ID A0A241WFE7_9GAMM Unreviewed; 403 AA.
AC A0A241WFE7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=3-oxoadipyl-CoA thiolase {ECO:0000313|EMBL:OTG92751.1};
GN ORFNames=B9T35_11545 {ECO:0000313|EMBL:OTG92751.1};
OS Acinetobacter sp. ANC 3832.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG92751.1, ECO:0000313|Proteomes:UP000194704};
RN [1] {ECO:0000313|EMBL:OTG92751.1, ECO:0000313|Proteomes:UP000194704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG92751.1,
RC ECO:0000313|Proteomes:UP000194704};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:OTG92751.1}.
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DR EMBL; NEGJ01000008; OTG92751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241WFE7; -.
DR STRING; 1977874.B9T35_11545; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000194704; 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:UP000194704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..400
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 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 403 AA; 43317 MW; E5D9C056039F4E61 CRC64;
MEQVFIFDAI RTPIGRYAGG LSSIRTDDLA ALPIQYLKNQ HPNLPWAELD EVILGCANQA
GEDNRNVARM ASLLAGIPDS VSAITVNRLC ASGLDAVGLA ARSIKSGEAQ FVLAGGVESM
SRAPFVQSKP TTAFSRSPEI FDSTIGWRFI NPKFKASFGV DSMPETAENV AEKYQISRVD
QDLFAYRSQQ KTAVAQQNGI FAEEILSIEI KDRKKNTIMI THDEHPRADT TLDVLTALKA
PFRKEGGSVT AGNASGVNDG AACVLLGNQQ FLDRYDLKPL VKVIALASAG VEAKYMGIGP
VPAVQKVLKL TGLTLEQIDV IELNEAFAAQ SLAVIRELGL RDDDTRVNPN GGAIALGHPL
GMSGTRLVIT AMKELKRRKG KYALCTMCVG VGQGVALILE NMD
//