(data stored in SCRATCH zone)

HOGENOM: PSEHT_1_PE10

ID   PSEHT_1_PE10                         STANDARD;      PRT;   389 AA.
AC   PSEHT_1_PE10; Q3IJ24;
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; (PSEHT_1.PE10).
GN   Name=fadA; OrderedLocusNames=PSHAa0010;
OS   PSEUDOALTEROMONAS HALOPLANKTIS TAC125.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSEHT_1.PE10.
CC       Pseudoalteromonas haloplanktis TAC125 chromosome I, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:FADA_PSEHT
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; Q3IJ24; -.
DR   EMBL; CR954246; CAI85124.1; -; Genomic_DNA.
DR   RefSeq; YP_338567.1; NC_007481.1.
DR   HSSP; P28790; 2D3T.
DR   ProteinModelPortal; Q3IJ24; -.
DR   SMR; Q3IJ24; 5-387.
DR   STRING; Q3IJ24; -.
DR   GeneID; 3709118; -.
DR   GenomeReviews; CR954246_GR; PSHAa0010.
DR   KEGG; pha:PSHAa0010; -.
DR   NMPDR; fig|326442.4.peg.21; -.
DR   eggNOG; COG0183; -.
DR   OMA; SSMEAIH; -.
DR   PhylomeDB; Q3IJ24; -.
DR   ProtClustDB; PRK08947; -.
DR   BioCyc; PHAL326442:PSHAA0010-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; PSEHT_1.PE10; -.
KW   Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW   Lipid degradation; Lipid metabolism; Transferase.
SQ   SEQUENCE   389 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNNPVIVDCI RTPMGRSKGG VFKNKRAEDL SAHLMKGLLD RNPAVDPASI DDIYWGCVQQ
     TLEQGFNVAR NAALLAGIPH SVPAVTVNRL CGSSMQALHD AARAIMTGAG DTYLIGGVEH
     MGHVPMTHGN DFHPGLATSI AQAAGSMGLT AEYLATLHGI SREQQDEFAY RSHQRAQAAT
     VEGRFRREIL AMEGHAADGS LILVEDDEVI RPETTVEGLS KLRPVFNPAS GTVTAGTSSA
     LSDGASAMLV MSEAKAKELG LPIRARIKAM AVAGCDPSIM GYGPVPASKK ALAQAGITID
     DLGVVELNEA FAAQSLPVMK DLGLMDVVDE KVNLNGGAIA LGHPLGCSGS RISTSLIHLM
     EDKNVRYGLA TMCIGLGQGI ATVFERVQD
//

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