ID A0A1A8TL05_9GAMM Unreviewed; 706 AA.
AC A0A1A8TL05;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 Name=pta {ECO:0000313|EMBL:SBS34537.1};
GN ORFNames=MSP8886_03096 {ECO:0000313|EMBL:SBS34537.1};
OS Marinomonas spartinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1792290 {ECO:0000313|EMBL:SBS34537.1, ECO:0000313|Proteomes:UP000092544};
RN [1] {ECO:0000313|EMBL:SBS34537.1, ECO:0000313|Proteomes:UP000092544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8886 {ECO:0000313|EMBL:SBS34537.1,
RC ECO:0000313|Proteomes:UP000092544};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; FLOB01000008; SBS34537.1; -; Genomic_DNA.
DR RefSeq; WP_067018012.1; NZ_FLOB01000008.1.
DR AlphaFoldDB; A0A1A8TL05; -.
DR STRING; 1792290.MSP8886_03096; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000092544; 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 Reference proteome {ECO:0000313|Proteomes:UP000092544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 218..328
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 375..690
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 706 AA; 75958 MW; E5AE06B01E36C06F CRC64;
MSTNVLMTVP TGPGVGLTSV SVGLVRALEQ QGLKASFFKP IAQPHPGDSG PDKSTAMVAQ
GSTLSPAEPI PLHEAERYLY NDNIEELMEE VVGRFQASVE PDSTVIVEGL AQIPGHPYAT
RLNKAIARTL DAGLVLVTAP NNMRVNELEH HVEIAAGSYG GIKAPDVIGC ILNKTIPGSL
GVKSYGDLFA QRAIFKRNFS LLGQIPVSDE LTYPRVKDVA DFLEAKIVNA GDIETRRVQS
YTLCARGVEN MLEALKPGVL VFTPGDRTDI IMATAIAALN DTKIAALVLT GGYQPSEALM
TLCGKAMAKG LPVLSVDSNS WETAITMQSF NQEIPLDDKE RILTVKEHIA RCIDHDWINS
FAMNQDERKL SPPAFRYRLI EQARSLNKRI ILPEGEEIRT IQAASICAER GIARCTLLGN
EAEIIRIAQN NGVELSHGVE ILDPSSIRER YVAPMVELRK HRGLTDIVAR EQLEDNVVLG
TMMLQTNDVD GLVSGAIHTT ANTIRPALQL VKTSPNASLV SSVFFMCLPD QVLVYGDCAI
NPDPTAEQLA EIAIQSADSA TAFGIAPKVA MISYSTGGSG SGNDVDKVRE ATAIAQQRRP
DLLIDGPLQY DAAIMEKVAK QKAPDSRVAG KATVFIFPDL NTGNTTYKAV QRSAEVVSIG
PMLQGIRKPV NDLSRGALVD DIVYTIAITA IQAGQAEVLA AKANKP
//
