ID A5L1L6_VIBBS Unreviewed; 721 AA.
AC A5L1L6;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 13-SEP-2023, 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=VSWAT3_15943 {ECO:0000313|EMBL:EDK28419.1};
OS Vibrionales bacterium (strain SWAT-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales.
OX NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK28419.1, ECO:0000313|Proteomes:UP000004912};
RN [1] {ECO:0000313|EMBL:EDK28419.1, ECO:0000313|Proteomes:UP000004912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK28419.1,
RC ECO:0000313|Proteomes:UP000004912};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (APR-2007) 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:EDK28419.1}.
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DR EMBL; AAZW01000021; EDK28419.1; -; Genomic_DNA.
DR AlphaFoldDB; A5L1L6; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000004912; 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 721 AA; 77154 MW; 37FFDC441543A630 CRC64;
MSRTIMLIPT SAGVGLTSAS MGVLRAMERK GVKVSFYKPI SQPRSGGDQP DLTSTIVGVN
SDVKIGQPLA MSVAESLIGN DNMDELLETV VERYNQINKD ADVTLIEGLV PTRKHPFANQ
VNAEIAATLG AEIVLVATPG TDNPAQLKER IVVACSNFGG TKNKNISGVI INKLNAPVDE
AGRTRPDLSE IFDDADSAQQ SELKVMEIFN TSPIRVLGCV PWSIELIATR AADMASHLNA
EIINEGELNT RRIKSITFCA RSLPHMIEHF KPGSLLVTSA DRPDVIVAAA LAAMNGVEIG
AVLLTGGYDI PAEIQDLIKP ALETGLPIFK AQGNTWQTSL NLQSFSLEVP ADDKERIEFI
NEHVAGHIDG NWIESMTEGT EKSRRLSPPA FRYQLTEFAR KAGKRIVLPE GDEPRTVKAA
AICAERGIAE CVLLGNPEEI RRVAAQQGVE LGAGVTIINS DEVRENYVAR LVELRGAKGM
TEVVAREKLQ DSVFLGTMML ENGEVDGLVS GAVHTTANTI VPPFQIIKTA PDASIVSSVF
FMLLPDQVLV YGDCAINPDP TAEQLAEIAI QSADSAAAFG IDPRVAMISY STGESGKGAD
VDKVREATKL AQEKRPDLVI DGPLQYDAAI MENVAASKAP NSPVAGKATV FVFPDLNTGN
TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TVALTAIQAD QAAQAEEKVV
N
//
