ID PTA_MYCTO Reviewed; 690 AA.
AC P9WHP0; L0T5A1; P96254;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-NOV-2024, entry version 45.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=MT0421;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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: Involved in acetate metabolism. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal region seems to be important for proper
CC quaternary structure. The C-terminal region contains the substrate-
CC binding site (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK44645.1; -; Genomic_DNA.
DR PIR; F70628; F70628.
DR RefSeq; WP_003898439.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WHP0; -.
DR SMR; P9WHP0; -.
DR KEGG; mtc:MT0421; -.
DR PATRIC; fig|83331.31.peg.450; -.
DR HOGENOM; CLU_019723_3_0_11; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR016475; P-Actrans_bac.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR InterPro; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR NCBIfam; TIGR00651; pta; 1.
DR PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..690
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000428151"
FT REGION 365..690
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 690 AA; 72949 MW; C01C412AF2810CCE CRC64;
MADSSAIYLA APESQTGKST IALGLLHRLT AMVAKVGVFR PITRLSAERD YILELLLAHT
SAGLPYERCV GVTYQQLHAD RDDAIAEIVD SYHAMADECD AVVVVGSDYT DVTSPTELSV
NGRIAVNLGA PVLLTVRAKD RTPDQVASVV EVCLAELDTQ RAHTAAVVAN RCELSAIPAV
TDALRRFTPP SYVVPEEPLL SAPTVAELTQ AVNGAVVSGD VALREREVMG VLAAGMTADH
VLERLTDGMA VITPGDRSDV VLAVASAHAA EGFPSLSCIV LNGGFQLHPA IAALVSGLRL
RLPVIATALG TYDTASAAAS ARGLVTATSQ RKIDTALELM DRHVDVAGLL AQLTIPIPTV
TTPQMFTYRL LQQARSDLMR IVLPEGDDDR ILKSAGRLLQ RGIVDLTILG DEAKVRLRAA
ELGVDLDGAT VIEPCASELH DQFADQYAQL RKAKGITVEH AREIMNDATY FGTMLVHNCH
ADGMVSGAAH TTAHTVRPAL EIIKTVPGIS TVSSIFLMCL PDRVLAYGDC AIIPNPTVEQ
LADIAICSAR TAAQFGIEPR VAMLSYSTGD SGKGADVDKV RAATELVRAR EPQLPVEGPI
QYDAAVEPSV AATKLRDSPV AGRATVLIFP DLNTGNNTYK AVQRSAGAIA IGPVLQGLRK
PVNDLSRGAL VDDIVNTVAI TAIQAQGVHE
//
