ID J2K4X9_9ACTN Unreviewed; 698 AA.
AC J2K4X9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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:QTZ94180.1};
GN ORFNames=SU9_024300 {ECO:0000313|EMBL:QTZ94180.1}, SU9_07310
GN {ECO:0000313|EMBL:EJJ07535.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ07535.1};
RN [1] {ECO:0000313|EMBL:EJJ07535.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ07535.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ94180.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ94180.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000057; EJJ07535.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ94180.1; -; Genomic_DNA.
DR RefSeq; WP_006603033.1; NZ_CP072931.1.
DR AlphaFoldDB; J2K4X9; -.
DR STRING; 1160718.SU9_07310; -.
DR KEGG; sauh:SU9_024300; -.
DR PATRIC; fig|1160718.3.peg.1479; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_3_0_11; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000009036; 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 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:UP000009036};
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 367..684
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 698 AA; 74015 MW; F3C9A12FA1EABABB CRC64;
MTRSVYVTGI DRGDGRQVIE LGVMELLTRH VDRVGVFRPL VHDDGPDRLF DLLRARYRLT
QPADTVHGIG YEEAAALQAE RGTDELVSRL VDRFHAVARD YEYVLVLGSD YAATSLPDEL
NLNARLANEF GAAVLAVVGG QGQEAESVRA EAHNAYRAYH SLGCDVVAVV VNRVAPEHRA
AVVERLAARL PVPCYALPED GSLSAPTVAQ IVHTLGAEVL LGDDSGLARD ARDFVFGGAM
LPTFLKALTP GCLVVTPGDR ADLVIGSLAA HSAGAPPIAG VLLTLDERPG PDIMALAGRL
APGTPVVSVP GGSFPTAGEL FAIEGKLNAA SPRKAETALG LFERHVDTVE LTNRISVARS
GRVTPMMFEH ELIERSRSGR RRVVLPEGSE ERVLRAADVL LRRDVCALTL LGDEEAIRKR
AADLAIDLAD AQIIDPQTSA LRERFAERYA ALRAHKGVSV ELAYDVVADV SYFGTLMVEE
GLADGMVSGA VHSTAATIRP AFEIIKTRPN AQIVSSVFFM CLADRVLVYG DCAVNPDPDA
EQLADIAIQS ATTAAQFGVE PRIAMLSYST GTSGSGADVD KVRKATELVR AQRPDLLVEG
PIQYDAAVDA AVAQTKLPES DVAGKATVLI FPDLNTGNNT YKAVQRSAGA VAVGPVLQGL
RKPVNDLSRG ALVQDIVNTV AITAIQAQGE RPGAGPAA
//
