ID H2INY2_RAHAC Unreviewed; 437 AA.
AC H2INY2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=fadI {ECO:0000256|HAMAP-Rule:MF_01618};
GN OrderedLocusNames=Rahaq2_1280 {ECO:0000313|EMBL:AEX51161.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX51161.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX51161.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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_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; CP003244; AEX51161.1; -; Genomic_DNA.
DR RefSeq; WP_015696408.1; NZ_JMPO01000007.1.
DR AlphaFoldDB; H2INY2; -.
DR STRING; 745277.Rahaq2_1280; -.
DR GeneID; 61511381; -.
DR KEGG; raq:Rahaq2_1280; -.
DR PATRIC; fig|745277.3.peg.1214; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OrthoDB; 8951704at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009010; 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; 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; 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; 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_01618};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01618};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01618};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01618}; Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01618};
KW Reference proteome {ECO:0000313|Proteomes:UP000009010};
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 437 AA; 46781 MW; CC94DF42A03CCF87 CRC64;
MNKVVPLVTR EGDRIAIVDG LRTPFAKQAT AYHGIPAVDL GKIVVSELLA KSGIDPKHID
QLVFGQVVQM PEAPNIAREI VLGTGMHVST DAYSVSRACA TSFQAVANVA ESIMSGMVHV
GIAGGADSSS VLPIGVSKRL ARALVDVSKA RTLSQRLSIF SKLKLRDLLP VPPAVAEYST
GLRMGDTAEQ MAKSHHISRA QQDELAHRSH TLAAQAWEQG YLTSQVMATQ VPPYREVLQK
DNNIRLNSEI SQYAKLRPAF DRKHGTVTAA TSTPLTDGAA AVLMMSESRA RELGLEPLGY
LKSFAFAAID VWEDMLLGPA YATPLALDRA GLTLGDLDLI DMHEAFAAQT LANINMLASE
EFAREKLGRS QAVGEIDWDK FNVLGGSLAY GHPFAATGAR MITQTLHELR RRGGKYGLTT
ACAAGGLGAA MILEAAQ
//
