PAPA3_MYCTU
ID PAPA3_MYCTU Reviewed; 472 AA.
AC P9WIK5; F2GG06; L0T8W4; O50438; Q7D8P1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Acyltransferase PapA3 {ECO:0000305};
DE EC=2.3.1.278 {ECO:0000269|PubMed:19276083};
DE EC=2.3.1.279 {ECO:0000269|PubMed:19276083};
DE AltName: Full=Long-chain-acyl-CoA--trehalose acyltransferase {ECO:0000305};
DE AltName: Full=Mycolipenoyl-CoA--2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase {ECO:0000305};
DE AltName: Full=Polyketide synthase-associated protein A3;
GN Name=papA3; OrderedLocusNames=Rv1182;
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, CATALYTIC ACTIVITY, MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=19276083; DOI=10.1074/jbc.m809088200;
RA Hatzios S.K., Schelle M.W., Holsclaw C.M., Behrens C.R., Botyanszki Z.,
RA Lin F.L., Carlson B.L., Kumar P., Leary J.A., Bertozzi C.R.;
RT "PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:12745-12751(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 polyacyltrehalose (PAT), a
CC pentaacylated, trehalose-based glycolipid that could have a role in
CC anchoring the bacterial capsule. Catalyzes the sequential transfer of
CC two palmitoyl groups onto a single glucose residue of trehalose
CC generating the diacylated product 2,3-diacyltrehalose (trehalose
CC dipalmitate). Although palmitoyl-CoA (PCoA) seems to be the
CC physiological acyl donor, PapA3 can also use docosanoyl (22-carbon
CC saturated fatty acid) coenzyme A as acyl donor.
CC {ECO:0000269|PubMed:19276083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + alpha,alpha-trehalose = 2-O-
CC (long-chain fatty acyl)-alpha,alpha-trehalose + CoA;
CC Xref=Rhea:RHEA:58044, ChEBI:CHEBI:16551, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:142477; EC=2.3.1.279;
CC Evidence={ECO:0000269|PubMed:19276083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58045;
CC Evidence={ECO:0000269|PubMed:19276083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(long-chain fatty acyl)-alpha,alpha-trehalose + a
CC mycolipenoyl-CoA = 2-O-(long-chain fatty acyl)-3-O-mycolipenoyl-
CC trehalose + CoA; Xref=Rhea:RHEA:38459, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:142475, ChEBI:CHEBI:142476, ChEBI:CHEBI:142477;
CC EC=2.3.1.278; Evidence={ECO:0000269|PubMed:19276083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38460;
CC Evidence={ECO:0000269|PubMed:19276083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + hexadecanoyl-CoA = 2-O-hexadecanoyl-
CC alpha,alpha-trehalose + CoA; Xref=Rhea:RHEA:44052, ChEBI:CHEBI:16551,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84041;
CC Evidence={ECO:0000269|PubMed:19276083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44053;
CC Evidence={ECO:0000269|PubMed:19276083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-hexadecanoyl-alpha,alpha-trehalose + hexadecanoyl-CoA = 2-
CC O,3-O-dihexadecanoyl-alpha,alpha-trehalose + CoA;
CC Xref=Rhea:RHEA:44056, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:84041, ChEBI:CHEBI:84042;
CC Evidence={ECO:0000269|PubMed:19276083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44057;
CC Evidence={ECO:0000269|PubMed:19276083};
CC -!- MASS SPECTROMETRY: Mass=51809; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19276083};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene prevents PAT synthesis.
CC {ECO:0000269|PubMed:19276083}.
CC -!- SIMILARITY: Belongs to the PapA acyltransferase family. {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; AL123456; CCP43938.1; -; Genomic_DNA.
DR PIR; F70876; F70876.
DR RefSeq; NP_215698.1; NC_000962.3.
DR RefSeq; WP_003898759.1; NZ_NVQJ01000025.1.
DR AlphaFoldDB; P9WIK5; -.
DR SMR; P9WIK5; -.
DR STRING; 83332.Rv1182; -.
DR SwissLipids; SLP:000001028; -.
DR PaxDb; P9WIK5; -.
DR PRIDE; P9WIK5; -.
DR DNASU; 886072; -.
DR GeneID; 45425153; -.
DR GeneID; 886072; -.
DR KEGG; mtu:Rv1182; -.
DR PATRIC; fig|83332.111.peg.1322; -.
DR TubercuList; Rv1182; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; GSVTSWH; -.
DR PhylomeDB; P9WIK5; -.
DR BioCyc; MetaCyc:G185E-5351-MON; -.
DR BRENDA; 2.3.1.278; 3445.
DR BRENDA; 2.3.1.279; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:MTBBASE.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0005991; P:trehalose metabolic process; IDA:MTBBASE.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR Pfam; PF00668; Condensation; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="Acyltransferase PapA3"
FT /id="PRO_0000420764"
SQ SEQUENCE 472 AA; 51575 MW; CAA4CB55B9B7C812 CRC64;
MLRVGPLTIG TLDDWAPSTG STVSWRPSAV AHTKASQAPI SDVPVSYMQA QHIRGYCEQK
AKGLDYSRLM VVSCQQPGQC DIRAANYVIN AHLRRHDTYR SWFQYNGNGQ IIRRTIQDPA
DIEFVPVHHG ELTLPQIREI VQNTPDPLQW GCFRFGIVQG CDHFTFFASV DHVHVDAMIV
GVTLMEFHLM YAALVGGHAP LELPPAGSYD DFCRRQHTFS STLTVESPQV RAWTKFAEGT
NGSFPDFPLP LGDPSKPSDA DIVTVMMLDE EQTAQFESVC TAAGARFIGG VLACCGLAEH
ELTGTTTYYG LTPRDTRRTP ADAMTQGWFT GLIPITVPIA GSAFGDAARA AQTSFDSGVK
LAEVPYDRVV ELSSTLTMPR PNFPVVNFLD AGAAPLSVLL TAELTGTNIG VYSDGRYSYQ
LSIYVIRVEQ GTAVAVMFPD NPIARESVAR YLATLKSVFQ RVAESGQQQN VA
