ID   FAD3_RICFE              Reviewed;         720 AA.
AC   Q4UL32;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Putative fatty acid oxidation complex trifunctional enzyme;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase;
DE              EC=4.2.1.17;
DE              EC=5.3.3.8;
GN   OrderedLocusNames=RF_0890;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000305}.
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DR   EMBL; CP000053; AAY61741.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4UL32; -.
DR   SMR; Q4UL32; -.
DR   STRING; 315456.RF_0890; -.
DR   KEGG; rfe:RF_0890; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_010448_0_0_5; -.
DR   OrthoDB; 5389341at2; -.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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; IPR045004; ECH_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF16113; ECH_2; 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; Isomerase; Lipid metabolism; Lyase;
KW   Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN           1..720
FT                   /note="Putative fatty acid oxidation complex trifunctional
FT                   enzyme"
FT                   /id="PRO_0000285697"
FT   REGION          1..384
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT   REGION          453..720
FT                   /note="Enoyl-CoA hydratase/isomerase"
SQ   SEQUENCE   720 AA;  81043 MW;  AB2E8CBC1C1F1426 CRC64;
     MQNEIKKVCV IGSGVMGSGI AALIANSSHK VVLLDIIAKD SDDPNKIVKT AKENLHKQKP
     PPLSFPDKVN FITIGNLEHD LELIRDCDLV IEVIVEKLEI KHQLYNKIIP YLKEDAIIAS
     NTSTLPLKRL KENLPDNIKS RFVITHFFNP PRYMELLELI IDSMVKFEVI ERVSGFLTKT
     LGKTIVKCND TPGFIANRVG CFLLELVARK AISQKLDFVA LDKIFTICLG LPSTGIFGLY
     DLIGHDVMKL ISSSLLAALP ANDAYHKIYV NTPVLDKMIE KKLIGRKGEG GFYRLSVSNG
     KKIKEVININ DLSYSSVQKV DISFNNLDEL LVSDSVYGKI FTEIITEFYV YLASLVPSVT
     DNIYDIDAAM KLGYSWKYGP FELLTIAAKD GWNSVIKNAD LMHIPLPQYL GNKEYQKIDK
     QKFNSHKDIL QESQIVLEND SAKLINYREN FIFVITTKMN CLNHNVFYLL QEAASKAEKD
     GKNLYIYPQG NNFSAGADLK LLLSYIEDGN FHDLENLLKL GQQTMLHLKY SGVHIISCAK
     GVALGGGCEL LLYSSYIVAN QELNAGLVEL GVGLIPGWGG VTEMFVRSKG DKTKLIRNVR
     NIIEQNKTSS ADYFKSDYDV ESMHVNMNKH YILDEALKLN LSKKIVPIPH KITLPKINLA
     TEIDTSKYND LQNKVLSKFQ NIIDKHPDTN EEELLGYERE IFLELAKDPK TIEKLKAIVK
//