPVIAGT SGGAPETVTP ATGLVVEGSD VDKLSELLIE LLDDPIRRAA MGAAGRAHVE
AEWSWEIMGE RLTNILQSEP R
