ID D4ZMH8_SHEVD Unreviewed; 436 AA.
AC D4ZMH8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01618};
DE EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=ACSs {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Acyl-CoA ligase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01618};
GN Name=fadA-2 {ECO:0000313|EMBL:BAJ02877.1};
GN Synonyms=fadI {ECO:0000256|HAMAP-Rule:MF_01618};
GN OrderedLocusNames=SVI_2906 {ECO:0000313|EMBL:BAJ02877.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02877.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
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_01618}.
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_01618};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC (FadI). {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01618,
CC ECO:0000256|RuleBase:RU003557}.
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DR EMBL; AP011177; BAJ02877.1; -; Genomic_DNA.
DR RefSeq; WP_013052176.1; NC_014012.1.
DR AlphaFoldDB; D4ZMH8; -.
DR STRING; 637905.SVI_2906; -.
DR KEGG; svo:SVI_2906; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OrthoDB; 1402717at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002350; Chromosome.
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; -; 1.
DR HAMAP; MF_01618; FadI; 1.
DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; TIGR02446; FadI; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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; 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_01618};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01618};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01618};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01618};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01618}; Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01618,
KW ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 15..288
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 296..434
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 436 AA; 46795 MW; F4E47B4CE6573E28 CRC64;
MSHRQQVTNA KGDRIAIVMG LRTPFAKQAT AFHGVSALEM GKMVVNEMLS RSQIDPKEIE
QLVYGQVVQM PAAPNIAREI VLGTGMNVST DAYSVSRACA TSFQSTVNVA ESIMTGNIDI
GIAGGADSSS VLPIGVSKRL AHALVDLNKA RSFSQKLAIF RRLGLKDLLP VPPAVAEFST
GISMGQTAEQ MAKTYNISRA DQDALAHRSH TLATETWNAG HLRDEVMAAH IAPYKSFIDR
DNNIRENSTL ESYAKLRPAF DRKHGTVTAA TSTPLTDGAS AVLMMSESRA KALGYDPIGY
IKSYAFTAID VWEDMLMGPS YATPLALQRA GMELEDLTLI EMHEAFAAQT LANMQMFASK
KFAAEKLGRN RAIGEIDMSK FNVLGGSLAY GHPFAATGTR LITQVCRELK RRGGGTGLTT
ACAAGGLGAA MIVEVE
//
