ID F4MZJ8_YEREN Unreviewed; 712 AA.
AC F4MZJ8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:CBX71256.1};
GN ORFNames=YEW_FQ24200 {ECO:0000313|EMBL:CBX71256.1};
OS Yersinia enterocolitica W22703.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX71256.1};
RN [1] {ECO:0000313|EMBL:CBX71256.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21453472; DOI=10.1186/1471-2164-12-168;
RA Fuchs T.M., Brandt K., Starke M., Rattei T.;
RT "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype 2,
RT serotype O:9): genomic evidence for oscillation between invertebrates and
RT mammals.";
RL BMC Genomics 12:168-168(2011).
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; FR718577; CBX71256.1; -; Genomic_DNA.
DR AlphaFoldDB; F4MZJ8; -.
DR UniPathway; UPA00340; UER00459.
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 229..338
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 386..701
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 712 AA; 76842 MW; 0868B03ED79C9EBC CRC64;
MLIPTGTSVG LTSVSLGVIR SMEQKGVRLS VFKPIAQPRA GNDAPDQTTT IIRANSSITA
AEPLNMNHVE NLLSSNQQDV LMEEIVARYH ENTKDAEVVL VEGLVPTRKH QFANALNYEI
AKTLNAEIVF VIALGNDSPD QLKERIELAR SSFGGSKNKN ITGVIINKLN APVDEQGRTR
PDLSEIFDDS TKASVASIDP KQLFANSPLP VLGCVPWSFE LIATRAIDMC KHLNARIINE
GDIRTRRVKS VTFCARSIPH MLEHFRPGSL LVTSADRPDV LVSACLAAMN GVEIGAILLT
GGYAIDEPIK KLCDRAFQTG LPVFMVDTNT WQTSLSLQSF NLEVPADDHE RVEKLQNYVA
SHINSEWIDS LSATSERSRR LSPPAFRYEL TELARKAGKR IVLPEGDEPR TVKAAAICAE
RGIATCVLLG NPEEIQRVAA AQGVELGKGV EIIDPVAVRE QYVPRLVELR KSKGMTEVVA
REQLEDNVVL GTLMLEKGEV DGLVSGAVHT TANTIRPPLQ LIKTAPGSSL VSSVFFMLLP
DQVLVYGDCA INPDPTAEQL SEIAIQSADS AAAFGIEPRV AMISYSTGNS GAGSDVEKVR
EATRLAQEKR PDLIIDGPLQ YDAAIMADVA KSKAPNSPVA GKATVFIFPD LNTGNTTYKA
VQRSADLISI GPMLQGMRKP VNDLSRGALV DDIVYTVALT AIQSAQADAS AS
//
