ID L0WCX8_9GAMM Unreviewed; 391 AA.
AC L0WCX8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ECO:0000313|EMBL:EKF73957.1};
GN ORFNames=A11A3_11387 {ECO:0000313|EMBL:EKF73957.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF73957.1, ECO:0000313|Proteomes:UP000010164};
RN [1] {ECO:0000313|EMBL:EKF73957.1, ECO:0000313|Proteomes:UP000010164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF73957.1,
RC ECO:0000313|Proteomes:UP000010164};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(2012).
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:EKF73957.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMRJ01000017; EKF73957.1; -; Genomic_DNA.
DR RefSeq; WP_008929453.1; NZ_AMRJ01000017.1.
DR AlphaFoldDB; L0WCX8; -.
DR STRING; 1177179.A11A3_11387; -.
DR PATRIC; fig|1177179.3.peg.2274; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000010164; 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 8..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 265..390
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 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 41776 MW; 78B506CBDE9E9774 CRC64;
MSLNPNDVVI VDAVRTPMGK SRNGQFRNVR AEKLSALLVQ ALMERNPSWD TQLTEDVIWG
CVNQTKEQGM NIARNISMLA GLPRTSAAQT VNRLCGSSMQ ALHSAAQAIM TGNGDTFVIG
GVEHMGHVAM DHGVDINPEI SKVTAKASNM MGLTAEMLGK MHGISREQQD EFGVRSHRLA
WEATQQGRWK NEIVPIEGHD QEGKKILCEI DEVIRPGASL EDMQKLRPVF DPANGTVTAG
TSSALSDGAS AMLVMSAERA QALGLKPRAK IRSMAVAGCD AAIMGYGPVP ATQKALKRAG
LTIDDIDYVE LNEAFAAQSL PVMKDLKLLD KADEKVNLNG GAIALGHPLG CSGARITGTL
LNVMEWKDGQ LGLATMCIGL GQGIATVIER V
//
