PTA_PSEAE
ID PTA_PSEAE Reviewed; 704 AA.
AC Q9I5A5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=PA0835;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15231792; DOI=10.1128/jb.186.14.4596-4604.2004;
RA Eschbach M., Schreiber K., Trunk K., Buer J., Jahn D., Schobert M.;
RT "Long-term anaerobic survival of the opportunistic pathogen Pseudomonas
RT aeruginosa via pyruvate fermentation.";
RL J. Bacteriol. 186:4596-4604(2004).
CC -!- FUNCTION: Involved in acetate metabolism. In combination with LdhA and
CC AckA, allows fermentation of pyruvate, enhancing long-term survival
CC under anaerobic conditions. {ECO:0000269|PubMed:15231792}.
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 Evidence={ECO:0000269|PubMed:15231792};
CC -!- ACTIVITY REGULATION: Activity is increased under anaerobic growth
CC conditions. {ECO:0000269|PubMed:15231792}.
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 -!- INDUCTION: The ackA-pta operon is induced under oxygen-limiting
CC conditions by the oxygen regulator Anr and DNA-binding integration host
CC factor. {ECO:0000269|PubMed:15231792}.
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 -!- DISRUPTION PHENOTYPE: Decreased survival under anaerobic conditions.
CC {ECO:0000269|PubMed:15231792}.
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; AE004091; AAG04224.1; -; Genomic_DNA.
DR PIR; C83541; C83541.
DR RefSeq; NP_249526.1; NC_002516.2.
DR RefSeq; WP_003114221.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; Q9I5A5; -.
DR SMR; Q9I5A5; -.
DR STRING; 287.DR97_1109; -.
DR PaxDb; Q9I5A5; -.
DR PRIDE; Q9I5A5; -.
DR EnsemblBacteria; AAG04224; AAG04224; PA0835.
DR GeneID; 882123; -.
DR KEGG; pae:PA0835; -.
DR PATRIC; fig|208964.12.peg.866; -.
DR PseudoCAP; PA0835; -.
DR HOGENOM; CLU_019723_2_1_6; -.
DR InParanoid; Q9I5A5; -.
DR OMA; FFMCLAD; -.
DR PhylomeDB; Q9I5A5; -.
DR BioCyc; PAER208964:G1FZ6-849-MON; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000002438; 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; 3.40.1390.20; -; 1.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75138; SSF75138; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..704
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000405549"
FT REGION 379..704
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 704 AA; 75697 MW; EEEF0FFDB388A88C CRC64;
MHTFFIAPTG FGVGLTSISL GLLRALERAG LKVGFFKPIA QLHPGDLGPE RSSELVARTH
GLDTPKPLPL AQVERMLGDG QLDELLEEII SLYQRAAADK DVVIVEGMVP TRHASYAARV
NFHLAKSLDA EVILVSAPEN ETLTELTDRI EIQAQLFGGP RDPKVLGVIL NKVRGEADAA
NAEDGVADFA RRLTEHSPLL RDDFRLIGCI PWQDELNAAR TRDIADLLSA RVINAGDYEQ
RRVQKIVLCA RAVPNTVQLL KPGVLVVTPG DRDDIILAAS LAAMNGVPLA GLLLCSDFPP
DPRIMELCRG ALQGGLPVLS VATGSYDTAT NLNRMNKEIP VDDRERAERV TEFVAGHIDF
EWLKQRCGTP RELRLSPPAF RYQVVQRAQK AGKRIVLPEG SEPRTVQAAA ICQARGIARC
VLLAKPEEVQ AVAQAQGIVL PEGLEIIDPD LVRQRYVEPM VELRKGKGLN APMAEQQLED
SVVLATMMLA LDEVDGLVSG AIHTTASTIR PALQLIKTAP GYNLVSSVFF MLLPDQVLVY
GDCAVNPDPS ASDLAEIAVQ SAASAQAFGI PARVAMISYS TGDSGSGVDV DKVREATRLA
REQRPDLLID GPLQYDAAAI ASVGRQKAPN SPVAGQATVF IFPDLNTGNT TYKAVQRSAD
CVSVGPMLQG LRKPVNDLSR GALVEDIVYT IALTAIQADA QAPA
