ID A0A095YBF0_9MICC Unreviewed; 701 AA.
AC A0A095YBF0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 36.
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 ORFNames=HMPREF2128_08865 {ECO:0000313|EMBL:KGF19770.1};
OS Pseudoglutamicibacter albus DNF00011.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudoglutamicibacter.
OX NCBI_TaxID=1401063 {ECO:0000313|EMBL:KGF19770.1, ECO:0000313|Proteomes:UP000053528};
RN [1] {ECO:0000313|EMBL:KGF19770.1, ECO:0000313|Proteomes:UP000053528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00011 {ECO:0000313|EMBL:KGF19770.1,
RC ECO:0000313|Proteomes:UP000053528};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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 -!- 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}.
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:KGF19770.1}.
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DR EMBL; JRNH01000026; KGF19770.1; -; Genomic_DNA.
DR RefSeq; WP_035757316.1; NZ_JRNH01000026.1.
DR AlphaFoldDB; A0A095YBF0; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000053528; 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 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; 2.
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:UP000053528};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 212..322
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 369..684
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 701 AA; 75460 MW; C658F8ECF574F331 CRC64;
MTRGLYISAT APGAAKTIIA VGVTELLHRR ATRVGFFRPI TEADTPENDT SLQYFRANYS
LTNKNSGVGL TRSEAHELIA SGRTEEIYTR TLETYSTLAA NTDVIVIEGT DLTGHDYGSE
FELNARLANH LGSHMIGVVN GSNKTAHDVA EAVDLARDAF YDANVSLLSM IVNRANPALL
DDIRTQVRPG RSHRKVYVIP ELTDVTAPTV ENIAKATDAR LIAGTNNPER TINNTIIAGM
NVGYLLERYI ADDTFLITPS DRSDVLLAAV AASRTLDFYS TAGVLVTGPR PVDSAVLPVL
AEAPFPVYAT EQGTFTTAQT VANIHGDITD NIARKNAAVL SAWEESVDED ELLARLELPS
PDVVTPVRFL HRLITKAQQD RRTVVLPEGQ DERILRAAEI ITRRNICDLI ILGGPEVETL
AREKGINLTG VTIVDPETDP RTEEFAHEFY ELRKHKGITE HDARAKMSDK TFWATMLVHT
GGADGMVAGA VGTTADTIRP ALQIIKTREG ADIVSSVFLM CLPEKVLVYG DCAVNPNPTA
QQLASIATAS AATARQFDVD PRVAMLSYST GTSGSGEDVD RVREATELVH AQNPDFPVEG
PIQYDAAVDT SIAASKLPDS NVAGHATVLI FPDLNTGNNT YKAVQQSAGA VAVGPVLQGL
NKAVNDLSRG TTVADIVNTV AITAIQAQSL TPREHTQHQD D
//
