ID G9Y772_HAFAL Unreviewed; 713 AA.
AC G9Y772;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ORFNames=HMPREF0454_02445 {ECO:0000313|EMBL:EHM42081.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM42081.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM42081.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM42081.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM42081.1}.
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DR EMBL; AGCI01000059; EHM42081.1; -; Genomic_DNA.
DR AlphaFoldDB; G9Y772; -.
DR PATRIC; fig|1002364.3.peg.2197; -.
DR HOGENOM; CLU_019723_2_2_6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000005959; Unassembled WGS sequence.
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 228..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 713 AA; 76927 MW; 0E3D38E935210AB0 CRC64;
MLIPTSTSVG LTSVSLGVIR SMEQKGVRLS VFKPIAQPRT GGDSLDQTTT IIRANSSIPA
AEPLRMSHVE TLLSSNQQDV LMEEIVARYH ENTKDAEVVL VEGLVPTRKH QFANALNYEI
AKTLNAEIVF VMALGNDTAS QVKERIELAR SSFGGSKNKN ITGVIINKLN APVDDQGRTR
PDLSEIFDDS NKASVANLDT AQLVANSPLP VLGCVPWSFE LIATRAIDMA NHLKARIVNE
GDIKTRRIKS VTFCARSIPH MLEHFRPGSL LVTSADRPDV LVAACLAAMN GVEIGAILLT
GGYDMDERIA KLCERAFQTG LPVFMVDTNT WQTSLSLQSF NLEVPADDHQ RVEKLQNYVA
SHIDSKWIDS LTAASERSRR LSPPAFRYEL TELARKACKR VVLPEGDEPR TVKAAAICAE
RGIAECVLLG NPEEIQRVAA AQGVVLGKGI EIVDPNVVRE QYVPRLVELR KNKGMTEVVA
REQLEDNVVL GTLMLEQNQV DGLVSGAVHT TANTIRPPLQ LIKTAPGSSL VSSVFFMLLP
DQVLVYGDCA INPDPTAEQL SEIAIQSADS AAAFGIEPRV AMISYSTGNS GAGSDVEKVR
EATRLAQEKR PDLIIDGPLQ YDAAIMADVA KSKAPNSPVA GKATVFIFPD LNTGNTTYKA
VQRSADLVSI GPMLQGMRKP VNDLSRGALV DDIVYTVALT AIQAAQAAAA AAK
//
