PTA_HAEIN
ID PTA_HAEIN Reviewed; 711 AA.
AC P45107;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=HI_1203;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22857.1; -; Genomic_DNA.
DR PIR; B64169; B64169.
DR RefSeq; NP_439359.1; NC_000907.1.
DR RefSeq; WP_005694242.1; NC_000907.1.
DR AlphaFoldDB; P45107; -.
DR SMR; P45107; -.
DR STRING; 71421.HI_1203; -.
DR DNASU; 950151; -.
DR EnsemblBacteria; AAC22857; AAC22857; HI_1203.
DR KEGG; hin:HI_1203; -.
DR PATRIC; fig|71421.8.peg.1255; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_1_6; -.
DR OMA; FFMCLAD; -.
DR PhylomeDB; P45107; -.
DR BioCyc; HINF71421:G1GJ1-1234-MON; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000000579; Chromosome.
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..711
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179130"
FT REGION 390..711
FT /note="Phosphate acetyltransferase"
SQ SEQUENCE 711 AA; 76517 MW; 4C684C943E2870CB CRC64;
MSRTIILIPV STGVGLTSIS LGLIHSLEQK GTKVAFMKPV SQPSTGEDKL DRTTSIIRTS
TSLETAEPFM LSVAESLIGQ NQSDVLLEKI VANHQQLTKN NDIVVVEGLI PTRKHGYANS
INYEIAQALD AEIVLVAAPA TETPTELKDR VEAAASLFGG KNNPNLLGVV VNKFNAPVDE
SGRTRPDLAE IFDSFQHNHI SETEVNKLFA GSAIKLLACV PWNANLIATR AIDLVKHLGA
SIINEGEINR RIRGITFCAR SLPNMVEHFR AGSLLVASAD RPDVLVAAAL AASNGIEIGG
ILLTGGYKID AQINKLCRPT FEKAKLPIFR IEGNTWQTAL SLQSFNLEVP VDDKERIENI
KQYISQHFNA DFINNLVADS SRLPRLSPPA FRFQLTELAR AAKKRIVLPE GDEPRTIKAA
VLCAERGIAE CVLLADPASV QRVAEAQGVK LGKGITIINP ADVRENYVDR LVELRKAKGM
TETAAREQLE DTVVLGTMML EANEVDGLVS GAVHTTANTI RPPMQIIKTA PGSSIVSSIF
FMLLPDQVLV YGDCAVNPDP TAEQLAEIAI QSADSAKAFG IDPKVAMISY STGTSGSGAD
VEKVKEATRI AKEKRPDLLI DGPLQYDAAV MEDVARSKAP NSPVAGKATV FVFPDLNTGN
TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAT Q