ID A0A241VVD2_9GAMM Unreviewed; 390 AA.
AC A0A241VVD2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01620};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01620};
DE AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01620};
GN Name=fadA {ECO:0000256|HAMAP-Rule:MF_01620};
GN ORFNames=B9T33_01140 {ECO:0000313|EMBL:OTG84426.1};
OS Acinetobacter sp. ANC 5054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977877 {ECO:0000313|EMBL:OTG84426.1, ECO:0000313|Proteomes:UP000194916};
RN [1] {ECO:0000313|EMBL:OTG84426.1, ECO:0000313|Proteomes:UP000194916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 5054 {ECO:0000313|EMBL:OTG84426.1,
RC ECO:0000313|Proteomes:UP000194916};
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 -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC shorter is formed. {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01620};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01620,
CC 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:OTG84426.1}.
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DR EMBL; NEGG01000001; OTG84426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241VVD2; -.
DR STRING; 1977877.B9T33_01140; -.
DR OrthoDB; 8951704at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000194916; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR HAMAP; MF_01620; FadA; 1.
DR InterPro; IPR012805; FadA.
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; TIGR02445; fadA; 1.
DR PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01620};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01620,
KW ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 9..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 265..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 41270 MW; FC3DC2F0168CBC4B CRC64;
MATLNPRDVV IVDGVRSAMG KTKNGMFRNV RADSLSAELV RALVARNQFD TNEVEDVIWG
CVNQTLEQGM NIGRNIALLA DLPKTVAGQT VNRLCGSSMQ AIHTAAAQIM TGQGDVFIIG
GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNGITREEQD AFGVESHRRA
WAATQEGRFK NEIVGVEGHD ANGFKILCDV DEVIRPDANI EAFQALRPVF DPKGGTVTAA
TSSALSDGAS AMLLMSAERA QALGLKPRAV IRSMAVAGCD AAIMGYGPVP ATQKALKRAG
LSIADIQTFE LNEAFAAQGL SVLKGLGIYD QQDRVNLNGG AIALGHPLGC SGARITTTLL
NVMEQQDTQI GLATMCIGLG QGIATIIERV
//
