ID FAD3_RICPR Reviewed; 720 AA.
AC Q9ZCZ1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=RP560;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
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; AJ235272; CAA15008.1; -; Genomic_DNA.
DR PIR; F71660; F71660.
DR RefSeq; NP_220931.1; NC_000963.1.
DR RefSeq; WP_004599039.1; NC_000963.1.
DR AlphaFoldDB; Q9ZCZ1; -.
DR SMR; Q9ZCZ1; -.
DR STRING; 272947.gene:17555640; -.
DR EnsemblBacteria; CAA15008; CAA15008; CAA15008.
DR GeneID; 57569682; -.
DR KEGG; rpr:RP560; -.
DR PATRIC; fig|272947.5.peg.573; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_010448_0_0_5; -.
DR OrthoDB; 5389341at2; -.
DR Proteomes; UP000002480; 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; Reference proteome.
FT CHAIN 1..720
FT /note="Putative fatty acid oxidation complex trifunctional
FT enzyme"
FT /id="PRO_0000285698"
FT REGION 1..384
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT REGION 453..720
FT /note="Enoyl-CoA hydratase/isomerase"
SQ SEQUENCE 720 AA; 81403 MW; BAEC37A40044234E CRC64;
MQNEIKKVCV IGAGVMGSGI AALIANSSHQ VVLLDILDKD SNDPNKIVKN SVKNLHKQKL
SPLSFPDKVN FITIGNLEHD LDLIKECNLV IEVIVEKLEI KHQLYNKIIP YLKEDAIIAS
NTSTLPLKKL KVNLPNNIKS RFVITHFFNP PRYMELVELI IDHTIKDEVI EKVSVFLTKM
LGKTIIKCND TPGFIANRVG CFLLELVVHK AIAQNLNFVT IDQIFSRCLG LPNTGIFGLY
DLIGHDVMKL ISSSLISALP KSDDYHRIYT NTKVFDKMIE HNLIGRKGEG GFYRLSVSNG
KKIKEVINIS DLSYHPVQKV DISFNSLNEL LSSNSIYGKF FSEIITEFYI YLTSLVPSVT
NNIYDIDTTM KLGYSWHYGP FELLTIAVKN GWNLIIKNAD LMNIPLPKYL ASKEYQKIDK
QKFNSKKDFL QESKIVLSND SANLIHYCEN LVFVITTKMN SLNHNVFYLL QEAVSKAENY
GKNLYIYPQG NNFSAGADLK LILSYIQDGN FHNLENLLKL GQQTMRYLKY SSVHIISCAR
GVALGGGCEL LLNSSYIVAN QELNAGLIEL GVGLIPGWTG VTEMFARSNG NKTKLIRNIK
NIIEQNKTSS ADYFKADYGI KNMQVNMNKH YILDDALKLR ISKKIVSIPN KITLPKINIV
SEIDTSKYNE LQNKVLNKFQ NIIDKHNEIS EAELLTYERE MFLELAKTPQ TIEKLQAIVG
//
