GenomeNet

Database: UniProt
Entry: A0A139SWC8_9GAMM
LinkDB: A0A139SWC8_9GAMM
Original site: A0A139SWC8_9GAMM 
ID   A0A139SWC8_9GAMM        Unreviewed;       688 AA.
AC   A0A139SWC8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=AXE65_10840 {ECO:0000313|EMBL:KXU38936.1};
OS   Ventosimonas gracilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ventosimonadaceae; Ventosimonas.
OX   NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU38936.1, ECO:0000313|Proteomes:UP000072660};
RN   [1] {ECO:0000313|EMBL:KXU38936.1, ECO:0000313|Proteomes:UP000072660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV58 {ECO:0000313|EMBL:KXU38936.1,
RC   ECO:0000313|Proteomes:UP000072660};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:KXU38936.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LSZO01000058; KXU38936.1; -; Genomic_DNA.
DR   RefSeq; WP_068387785.1; NZ_LSZO01000058.1.
DR   AlphaFoldDB; A0A139SWC8; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000072660; 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:UP000072660};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          211..322
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          370..683
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   688 AA;  73641 MW;  511ADFC6DA3042C1 CRC64;
     MQTFFLAPTD FGVGLTSISL GLVGALERAG LRVGYLKPIA QVRREKPGPS RASELIARTH
     GLSSPQPLQR AEVEKLLADG ALDHLLEQIV SLYQEAARDK DVVIVEGMVQ NRQSSYASRV
     NFHLAKSLDA GVILVSAAED EPSSELLERI EILAQLFAGP NDPELLGLIL NKVREPAAFT
     VHHAPLLKNG GLRLLGCIPW QAELNAPRTS DVADLLGARV INAGDFHHRR MQKIVLCTRA
     VANTVHLLKP GVLIVTSGDR ADIIIAASLA AMNGVPLAGL LLCSDLPPDA RIMELCRGAL
     QAGLPVLSVQ TGAYDTATNL NRLSREIPID DRERAEKVAD FVAEYLDGDW LRARCGQPRE
     VRLSPPAFRW QLVKRAQAAG KRIVLPEGSE PRTVQAAAIC QARGIARCVL LAKREEVEAV
     ARAQGIDLPA DLEILDPDLI RENYVAPMVE LRKSKSLNAP MARAQLDDLV TLGTMMLAQD
     DVDGLVSGAA HTTANTIRPA LQLLKTAPGI ALVSSVFFML LPDQVVVYGD CAVNPDPSAE
     ELAEIALLSA ESAAAFGIEP RVAMLSYSTG HSGSGADVEK VRKATELARA ARPDLLIDGP
     LQYDAAAIAS VGQQKAPNSK VAGRATVFIF PDLNTGNTTY KAVQRSANCL SVGPMLQGLR
     KPVNDLSRGA LVDDIIYTIA LTAVQAAR
//
DBGET integrated database retrieval system