ID   A0A1X0NSD1_9TRYP        Unreviewed;       815 AA.
AC   A0A1X0NSD1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Trifunctional enzyme alpha subunit, mitochondrial-like protein {ECO:0000313|EMBL:ORC87521.1};
GN   ORFNames=TM35_000211270 {ECO:0000313|EMBL:ORC87521.1};
OS   Trypanosoma theileri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC87521.1, ECO:0000313|Proteomes:UP000192257};
RN   [1] {ECO:0000313|EMBL:ORC87521.1, ECO:0000313|Proteomes:UP000192257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|EMBL:ORC87521.1};
RA   Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA   Matthews J., Matthews K., Carrington M.;
RT   "An alternative strategy for trypanosome survival in the mammalian
RT   bloodstream revealed through genome and transcriptome analysis of the
RT   ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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:ORC87521.1}.
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; NBCO01000021; ORC87521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0NSD1; -.
DR   STRING; 67003.A0A1X0NSD1; -.
DR   VEuPathDB; TriTrypDB:TM35_000211270; -.
DR   OrthoDB; 622692at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000192257; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProt.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192257}.
FT   DOMAIN          398..578
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          581..676
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          706..791
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   815 AA;  89799 MW;  7A942CFC5C229FC9 CRC64;
     MMRRNGLGKL PALGFISGFF HQQLHCQSCM CKTNAPLNSE PPVEVPSGKK TTVSVNDFKS
     CILKNRIWAI HPAGKHVTVY VDSGIYAWIV MDRAGSSANA LGEEFVKCMH QALDIVEKLV
     AENKARVVII ASAKSSFCVG ADLDQLYPLT DRKMASEAAK MGHGLFNRIQ QEPFPVVAAI
     NGLALGGGFE MTLACHHRLL ASNGSVGLPE CLLGLLPGAG GTVRLQRFVG LATAVQWIMT
     SVPAKAPKAK KAGVLDAVIE AEPRWEGEER FFEGVRKWSG RLVDKPLKPM KRKNISLMDR
     FLERTSFGRK IVGNKTIEML NKKTKGKYIA QYKALEAIIY SAAHSEKEGL AKERDIFSEL
     LVTPEAKNQI ALYFLDEGMK KSERKTGISK DKVPPVRKVG VIGAGVMGSG IVHYFANKGI
     PVAVKDVKQE AVDKGIEMVR GEFKTAVVRK KITPTVMEAK MKLVTGGTSD TVFHDVDVIV
     EAAVEVMDIK KKIIQEMENQ GVINGKNIFA TNTSSLSLTE MQTVSKYPER IVGMHFFNPV
     SKMPLVEVIK GKKTSAETAA VIFNLALKTG KKPIIVNDAP GFVVNRILGV YMAEASRLAI
     EEEVDLALIE KAMLNFGMPM GPFRLLDEVG LDIACHVGPV LSEGIKSKRF AVGSQVEQMM
     KDGYLGKKNG KGLYRYDAKG KETVMNTETL EKYFPQSKKS KDENEIVDRC VLLMVNEACY
     ILQEGVAATP EDVDIGMIWG TGFPAFRGGL LQHADHRGLQ AVVGRLRQFQ DETGSDRYAP
     SPLLLTMVKE EKRFFPNRPF VPYKERSGYP QVKFY
//