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Database: UniProt
Entry: R6R9M6_9FIRM
LinkDB: R6R9M6_9FIRM
Original site: R6R9M6_9FIRM 
ID   R6R9M6_9FIRM            Unreviewed;       332 AA.
AC   R6R9M6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528};
DE            EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE   AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108};
GN   ORFNames=BN606_01723 {ECO:0000313|EMBL:CDC39666.1};
OS   Butyrivibrio sp. CAG:318.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio; environmental samples.
OX   NCBI_TaxID=1262761 {ECO:0000313|EMBL:CDC39666.1, ECO:0000313|Proteomes:UP000018075};
RN   [1] {ECO:0000313|EMBL:CDC39666.1, ECO:0000313|Proteomes:UP000018075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:318 {ECO:0000313|Proteomes:UP000018075};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000705};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989}.
CC   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000256|ARBA:ARBA00005656}.
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:CDC39666.1}.
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DR   EMBL; CBFF010000070; CDC39666.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6R9M6; -.
DR   STRING; 1262761.BN606_01723; -.
DR   Proteomes; UP000018075; Unassembled WGS sequence.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018075};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDC39666.1}.
FT   DOMAIN          3..324
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   332 AA;  35738 MW;  2285A9D4E708D7E0 CRC64;
     MAFIDVIKAK AKADKKRIVL PEGMDRRIWE AAVEIVKDDI ADLTVIATEE DVKNNTEGLN
     LAGINIIDPV RSDKLEKYTA DLAELRRMKG MTIDEARELL TTDYVYYACM MLRENEADGV
     VSGACHSTAN TLRPALQLVK AKPGVKLVSA FFIMVVPDCE YGANGTFLFA DCGLEQNPDP
     EKLAAIAVDS ANSFAKLVEE EPLVAFLSHS TKGSARHPDI DKVTSAFKIA KEMAPDVKMD
     GELQLDAAIV PEVGALKAPD SPVAGKANVL IFPDLDAGNI GYKLVHRLAK AEAYGPVTQG
     IAKPVNDLSR GCSPMDIVGV VALTSVQAQL QI
//
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