ID A0A4Y9QT76_9BACT Unreviewed; 696 AA.
AC A0A4Y9QT76;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 18.
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=E4S40_10085 {ECO:0000313|EMBL:TFV94366.1};
OS Algoriphagus kandeliae.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Cyclobacteriaceae; Algoriphagus.
OX NCBI_TaxID=2562278 {ECO:0000313|EMBL:TFV94366.1, ECO:0000313|Proteomes:UP000297647};
RN [1] {ECO:0000313|EMBL:TFV94366.1, ECO:0000313|Proteomes:UP000297647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XY-J91 {ECO:0000313|EMBL:TFV94366.1,
RC ECO:0000313|Proteomes:UP000297647};
RA Yin Q., Wang K., Song Z.;
RT "Algoriphagus sp. nov, a new strain isolated from root system soil of
RT mangrove plant Kandelia.";
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}.
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:TFV94366.1}.
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DR EMBL; SPSB01000003; TFV94366.1; -; Genomic_DNA.
DR RefSeq; WP_135073626.1; NZ_SPSB01000003.1.
DR AlphaFoldDB; A0A4Y9QT76; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000297647; 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 FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 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; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR InterPro; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR NCBIfam; NF004167; PRK05632.1; 1.
DR NCBIfam; NF007233; PRK09653.1; 1.
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:UP000297647};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 214..326
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 371..690
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 696 AA; 76376 MW; 2084B8599AD4CA07 CRC64;
MTNAIYLTTT EPFSGKSIFA LGLMNMLASK AEKLAYFKPI ISGGKKSRDR RLELISKQFN
LTQSYEEMYA FTRKNAIKEI NKRNEAYLID SIIEKFNSLK EEADFVVVEG TDFTDVNTNV
EFDGNITVAK NLGIPAAIIL NGADRTTSEI VDLAMASANS YLTRGVQVLT LIANKVQASK
LDEVLRRLRY VLPESILVNV IPSHQQLSNP TMGEIMESLG AKLLFGKEFL TNRVDHSIVG
AMQLHNFLDR LDNNTLVVTP GDRGDILVGS LQANISRNFG KVAGVIVSGG MYPESTIVKL
IEGLETVVPV LQVEDGTFMV VTKVNQIRAR ISPNDKDKIA LAIRLFDSHV DEKALSERIT
SFNSTILTPR MFQYQIVRRA KSHKKHIVLP EGNDERILKA ADMLLRQEIV DLTILGNQDE
IRSAISKLNL SMDLDKVNIV DPASSPNFEN YAMTLYELRK NKGLSLATAR DLMHDVSYFG
TMMVYKGDAD GMVSGAIHTT QHTIRPALQF VKTKPGVNTV SSVFFMCLPN RVSVFGDCAV
VPNPTSEQLA DIAISSAESA QMFGIEPKIA MLSYSSGSSG SGEEVEKVRA ATELVKSRRP
DLKIEGPIQY DAAVDPIVGK QKLPNSEVAG QASVLIFPDL NTGNNTYKAV QRETGAIAIG
PMLQGLNKPV NDLSRGCTVI DIFNTVVITA IQAQES
//
