ID   A0A1F8EBN9_9BACT        Unreviewed;       847 AA.
AC   A0A1F8EBN9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2817_00630 {ECO:0000313|EMBL:OGM97405.1};
OS   Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_39_8b.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1802659 {ECO:0000313|EMBL:OGM97405.1, ECO:0000313|Proteomes:UP000177594};
RN   [1] {ECO:0000313|EMBL:OGM97405.1, ECO:0000313|Proteomes:UP000177594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
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:OGM97405.1}.
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DR   EMBL; MGIZ01000052; OGM97405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8EBN9; -.
DR   Proteomes; UP000177594; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 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; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 2.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          7..211
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          272..301
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          309..430
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          445..625
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          628..719
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          751..834
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   847 AA;  92855 MW;  EA82E4D86BC6EB58 CRC64;
     MVKQRMVIVE GVRTAIGSFG GGLKDAPADM LLAICFQEVI KRTGIDPAVI DEVIAGNICQ
     PSDSVNIARV SALRAGVPSH VPAITVGCNC FSGAEAILQA YRAYKAGDCE IVLVGGTENM
     SRVPYLLKQA RFGQKLQHHV VTDGLWEGLV DPTINQIMGR TAENVARKWN ISRRDQDDFA
     VASHKKAKYA KTEGKFKSQI VSVVIKKTMS VGDNISGGES IFAEDECINP DPDDQKWVQR
     VYSLPAMFLN EHVSEPKNPK PVFKDGKVVL HDSYANEGTV TSGNSCPMSD GAAALLLMSE
     EKAKEFNLEP MAYVLSYSRI GCDQEYMGEG PIYAVPKVLE KAGLKVGDID LFELNEAFAA
     QAIVCQRQLG IPDEKLNIWG GAIALGHPVG ATGAILTIKA MHMLEEAQKR YALITMCVGG
     GQGGCLIIER GSRNKKENKT KAINKIAVIG GGAMGCGIAL LVSQHGRQVV IKEVIPEFAE
     KSLKTVHDKL NAAVARGKLM SDRANTAKGL VTATADISEI RDVDLVIEAV FENLEVKKKV
     FAELDRVVRP DAIFATNTSS LSITEIASAT TRPERFIGMH FFNPPITMPL VELISSNMTS
     RETLAAADDF AKNSLGKVTI HVKECPAFLI NRLLMPYLNE AAYLLTETTL TVEEIDAYAR
     QFSWPMGPFV LLDYLGIDIA AEVAEICRRG YGKRAKPAPL MRRLVELGRF GDKSGAGFYI
     KDKTKGLEPL SAILGREYPN RMPLNVAEGF HRMMLGMVNE AFLCLEENIS SPEEVDIGCL
     YGIGFPMALE GPLHWAEKEG LANILGDLKR FEQECGERFK PSRLLERYVA ENKNIFKKKE
     TDEREEW
//