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Database: UniProt
Entry: I4N9I0_9PSED
LinkDB: I4N9I0_9PSED
Original site: I4N9I0_9PSED 
ID   I4N9I0_9PSED            Unreviewed;       400 AA.
AC   I4N9I0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=PMM47T1_02604 {ECO:0000313|EMBL:EIK98120.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK98120.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK98120.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK98120.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA;
CC         Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174;
CC         Evidence={ECO:0000256|ARBA:ARBA00000708};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000256|ARBA:ARBA00005211}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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:EIK98120.1}.
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DR   EMBL; AJWX01000002; EIK98120.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4N9I0; -.
DR   STRING; 1179778.PMM47T1_02604; -.
DR   PATRIC; fig|1179778.3.peg.533; -.
DR   eggNOG; COG0183; Bacteria.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000004339; Unassembled WGS sequence.
DR   GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR012793; PcaF.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   NCBIfam; TIGR02430; pcaF; 1.
DR   PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          4..265
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..399
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   400 AA;  41803 MW;  611CC5282841F3DF CRC64;
     MREVFICDAI RTPIGRFGGG LSTVRADDLA AAPIKALIER NPQVDWSAVD EVFMGCANQA
     GEDNRNVARM ALLLAGLPES IPGVTLNRLC ASGMDAIGTA FRAIASGEME LAIAGGVESM
     SRAPFVMGKA DAAFSRNMKL EDTTIGWRFI NPLMKAQYGV DAMPQTADNV ADDYKVSRAD
     QDAFAVRSQQ RTAAAQAAGY FAEEIVPVRV AHKKGETIVD TDEHPRADTT LETLAKLKPV
     NGPDKTVTAG NASGVNDGAA ALILACAEAV KKHGLKPRAR VLGMASAGVA PRVMGIGPVP
     AVRKLIERLG VAVNDFDVIE LNEAFASQGL AVMRELGLAD DAPQVNPNGG AIALGHPLGM
     SGARIVMTAL HQLEKTGGKK GLATMCVGVG QGLALAIERV
//
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