(data stored in ACNUC7421 zone)

HOGENOM: IDLOI1_1_PE10

ID   IDLOI1_1_PE10                        STANDARD;      PRT;   387 AA.
AC   IDLOI1_1_PE10; Q5QXH8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=3-ketoacyl-CoA thiolase; EC=2.3.1 16;AltName:
DE   Full=Acetyl-CoA acyltransferase;AltName: Full=Beta-ketothiolase;AltName:
DE   Full=Fatty acid oxidation complex subunit beta; (IDLOI1_1.PE10).
GN   Name=fadA; OrderedLocusNames=IL0010;
OS   IDIOMARINA LOIHIENSIS L2TR.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IDLOI1_1.PE10.
CC       Idiomarina loihiensis L2TR chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FADA_IDILO
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in
CC       which acetyl-CoA is released and the CoA ester of a fatty acid two
CC       carbons shorter is formed (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (fadB) and two beta
CC       chains (fadA) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the thiolase family.
CC   -!- GENE_FAMILY: HOG000012239 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5QXH8; -.
DR   EMBL; AE017340; AAV80854.1; -; Genomic_DNA.
DR   RefSeq; YP_154403.1; NC_006512.1.
DR   ProteinModelPortal; Q5QXH8; -.
DR   SMR; Q5QXH8; 2-387.
DR   GeneID; 3174456; -.
DR   GenomeReviews; AE017340_GR; IL0010.
DR   KEGG; ilo:IL0010; -.
DR   NMPDR; fig|283942.3.peg.60; -.
DR   OMA; QDIVNIN; -.
DR   ProtClustDB; PRK08947; -.
DR   BioCyc; ILOI283942:IL0010-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01620; FadA; 1; -.
DR   InterPro; IPR012805; FadA.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
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   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 4.
DR   PANTHER; PTHR18919:SF35; PTHR18919:SF35; 1.
DR   PANTHER; PTHR18919; 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   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   TIGRFAMs; TIGR02445; FadA; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
DR   HOGENOMDNA; IDLOI1_1.PE10; -.
KW   Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW   Lipid degradation; Lipid metabolism; Transferase.
SQ   SEQUENCE   387 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKDIVIVDCI RTPMGRSKNG VFRHTRAEDL SAALMKGLLE RNPEVDPEEL EDIYWGCVQQ
     TLEQGFNIAR NSALIAGIPH KVAGVTVNRL CGSSMQALHD ATRAIMNGDG DIFMAGGVEH
     MGHVPMTHGI DFHPGMNKSV AKASGSMGMT AELLSRKFGI TREQQDEFGA RSHRKAHEAT
     VEGRFAKEIY AMNGHNADGE LVRVTEDEVI RPETTAEGLS QLRPVFDPAN GTVTAGTSSA
     LSDGAAAMLV MSADKAKELG LTPRVKIRSM AVAGCDPSIM GYGPVPATEK ALKRAGVSID
     DIDVVELNEA FAAQSLPVLK GLKLFDKMEE KVNLNGGAIA LGHPLGCSGA RISTTLINLM
     EEKDAKLGLA TMCIGLGQGI ATVFERV
//

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