ID PTA_DEIGD Reviewed; 703 AA.
AC Q1J2D0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 27-NOV-2024, entry version 95.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=Dgeo_0051;
OS Deinococcus geothermalis (strain DSM 11300 / CIP 105573 / AG-3a).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / CIP 105573 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000359; ABF44354.1; -; Genomic_DNA.
DR RefSeq; WP_011529201.1; NC_008025.1.
DR AlphaFoldDB; Q1J2D0; -.
DR SMR; Q1J2D0; -.
DR STRING; 319795.Dgeo_0051; -.
DR KEGG; dge:Dgeo_0051; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_1_0; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000002431; 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 CDD; cd03109; DTBS; 1.
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; Transferase.
FT CHAIN 1..703
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000405545"
FT REGION 377..703
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 703 AA; 74708 MW; B27D3B9DC99BD169 CRC64;
MKTLFIAPTR NGVGLTSTAL GLLRALERQG LKVAFLKPIA QTHEAAPDDS VHWARTLAHA
VTPDPILLSV AEEQLSQGQE EELMENVVAL AREAAAGVTG GADVLVVEGL ALNERNVYAG
PLNASLARNL EADVVLVSSL AGVTPATLAD ELEIAAQAYR RSDGSGLAGY VLNFAPLELD
FGGLLADLRA RSRILASGEL PLLGVIAQSP TLAAPRTLDV ARHLGAEVLN EGEARLRRVT
STVVTARSVP KMADLFTSGA LVVTPGDRED VVMAAALSHL SGVPLAGLLF TSGSTPEAAI
ERLCRAALTS TLPVLRVETN SYNTASRLSR MEARVPHDDL ERMERTLDFI ADRLDTVPLG
TRLRAPEGSE RRLPPSAFRY ELIQKARAAN KRIVLPEGDE PRTVRAAIRC VEKGIARCVL
LAQPEKVRQV AEGQGLTLPD GLEIIDPDRV RANYVAPMVE LRKHKGLTAP QAEAQLEDNV
VLGTMMLALD EVDGLVSGAV HTTANTVRPA LQLIKTAPGV RLVSSIFFML MPEQVVVYGD
AAINPNPNAE ELADIAIQSA DSARAFGIPP RIAMLSYSTG ESGAGADVEK VRIATRLVRE
RRPDLPVDGP LQYDAASVLS VGRQKAPNSP VAGRATVFIF PDLNTGNTTY KAVQRAAGVV
AVGPMLQGLR KPVNDLSRGA LVDDIVYTIA LTAIQATQAR EGA
//
