ID F9RFG3_VIBSN Unreviewed; 717 AA.
AC F9RFG3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=VIBRN418_18668 {ECO:0000313|EMBL:EGU31848.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU31848.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU31848.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU31848.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
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:EGU31848.1}.
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DR EMBL; AFWD01000069; EGU31848.1; -; Genomic_DNA.
DR RefSeq; WP_005594696.1; NZ_AFWD01000069.1.
DR AlphaFoldDB; F9RFG3; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000003627; 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 233..344
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 717 AA; 76939 MW; DDA3F16711909201 CRC64;
MSRTIMLIPT SAGVGLTSVS MGVLRTMERK GVKVSFYKPI AQPRSGGDQP DLTSTIVGAN
SDMKIGTPMQ MSVAESLIGN DNMDELLETI VERYNQINKD ADVTLIEGLV PTRKHPFANQ
VNAEIAATLG AEIVLVATPG LDNPAQLKER IEVACSNFGG TKNKNISGVI INKLNAPVDE
AGRTRPDLSE MFDDADSAQT NEMKVMEIFN TSPIRVLGCV PWSIDLIATR AIDMAQHLNA
DIINAGDINT RRIKSITFCA RSLPNMIEHF KPGSLLVTSA DRPDVIVAAA LAAMNGVEIG
AILLTGGYDI PQEIEGLCKP AFDTGLPIFK AQGNTWQTSL NLQSFSIEVP ADDKERIEFI
NDHVAGHIDG NWIESMTEGT QKSRRLSPPA FRYQLTEFAR KAGKRIVLPE GDEPRTVKAA
AICAERGIAE CVLLGNPEEI RRVAAQQGVE LGAGVTIIDS DAVRENYVAR LVELRGAKGM
TEVVAREKLQ DSVFLGTMML ENNEVDGLVS GAVHTTANTI VPPFQIIKTA PDASIVSSVF
FMLLPDQVLV YGDCAINPDP TAEQLAEIAI QSADSAAAFG IEPRVAMISY STGESGKGAD
VDKVREATKL AQEKRPDLII DGPLQYDAAI MENVAASKAP NSPVAGKATV FVFPDLNTGN
TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TVALTAIQAD QAEQANK
//
