ID C4K6R2_HAMD5 Unreviewed; 709 AA.
AC C4K6R2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528, ECO:0000256|PIRNR:PIRNR006107};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707, ECO:0000256|PIRNR:PIRNR006107};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108, ECO:0000256|PIRNR:PIRNR006107};
GN Name=pta {ECO:0000313|EMBL:ACQ68255.1};
GN OrderedLocusNames=HDEF_1643 {ECO:0000313|EMBL:ACQ68255.1};
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX NCBI_TaxID=572265 {ECO:0000313|EMBL:ACQ68255.1, ECO:0000313|Proteomes:UP000002334};
RN [1] {ECO:0000313|EMBL:ACQ68255.1, ECO:0000313|Proteomes:UP000002334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT {ECO:0000313|Proteomes:UP000002334};
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
CC -!- FUNCTION: Involved in acetate metabolism.
CC {ECO:0000256|PIRNR:PIRNR006107}.
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:0000256|PIRNR:PIRNR006107};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989,
CC ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006107}.
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. {ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family.
CC {ECO:0000256|ARBA:ARBA00008756, ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000256|ARBA:ARBA00009786, ECO:0000256|PIRNR:PIRNR006107}.
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DR EMBL; CP001277; ACQ68255.1; -; Genomic_DNA.
DR RefSeq; WP_015874022.1; NC_012751.1.
DR AlphaFoldDB; C4K6R2; -.
DR STRING; 572265.HDEF_1643; -.
DR GeneID; 66261249; -.
DR KEGG; hde:HDEF_1643; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_2_6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000002334; 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 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; 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 {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR006107};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR006107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 226..337
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 384..699
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 709 AA; 77635 MW; 87BCAF5BCEEA2E2F CRC64;
MLIPIGTGIG LSSVSLGVIR SMEQKGIRLT LFKPISQSSS NKPDKTTAII RAHSNLNVGK
SLNLDYVESL LRTSQQNVLM EEILAHYHES TLDNEVVLIE GLVSIRQHQF VNMLNEQIAR
TLNAKIIFVM AMGNDSPVQL RERIELARSN FGGSKNKNIV GVIINKLNAP MDEQGRTRPD
LSDICDGSRK TNLKNIDIEH LQNHLPLPLL ACIPWHADLI AIRATDIAKH LGAQVINEGD
IQTRRIRSFN FCARSLPNML QYFRAGALLV TSADRSDVLV AACLAAMNGV EIGAILLTGG
YIIDPSVNQL CQQAFQTGLP VFKVETNTWQ TSLNLQSFSL EIPVDDHERI EKVQNYVADH
ISNQWICSLT AFSERTHRLS PPAFRYELTE RARKANKRIV LPEGDEPRTI KAAAFCAERG
IARCVLLGNP EEIHRIAAAQ GVELGQEIEI IDPVTTRENY VARLVELRKN KGMTEVVARE
QLQDNVVLGT LMLERDEVDG LVSGAVHTTA HTIRPALQLI KTAPGNSLVS SVFFMLLPDQ
VLVYGDCAIN PDPTAEQLAE IAIQSADSAA AFGIEPRVAM ISYSTGNSGT GSDVEKVREA
TMMAQKKRPD LMIDGPLQYD AAIMADVAQS KAPHSPVAGQ ATVFIFPDLN TGNTTYKAVQ
RSADLVSIGP MLQGMRKPLN DLSRGALVED IIYTIALTAI QAVSIKNGT
//
