ID A0A0F7FZM6_9ACTN Unreviewed; 723 AA.
AC A0A0F7FZM6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=SXIM_42350 {ECO:0000313|EMBL:AKG45619.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45619.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) 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}.
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DR EMBL; CP009922; AKG45619.1; -; Genomic_DNA.
DR RefSeq; WP_030733689.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7FZM6; -.
DR STRING; 408015.SXIM_42350; -.
DR KEGG; sxi:SXIM_42350; -.
DR PATRIC; fig|408015.6.peg.4289; -.
DR HOGENOM; CLU_019723_3_0_11; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000034034; Chromosome.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 209..320
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 366..702
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 723 AA; 76901 MW; 74CF2B04F4E74A1F CRC64;
MTRSVYVTGI GRGDGRQVIE LGVMELLTRQ VDRVGVFRPL AHPGPDPVFE LLRGRYRLSQ
TREDARGMEY AEAAALQAEQ GMDELVTALV ERYHNVARDY EAVLVLGTDY ADTQLPAELT
LNARLANEFG SVVLPVVAGL DQSAESVVAE VRNAHHAFTS LGCEVIATIA NRVRDSHAAA
AARELGTHLP EPVYVLPEEP ALSAPTVTQI AEALDAEVLL GDRTGLARDV RDFVIGGAML
PTFLTALREA SLVVTPGDRA DLVVGALAAH SAGAPPIAGV LLTLGERPGA ETMALAARLA
PGTPVLSVPG GTFHTAAALS GLEGKLTAAT PRKAEIALGL FETHVDTAQL TERLSVVRSE
RVTPMMFEHE LIERSRTGRR HVVLPEGTEE RVLRAAEVLL RRNVCDLTLL GEEGAVRKRA
ADLGIDLRLH GAAEPVDIDP GATATACVAR VVDPQTSPLR ERFAELYAKL RAHKGVTYEL
AWDVVCDVSY FGTLMVQEGL ADGMVSGAVH STAATIRPAF EVIKTKPDAA IVSSVFFMCL
ADKVLVYGDC AVNPDPNAEQ LADIAIQSAT TAAQFGVEPR IAMLSYSTGT SGSGADVDKV
RAATELVRER RPDLLVEGPI QYDAAVEPSV AATKLPGSEV AGQATVLVFP DLNTGNNTYK
AVQRSAGAVA VGPVLQGLRK PVNDLSRGAL VQDIVNTVAI TAIQAQRQNP HHPQQRHQQK
VNS
//
