LYSAC_SALTY
ID LYSAC_SALTY Reviewed; 886 AA.
AC Q8ZMX2;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Peptidyl-lysine N-acetyltransferase Pat {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15236963, ECO:0000269|PubMed:22010215};
DE AltName: Full=Protein lysine acetyltransferase {ECO:0000305};
GN Name=pat; Synonyms=yfiQ; OrderedLocusNames=STM2651;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION IN ACETYLATION OF ACS, CATALYTIC ACTIVITY, AND GENE NAME.
RC STRAIN=LT2;
RX PubMed=15236963; DOI=10.1016/j.jmb.2004.05.010;
RA Starai V.J., Escalante-Semerena J.C.;
RT "Identification of the protein acetyltransferase (Pat) enzyme that
RT acetylates acetyl-CoA synthetase in Salmonella enterica.";
RL J. Mol. Biol. 340:1005-1012(2004).
RN [3]
RP FUNCTION.
RX PubMed=20167787; DOI=10.1126/science.1179687;
RA Wang Q., Zhang Y., Yang C., Xiong H., Lin Y., Yao J., Li H., Xie L.,
RA Zhao W., Yao Y., Ning Z.B., Zeng R., Xiong Y., Guan K.L., Zhao S.,
RA Zhao G.P.;
RT "Acetylation of metabolic enzymes coordinates carbon source utilization and
RT metabolic flux.";
RL Science 327:1004-1007(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=22010215; DOI=10.1128/mbio.00216-11;
RA Thao S., Escalante-Semerena J.C.;
RT "Biochemical and thermodynamic analyses of Salmonella enterica Pat, a
RT multidomain, multimeric N(epsilon)-lysine acetyltransferase involved in
RT carbon and energy metabolism.";
RL MBio 2:E216-E216(2011).
RN [5]
RP MUTAGENESIS OF ASP-165; ARG-170; ALA-220; ARG-450; ASP-592; ALA-780 AND
RP ALA-811.
RC STRAIN=LT2;
RX PubMed=22677774; DOI=10.1016/j.resmic.2012.05.008;
RA Thao S., Escalante-Semerena J.C.;
RT "A positive selection approach identifies residues important for folding of
RT Salmonella enterica Pat, an N(epsilon)-lysine acetyltransferase that
RT regulates central metabolism enzymes.";
RL Res. Microbiol. 163:427-435(2012).
CC -!- FUNCTION: Acetylates and inactivates the acetyl-CoA synthase (Acs). Can
CC also acetylate other central metabolic enzymes in response to
CC environmental changes. {ECO:0000269|PubMed:15236963,
CC ECO:0000269|PubMed:20167787, ECO:0000269|PubMed:22010215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:15236963, ECO:0000269|PubMed:22010215};
CC -!- ACTIVITY REGULATION: Exhibits positive cooperativity. It may be the
CC result of acetyl-CoA binding to two distinct sites, or the result of
CC subunit interactions. {ECO:0000269|PubMed:22010215}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=132 uM for Acs {ECO:0000269|PubMed:22010215};
CC Vmax=4.9 umol/min/mg enzyme toward Acs {ECO:0000269|PubMed:22010215};
CC Vmax=2.7 umol/min/mg enzyme toward acetly-CoA
CC {ECO:0000269|PubMed:22010215};
CC Note=Kinetic analysis use an approximately 15-kDa truncated C-
CC terminal construct of Acs.;
CC -!- SUBUNIT: Monomer in the absence of acetyl-CoA. Oligomerizes to a
CC tetrameric form in the presence of acetyl-CoA.
CC {ECO:0000269|PubMed:22010215}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA
CC ligase alpha subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the acetate CoA ligase
CC beta subunit family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21545.1; -; Genomic_DNA.
DR RefSeq; NP_461586.1; NC_003197.2.
DR RefSeq; WP_000082639.1; NC_003197.2.
DR AlphaFoldDB; Q8ZMX2; -.
DR SMR; Q8ZMX2; -.
DR DIP; DIP-61211N; -.
DR IntAct; Q8ZMX2; 2.
DR STRING; 99287.STM2651; -.
DR PaxDb; Q8ZMX2; -.
DR EnsemblBacteria; AAL21545; AAL21545; STM2651.
DR GeneID; 1254174; -.
DR KEGG; stm:STM2651; -.
DR PATRIC; fig|99287.12.peg.2801; -.
DR HOGENOM; CLU_007415_0_2_6; -.
DR OMA; SFMSQSG; -.
DR PhylomeDB; Q8ZMX2; -.
DR BioCyc; SENT99287:STM2651-MON; -.
DR BRENDA; 2.3.1.B34; 5542.
DR PHI-base; PHI:5571; -.
DR PHI-base; PHI:6366; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 2.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..886
FT /note="Peptidyl-lysine N-acetyltransferase Pat"
FT /id="PRO_0000430414"
FT DOMAIN 487..523
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 726..881
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 513..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MUTAGEN 165
FT /note="D->N: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 170
FT /note="R->H: Strong decrease in activity. Small decrease in
FT the helical content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 220
FT /note="A->T: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 450
FT /note="R->W: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 592
FT /note="D->N: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 780
FT /note="A->T,V: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
FT MUTAGEN 811
FT /note="A->V: Almost loss of activity. Decreases helical
FT content of the protein."
FT /evidence="ECO:0000269|PubMed:22677774"
SQ SEQUENCE 886 AA; 97767 MW; CD73A7BB6A5F5E48 CRC64;
MSQQGLEALL RPKSIAVIGA SMKPHRAGYL MMRNLLAGGF NGPVLPVTPA WKAVLGVMAW
PDIASLPFTP DLAILCTNAS RNLALLDALG AKGCKTCIIL SAPTSQHEEL LACARHYKMR
LLGPNSLGLL APWQGLNASF SPVPIKQGKL AFISQSAAVS NTILDWAQQR EMGFSYFIAL
GDSLDIDVDE LLDYLARDSK TSAILLYLEQ LSDARRFVSA ARSASRNKPI LVIKSGRSPA
AQRLLNTSAG MDPAWDAAIQ RAGLLRVQDT HELFSAVETL SHMRPLRGDR LMIISNGAAP
AALALDELWS RNGKLATLSE ETCLQLRQAL PAHIDIANPL DLCDDASSEH YVKTLDILLA
SQDFDALMVI HSPSAAAPGT ESAHALIETI KRHPRGKFVT LLTNWCGEFS SQEARRLFSE
AGLPTYRTPE GTITAFMHMV EYRRNQKQLR ETPALPSNLT SNTAEAHNLL QRAIAEGAAS
LDTHEVQPIL HAYGLHTLPT WIASDSAEAV HIAEQIGYPV ALKLRSPDIP HKSEVQGVML
YLRTASEVQQ AANAIFDRVK MAWPQARIHG LLVQSMANRA GAQELRVVVE HDPVFGPLIM
LGEGGVEWRP EEQAVVALPP LNMNLARYLV IQGIKQRKIR ARSALRPLDI VGLSQLLVQV
SNLIVDCPEI QRLDIHPLLA SASEFTALDV TLDIAPFDGD NESRLAVRPY PHQLEEWVEM
KNGDRCLFRP ILPEDEPQLR QFIAQVTKED LYYRYFSEIN EFTHEDLANM TQIDYDREMA
FVAVRRMDNA EEILGVTRAI SDPDNVDAEF AVLVRSDLKG LGLGRRLMEK LIAYTRDHGL
KRLNGITMPN NRGMVALARK LGFQVDIQLE EGIVGLTLNL AKCDES
