ACYLT_MYCTO
ID ACYLT_MYCTO Reviewed; 316 AA.
AC P9WMB4; L0TCW4; O06203; Q7D6W7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Phosphatidylinositol mannoside acyltransferase;
DE Short=PIM acyltransferase;
DE EC=2.3.1.265 {ECO:0000250|UniProtKB:A0QWG5};
GN Name=patA {ECO:0000250|UniProtKB:A0QWG5}; OrderedLocusNames=MT2686;
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: Catalyzes the transfer of a palmitoyl moiety from palmitoyl-
CC CoA to the 6-position of the mannose ring linked to the 2-position of
CC myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or
CC dimannoside (PIM2). {ECO:0000250|UniProtKB:A0QWG5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-
CC inositol + an acyl-CoA = 2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-
CC D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA;
CC Xref=Rhea:RHEA:52436, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:136624, ChEBI:CHEBI:136625; EC=2.3.1.265;
CC Evidence={ECO:0000250|UniProtKB:A0QWG5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-
CC (1<->6)-D-myo-inositol] + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-
CC phospho-[alpha-D-6-acyl-mannopyranosyl-(1<->6)-D-myo-inositol] + CoA;
CC Xref=Rhea:RHEA:47412, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:87673, ChEBI:CHEBI:88053; EC=2.3.1.265;
CC Evidence={ECO:0000250|UniProtKB:A0QWG5};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000250|UniProtKB:A0QWG5}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:A0QWG5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A0QWG5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:A0QWG5}. Note=Permanently associated with the
CC membrane. {ECO:0000250|UniProtKB:A0QWG5}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47002.1; -; Genomic_DNA.
DR PIR; B70571; B70571.
DR RefSeq; WP_003900533.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMB4; -.
DR SMR; P9WMB4; -.
DR EnsemblBacteria; AAK47002; AAK47002; MT2686.
DR KEGG; mtc:MT2686; -.
DR PATRIC; fig|83331.31.peg.2896; -.
DR HOGENOM; CLU_049421_3_0_11; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IEA:UniProt.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07984; LPLAT_LABLAT-like; 1.
DR InterPro; IPR004960; LipA_acyltrans.
DR PANTHER; PTHR30606; PTHR30606; 1.
DR Pfam; PF03279; Lip_A_acyltrans; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..316
FT /note="Phosphatidylinositol mannoside acyltransferase"
FT /id="PRO_0000427333"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0QWG5"
FT ACT_SITE 211
FT /evidence="ECO:0000250|UniProtKB:A0QWG5"
FT BINDING 137
FT /ligand="hexadecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57379"
FT /evidence="ECO:0000250|UniProtKB:A0QWG5"
FT BINDING 175
FT /ligand="hexadecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57379"
FT /evidence="ECO:0000250|UniProtKB:A0QWG5"
FT BINDING 240
FT /ligand="hexadecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57379"
FT /evidence="ECO:0000250|UniProtKB:A0QWG5"
SQ SEQUENCE 316 AA; 35160 MW; 36B814D6F5B29950 CRC64;
MIAGLKGLKL PKDPRSSVTR TATDWAYAAG WMAVRALPEF AVRNAFDTGA RYFARHGGPE
QLRKNLARVL GVPPAAVPDP LMCASLESYG RYWREVFRLP TMNHRKLARQ LDRVIGGLDH
LDAALAAGLG AVLALPHSGN WDMAGMWLVQ RHGTFTTVAE RLKPESLYQR FIDYRESLGF
EVLPLSGGER PPFEVLCERL RNNRVVCLMA ERDLTRTGVE VDFFGEPTRM PVGPAKLAVE
TGAALLPTHC WFEGRGWGFQ VYPALDCTSG DVAAITQALA DRFAQNIAAH PADWHMLQPQ
WLADLSESRR AQLRSR
