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Database: UniProt
Entry: J3I9F7_9PSED
LinkDB: J3I9F7_9PSED
Original site: J3I9F7_9PSED 
ID   J3I9F7_9PSED            Unreviewed;       497 AA.
AC   J3I9F7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EJN19361.1};
GN   ORFNames=PMI35_05812 {ECO:0000313|EMBL:EJN19361.1};
OS   Pseudomonas sp. GM78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1144337 {ECO:0000313|EMBL:EJN19361.1, ECO:0000313|Proteomes:UP000007302};
RN   [1] {ECO:0000313|EMBL:EJN19361.1, ECO:0000313|Proteomes:UP000007302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM78 {ECO:0000313|EMBL:EJN19361.1,
RC   ECO:0000313|Proteomes:UP000007302};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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:EJN19361.1}.
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DR   EMBL; AKJF01000198; EJN19361.1; -; Genomic_DNA.
DR   RefSeq; WP_008064821.1; NZ_AKJF01000198.1.
DR   AlphaFoldDB; J3I9F7; -.
DR   PATRIC; fig|1144337.3.peg.5612; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000007302; Unassembled WGS sequence.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR   Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR046433; ActCoA_hydro.
DR   InterPro; IPR003702; ActCoA_hydro_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR017821; Succinate_CoA_transferase.
DR   NCBIfam; TIGR03458; YgfH_subfam; 1.
DR   PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR   PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:EJN19361.1}.
FT   DOMAIN          13..215
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          322..463
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        288
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         378
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         382
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         402
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   497 AA;  53862 MW;  796ED874D6DDD69E CRC64;
     MYRDRIRLPS LLDKVMSAAE AAALIEDGMT VGMSGFTRAG EAKAVPHALA ERAKVTPLKI
     SLMTGASLGN DLDKQLTEAG VLSRRMPFQV DSTLRKAINA GDVMFIDQHL SETVEQLRNQ
     QLKLPDIAVI EAVAITEQGH IVPTTSVGNS ASFAIFAKHV IVEINLAHNP NLEGLHDIYI
     PTYRPTRTPI PLVKVDDRIG STAIPIPPEK IVAIVVTNQP DSPSTVLPPD VDTRAIADHL
     IDFFKQEVDA GRMTNKLGPL QAGIGTIANS VMCGLIESPF EDLTMYSEVL QDSTFDLIDA
     GKLSFASGSS ITLSSRRNAD VFGNLERYKD KLVLRPQEIS NHPEVVRRLG IIGINTALEF
     DIYGNVNSTH VCGTRMMNGI GGSGDFARNA HLAIFVTKSI AKGGAISSVV PMVSHVDHTE
     HDVDILVTEV GLADLRGLAP RERARVIIDN CVHPDYRQAL NDYFTAACAI GGHTPHILRG
     ALSWHMNLEE TGRMIAV
//
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