ID A0A0C1GEC7_9FLAO Unreviewed; 697 AA.
AC A0A0C1GEC7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=OA93_09895 {ECO:0000313|EMBL:KIA98419.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA98419.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA98419.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA98419.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) 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 -!- 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:KIA98419.1}.
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DR EMBL; JSYP01000008; KIA98419.1; -; Genomic_DNA.
DR RefSeq; WP_039113024.1; NZ_JSYP01000008.1.
DR AlphaFoldDB; A0A0C1GEC7; -.
DR STRING; 1566023.OA93_09895; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000031466; 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 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:UP000031466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 215..325
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 372..691
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 697 AA; 76039 MW; 2D0FA40E01D60B39 CRC64;
MSKAVYIATS EQNSGKSIIT LGLMSMLMGK TAKVGYFRPI VEDFIDGELD NHIETVITHF
NLDIKFEDAF AITKSKLIKK KNKGKIGEVL DLIIEKYKRL EERFDFVLVE GTSFTGEGTV
IELDTNVLIA KNLGIPTIIL GSGIGKTLDE LVDNLSLVYN SFKIKEVEVL AVIANKVQIE
NVELVTSGLK KSLPESVLVN AIPVISSLNN PTVQEIVNEL DAKVLFGAAH LNNQTGHFSV
GAMQLHNYLM HLKENSLVIT PGDRADIILG ALQANESANY PTISGIVLTG NIIPEESILK
LIEGLSPIVP IISVEGGTYN ITNQIGAVKS KIYANNEHKI ETSINTFEKY VDLDSLSEKL
ITFVAEGMTP KMFQYNLVTR AKKHRKHIIL PEGSDERIII AASRLLAMDV VDISIIGDKK
QIESKVAELG ITFDFSKIKI INPIESPFYE DYANTYYELR KNKNVTITMA RDLMEDVSYF
GTMMVYKGHA DGMVSGAAHT TQHTILPALQ FIKTKPNSSV VSSVFFMCLE DRVSVFGDCA
INPNPTAEQL AEIAISSADS SAAFGIEPKI AMLSYSSGTS GKGDEVEKVR AATEIVKQKR
PDLKIEGPIQ YDAAVDRSVG KSKMPDSEVA GQASVLIFPD LNTGNNTYKA VQRETGALAI
GPMLQGLNKP VNDLSRGCTV DDIINTVVIT AIQAQGL
//
