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Database: UniProt
Entry: C9P5D2_VIBME
LinkDB: C9P5D2_VIBME
Original site: C9P5D2_VIBME 
ID   C9P5D2_VIBME            Unreviewed;       714 AA.
AC   C9P5D2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=VIB_001506 {ECO:0000313|EMBL:EEX37386.1};
OS   Vibrio metschnikovii CIP 69.14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX37386.1, ECO:0000313|Proteomes:UP000005604};
RN   [1] {ECO:0000313|EMBL:EEX37386.1, ECO:0000313|Proteomes:UP000005604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX37386.1,
RC   ECO:0000313|Proteomes:UP000005604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA   Vonstein V.;
RL   Submitted (OCT-2009) 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; ACZO01000006; EEX37386.1; -; Genomic_DNA.
DR   RefSeq; WP_004395489.1; NZ_ACZO01000006.1.
DR   AlphaFoldDB; C9P5D2; -.
DR   STRING; 675813.VIB_001506; -.
DR   GeneID; 79887537; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000005604; 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:UP000005604};
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   714 AA;  76553 MW;  FA552BC6BBFFB296 CRC64;
     MSRTIMLVPI SAGVGLTSVS MGLLRAMERK GVSVSFYKPI SQPRSGGDQP DLTSTIIRHS
     SDIKIAEPMA MSAAEALIGG EKMDVLLETV VERYNQIIVD AEVTLIEGLV PTRKHPFANQ
     VNAEIAKTLG AEIVFVATPG TDNPTQLKER IEVACSNFGG TKNKNISGVV INKLNAPVDD
     AGRTRPDLSE IFDDADGAKQ ANLEVMQIFN SSPIRVLGCV PWSIDLIATR AIDMAKHLKA
     EIVNEGDINS RRIKSITFCA RSIPHMIEHF KPGSLLVTSA DRPDVIVAAA LAAMNGVEIG
     AVLLTGGYDI PKEIANLCKP AFDTGLPIFK AQGNTWQTSL NLQSFSLEVP ADDKERVEFV
     SEHVASHIDG PWIDSLTEGT QATRRLSPPA FRYQLTEFAR RANKRIVLPE GDEPRTVKAA
     AICAERGIAK CVLLGNPEEI KRVAALQGVE LGAGVEIIDA AAVRENYVAR LVELRGAKGM
     TEVVAREKLE DSVFLGTMML EANEVDGLVS GAVHTTANTI VPPFQIIKTA PNASIVSSVF
     FMLLPDQVLV YGDCAINPDP TAEQLAEIAI QSADSAAAFG IEPRVAMISY STGTSGKGAD
     VDKVREATRL AQEKRPDLII DGPLQYDAAI MENVAASKAP NSPVAGKATV FIFPDLNTGN
     TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAD QEQK
//
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