ID A0A2C6DRZ5_9GAMM Unreviewed; 716 AA.
AC A0A2C6DRZ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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_2 {ECO:0000313|EMBL:VFS52158.1};
GN ORFNames=CRN84_20780 {ECO:0000313|EMBL:PHI31594.1}, NCTC12282_05693
GN {ECO:0000313|EMBL:VFS52158.1};
OS Budvicia aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Budvicia.
OX NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI31594.1, ECO:0000313|Proteomes:UP000224974};
RN [1] {ECO:0000313|EMBL:PHI31594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI31594.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000224974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VFS52158.1, ECO:0000313|Proteomes:UP000373449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS52158.1,
RC ECO:0000313|Proteomes:UP000373449};
RG Pathogen Informatics;
RL Submitted (MAR-2019) 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}.
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DR EMBL; PDDX01000001; PHI31594.1; -; Genomic_DNA.
DR EMBL; CAADJA010000002; VFS52158.1; -; Genomic_DNA.
DR RefSeq; WP_029095822.1; NZ_PDDX01000001.1.
DR AlphaFoldDB; A0A2C6DRZ5; -.
DR STRING; 1111728.GCA_000427805_03952; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000224974; Unassembled WGS sequence.
DR Proteomes; UP000373449; 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 Reference proteome {ECO:0000313|Proteomes:UP000224974};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 233..343
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 391..706
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 716 AA; 77588 MW; 847697D6CB1A60D7 CRC64;
MSRTIMLIPT GTSVGLTSVS LGVVRAMERK GVRLGVFKPV AQSRSGGDVP DQTTSIIRAN
STVFTAEPLS MSYVENLLST NQQDVLMEAI VERYQECAKN SEVILIEGLV PTYNHQFANA
LNYEIAKTLG AEIVFVMALG TDSPAQLKER IELARSNFGG SKNENITGVI INKLNAPVDD
QGRTRPDLSE MFDDTSKAAI SVVDTAQLFT NSTLPILGCI PWNLDLIATR AIDMAHHLKA
KILNEGQIRT RRIKAITFCS RSVPNMLAHF RPGSLLVTSA DRPDVLVSAC LAAMNGVEIG
AVLLTGGYEM DERIHKLCEQ AFQTGLPVFM VETNTWQTSL SLQSFRLEAP ADDHERIESS
QDYIASHINS EWIDTLTANS EGSRRMSPPA FRYQLTELAR KAGKRVVLPE GEEPRTIKAA
AICAARGIAQ CILLGNPEEV KRVAEAQGVE LGKGIEIVDP VQVREQYVPR LVELRKSKGM
TEVVAREQLQ DNVVLGTLML EQNEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSIF
FMLLPEQVLV YGDCAINPDP TAEQLAEIAI QSADSATAFG IEPRVAMISY STGNSGTGSD
VDKVREATRI AQEKRPDLII DGPLQYDAAI MEDVARSKAP DSPVAGKATV FIFPDLNTGN
TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TVALTAIQAA QNEANS
//
