PTAS_METTE
ID PTAS_METTE Reviewed; 333 AA.
AC P38503;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8;
DE AltName: Full=Phosphotransacetylase;
GN Name=pta;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8226623; DOI=10.1128/jb.175.21.6822-6829.1993;
RA Latimer M.T., Ferry J.G.;
RT "Cloning, sequence analysis, and hyperexpression of the genes encoding
RT phosphotransacetylase and acetate kinase from Methanosarcina thermophila.";
RL J. Bacteriol. 175:6822-6829(1993).
RN [2]
RP MUTAGENESIS.
RX PubMed=9401029; DOI=10.1128/jb.179.24.7712-7717.1997;
RA Rasche M.E., Smith K.S., Ferry J.G.;
RT "Identification of cysteine and arginine residues essential for the
RT phosphotransacetylase from Methanosarcina thermophila.";
RL J. Bacteriol. 179:7712-7717(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=15062079; DOI=10.1016/j.str.2004.03.007;
RA Iyer P.P., Lawrence S.H., Luther K.B., Rajashankar K.R., Yennawar H.P.,
RA Ferry J.G., Schindelin H.;
RT "Crystal structure of phosphotransacetylase from the methanogenic archaeon
RT Methanosarcina thermophila.";
RL Structure 12:559-567(2004).
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: Homodimer. {ECO:0000269|PubMed:15062079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000305}.
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DR EMBL; L23147; AAA72041.1; -; Unassigned_DNA.
DR PIR; A49338; A49338.
DR PDB; 1QZT; X-ray; 2.70 A; A/B/C/D=1-333.
DR PDB; 2AF3; X-ray; 2.60 A; C/D=1-333.
DR PDB; 2AF4; X-ray; 2.15 A; C/D=1-333.
DR PDBsum; 1QZT; -.
DR PDBsum; 2AF3; -.
DR PDBsum; 2AF4; -.
DR AlphaFoldDB; P38503; -.
DR SMR; P38503; -.
DR BRENDA; 2.3.1.8; 3281.
DR SABIO-RK; P38503; -.
DR UniPathway; UPA00340; UER00459.
DR EvolutionaryTrace; P38503; -.
DR GO; GO:0005886; C:plasma membrane; 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; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR InterPro; IPR012147; P_Ac_Bu_trans.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell membrane; Direct protein sequencing;
KW Membrane; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8226623"
FT CHAIN 2..333
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179151"
FT MUTAGEN 159
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9401029"
FT MUTAGEN 159
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:9401029"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2AF4"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2AF3"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2AF3"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2AF3"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 180..198
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:2AF3"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:2AF4"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1QZT"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 292..303
FT /evidence="ECO:0007829|PDB:2AF4"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2AF4"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:2AF4"
SQ SEQUENCE 333 AA; 35220 MW; EC87B47A387B8398 CRC64;
MVTFLEKISE RAKKLNKTIA LPETEDIRTL QAAAKILERG IADIVLVGNE ADIKALAGDL
DLSKAKIVDP KTYEKKDEYI NAFYELRKHK GITLENAAEI MSDYVYFAVM MAKLGEVDGV
VSGAAHSSSD TLRPAVQIVK TAKGAALASA FFIISVPDCE YGSDGTFLFA DSGMVEMPSV
EDVANIAVIS AKTFELLVQD VPKVAMLSYS TKGSAKSKLT EATIASTKLA QELAPDIAID
GELQVDAAIV PKVAASKAPG SPVAGKANVF IFPDLNCGNI AYKIAQRLAK AEAYGPITQG
LAKPINDLSR GCSDEDIVGA VAITCVQAAA QDK
