PTA_VIBCH
ID PTA_VIBCH Reviewed; 714 AA.
AC Q9KT08;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=VC_1097;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}.
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 -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR EMBL; AE003852; AAF94256.1; -; Genomic_DNA.
DR PIR; H82242; H82242.
DR RefSeq; NP_230742.1; NC_002505.1.
DR RefSeq; WP_000091710.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KT08; -.
DR SMR; Q9KT08; -.
DR STRING; 243277.VC_1097; -.
DR DNASU; 2614367; -.
DR EnsemblBacteria; AAF94256; AAF94256; VC_1097.
DR GeneID; 57739774; -.
DR KEGG; vch:VC_1097; -.
DR PATRIC; fig|243277.26.peg.1047; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_1_6; -.
DR OMA; FFMCLAD; -.
DR BioCyc; VCHO:VC1097-MON; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000000584; Chromosome 1.
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; 3.40.1390.20; -; 1.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75138; SSF75138; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..714
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000405554"
FT REGION 390..714
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 714 AA; 76892 MW; 18B90F0A6D87AC80 CRC64;
MSRTIMLIPI SAGVGLTSVS MGLLRAMERK GVSVSFYKPI AQPRTGDDQP DLTSTVMSRN
SDIKIGQPMS MSAAETLIGS EKMDVLLETV VERYNQINKD AEVTLIEGLV PTRKHPFANQ
VNAEIANTLG AEIVFVATPG TDNPTQLKER IEVACSNFGG TKNKSISGVI INKLNAPVDE
AGRTRPDLSE IFDDADHAKQ ANLEVMQIFN TSPIRVLGCV PWSIDLIATR AIDMAKHLKA
EIINQGDINT RRIKSITFCA RSIPNMIEHF KPGSLLVTSA DRPDVIVAAA LAAMNGVEIG
AVLLTGGYDI PRELVSLCKP AFDTGLPIFK AQGNTWQTSL NLQSFSLEVP ADDKERIEFI
SEHVASHIDG PWVDSLTEGA QASRRLSPPA FRYQLTELAR SANKRIVLPE GDEPRTVKAA
AICAERGIAQ CVLLGNPEEI KRVAAQQGVE LGSGIEIIDP KVAQEKYVAR LVELRKSKGM
TEVVAREQLE DTVVLGTMML ERNEVDGLVS GAVHTTANTI RPPLQIIKTA PNASLVSSIF
FMLLPDQVLV YGDCAINPDP NAEQLAEIAI QSADSAAAFG IEPRVAMISY STGTSGQGAD
VDKVREATRI AKEKRPDLVI DGPLQYDAAI MENVAASKAP NSPVAGKATV FVFPDLNTGN
TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAG QEQK