ID V6KAF5_9ACTN Unreviewed; 707 AA.
AC V6KAF5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=N566_22615 {ECO:0000313|EMBL:EST29018.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST29018.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST29018.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST29018.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST29018.1}.
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DR EMBL; AWQV01000736; EST29018.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KAF5; -.
DR STRING; 1380770.N566_22615; -.
DR PATRIC; fig|1380770.3.peg.3941; -.
DR HOGENOM; CLU_019723_3_0_11; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000017915; 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 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:UP000017915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 210..319
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 366..696
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 707 AA; 74905 MW; 272FC8E5B3BB9D8D CRC64;
MARSVYVTGV ERGDGRQVVE LGVMELLTRH VDRVGVFRPL AHDGPDSIFD LLRARYRLTQ
SPATVVGLGH DEAAALQAER GTDELVARLV SRYHEVLADY EAVLVLGTDF ADTGLPAELA
LNARLANEFG AAVLPVVGGY DQTAESVVAE VRNAHHAYAS LGCEILAMVA NRVRDADARD
AARTLSAHLP VPVYVLPEEP ALSAPTVAQV RETLDAEALL GDPAGMSRDV RDFVFGGAHL
PTFLPALTEG CLVITPGDRA DLIIGSLAAH SAGSPAIAGV LLTLGEQPGP ETMALAERLA
PGTPLLAVPH GSFPTAAELF ELQGKLTAAT PRKAEVALGL FERHVDTPQL TERLSVARSA
RVTPMMFEHE LIQRARSQRR CVVLPEGTEE RVLRAAEVLL RRNVCDLTLL GEPATLRRRT
AELGIDLPLL EDDQVPETDA ATARVVDPQT SPLRERFAEL YAGLRAHRGA TYELAYDVVA
DVSYFGTLMV REGLADGMVS GAAHSTAATI RPAFEVIRTK AEAGIVSSVF FMCLSDRVLA
YGDCAVNPDP DAGQLADIAE QSAATAAQFG VEPRIAMLSY STGTSGSGAD VDKVRSATEL
LRSRRPDLLV EGPVQYDAAV DPSVAATKLP GSPVAGRATV LVFPDLNTGN NTYKAVQRSA
GAVAVGPVLQ GLRKPVNDLS RGALVSDIVN TVAITAIQAQ AGRETRG
//
