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Database: UniProt
Entry: A0A135WG91_9BACL
LinkDB: A0A135WG91_9BACL
Original site: A0A135WG91_9BACL 
ID   A0A135WG91_9BACL        Unreviewed;       323 AA.
AC   A0A135WG91;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528};
DE            EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE   AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108};
GN   Name=eutD {ECO:0000313|EMBL:KXH83929.1};
GN   ORFNames=AU377_04030 {ECO:0000313|EMBL:KXH83929.1};
OS   Sporosarcina sp. HYO08.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH83929.1, ECO:0000313|Proteomes:UP000070230};
RN   [1] {ECO:0000313|EMBL:KXH83929.1, ECO:0000313|Proteomes:UP000070230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYO08 {ECO:0000313|EMBL:KXH83929.1,
RC   ECO:0000313|Proteomes:UP000070230};
RA   Choi I.-G., Park W.;
RT   "Draft genome sequences of microorganisms having biocementation activity.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000705};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989}.
CC   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000256|ARBA:ARBA00005656}.
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:KXH83929.1}.
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DR   EMBL; LPUT01000012; KXH83929.1; -; Genomic_DNA.
DR   RefSeq; WP_067405363.1; NZ_LPUT01000012.1.
DR   AlphaFoldDB; A0A135WG91; -.
DR   STRING; 1759557.AU377_04030; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000070230; Unassembled WGS sequence.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   InterPro; IPR012147; P_Ac_Bu_trans.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070230};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..319
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   323 AA;  34409 MW;  EB7B4E21672111EC CRC64;
     MADLFSGIKE RLHGSKKTII LPEGNDTRVV EAASRLYQEG LVEPVLLGNE DEVRKTAAEA
     GVELTNISII NPANAPYLEE LVEKFVERRK GKVTVEQARE QLKDVNYFGT MLIFTGRADG
     LVSGAAHSTA DTVRPALQII KTKPGVSKTS GAFIMIKGDE RLVFADCAIT VAPTSQELAE
     IAVESAETAK SFGIDPKIAL LSFSTKGSAV TEETQKVADA VSIAKELAPE LHLDGEFQFD
     AAYVPEVAAK KAPGSLIQGD ANVFVFPSLE AGNIGYKLTE RLGGYEAIGP ILQGLNAPVN
     DLSRGCSADD VYKLSLITAA QSL
//
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