ID PTA_BUCBP Reviewed; 715 AA.
AC Q89AS7;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JUL-2024, entry version 112.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=bbp_165;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 -!- SUBUNIT: Homohexamer. {ECO:0000250}.
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; AE016826; AAO26898.1; -; Genomic_DNA.
DR RefSeq; WP_011091299.1; NC_004545.1.
DR AlphaFoldDB; Q89AS7; -.
DR SMR; Q89AS7; -.
DR STRING; 224915.bbp_165; -.
DR KEGG; bab:bbp_165; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_3_0_6; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000000601; 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 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 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; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 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..715
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179124"
FT REGION 392..715
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 715 AA; 80489 MW; EC82E2C55C0DAE1C CRC64;
MTRTIMLVPI GKNIGLTTIS LSVISAMKRC KFNVKFLKSA IEYSNTNYNI DDTSLILKDT
QSLSYINPLI VDFINQFSLK QIKQRIVDYI LSKVYAKKEK YDIFLIEGFD TKSHTYVLSN
DINYYISKSI NVEIVFVCAV DRSSQLDINN IVYIINNVFK KNKNINIRGV IINELCQKVR
NDYGNVNLFD MFKSSVKKIN FGDVKYDFLF QKNGIEVLGC VPWIHKLMEP SVKILCDKYL
GANIIYDRCM NSQYIKTFII YDTNEDIKNA KKFHRSLLII PAISNDKIKE ICVQINKNKI
LISAILLTNF LNVHDKCTDF IDQLKIANCT ICSTPNDVFT VVSLLHKFNF KLDNKNYQLN
IIENDMSRHI NLDWIRSLKH SYQYNSICLP SLFIYNLKHL AKKFMKNILL PEGCELRIIK
AASICSKNDI AYCTLLGNPK KIKNIAESNN IVLNSNIEII DPKLIRKNYV ERLCHLRRHH
GITLAHANEL VKDNSILSTL ILESKKVDGL VSGSIGTTSS IILPALQLIK TSPGSSLISS
VFFMLLSDYV TLYADCAVNI NPDATQLAEI AIQSSNTARL FGIFPKVAML SYATGCSGFG
DTVDKVKEAT RIVQERSPNL IVDGPIQYDA AINRSVAKLK CPHSLVAGNA TVFIFPDLNS
GNITYKAVQR SANILSIGPI LQGINQPVND LSRGSSVQDI VYTIAVTVLQ SSLSH
//
