ID PTA_BUCAI Reviewed; 708 AA.
AC P57273;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 27-NOV-2024, entry version 112.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=BU176;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12893.1; -; Genomic_DNA.
DR RefSeq; NP_240007.1; NC_002528.1.
DR RefSeq; WP_010895985.1; NC_002528.1.
DR AlphaFoldDB; P57273; -.
DR SMR; P57273; -.
DR STRING; 563178.BUAP5A_173; -.
DR EnsemblBacteria; BAB12893; BAB12893; BAB12893.
DR KEGG; buc:BU176; -.
DR PATRIC; fig|107806.10.peg.187; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_1_6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000001806; 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 InterPro; IPR010766; DRTGG.
DR InterPro; IPR016475; P-Actrans_bac.
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.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..708
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179122"
FT REGION 388..708
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 708 AA; 80770 MW; 1EDC4394824ED89A CRC64;
MSRIIMLIPL DKDIGLTSIG LSIIYFFYQK KIKKKSVQSI LYFSCTQNSS NSTSHVINKY
FSKIVHTVDY IDFSKVLFNS PEYSFLLNKV IDEHYNNKFL RELILIEGIK NNYCINSEEM
NYDISQNLNA EVIFIANLEN SSPEYIKNKE KKINFFLKQK KYKNILGVIF NQINSPFLEN
KYDFIKKLIV LKKIKNETKT IVPKKILKNN FFSIIACIPW NRNIVTTRVI DLFNFLNIQH
TNLVQKKNHI IEEIIIFDTH HLNLLNKHSL NTLVIVSFSR VDVFLNVLNC NVNRSKVKCI
ILTGILKLKK NIASLYKFLI KRSISIFFTE KNTIEILSQL QNFNFDISVK DITYIKKLQR
YISNFFCHSS FMFFKKKYNI NVIYPPKEFC YNLKLLSQKK NKRIKLPESY EIRILKSVAI
CSDSNIAQCV LLGDPKKIYS IANDNGINLK KNIEIIDPIS VRQEYLARFL EIRKGKNINE
FSAKKQLEDN TVLATLILES NHVDGLVSGS INTTSDTIRP ALQIIKTNPQ SLLVSSIFFM
LLPNQVLIYG DCAININPTA EELAVIAIQS ADSAKMFGIE PRIAMLSYST GCSGFGCQVE
KVKEATSIIK NRRSDLIIDG PIQYDAAVSN KVAKLKAPSS PISGSANVFI FPDLNSGNIA
YKAVQRSSRI VSIGPMLQGL RKPVNDLSRG ASVEDIIYTI ALTSIQSE
//
