ID F2RAP1_STRVP Unreviewed; 712 AA.
AC F2RAP1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Enoyl-CoA hydratase or 3-hydroxyacyl-CoA dehydrogenase or 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:CCA59110.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:CCA59110.1};
GN OrderedLocusNames=SVEN_5824 {ECO:0000313|EMBL:CCA59110.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59110.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA59110.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA59110.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00023693};
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}.
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DR EMBL; FR845719; CCA59110.1; -; Genomic_DNA.
DR RefSeq; WP_015037005.1; NZ_JABVZO010000214.1.
DR AlphaFoldDB; F2RAP1; -.
DR STRING; 953739.SVEN_5824; -.
DR GeneID; 69867874; -.
DR KEGG; sve:SVEN_5824; -.
DR PATRIC; fig|953739.5.peg.1037; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_2_11; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 1.
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 degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CCA59110.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT DOMAIN 340..520
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 524..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 712 AA; 75742 MW; 5A2B83E0AE427892 CRC64;
MSTTAELLKG AAELFPDEVV TSAHVRHFEL PAGAGRFALI TLDNGFDHTK PTTFGPQSLA
NLNTAIDQVE AEAANGEIVG VGITGKPFIF AVGADLKGVE LLKKHDEALA IGKGGHDVFK
RLSALAVPTF AYYNGAAMGG GVEVGLHCTY RTVSKALPAF SLPEVFLGLV PGWGGCAILP
NLIGAEKAVS VIIENSLNQN RQLKGKQVFE LGIADALFEG ADFLEQSLIW TAGVLTGSVT
VERPEVDRGE AWDQAVAKGR AIADSKVHGA APAAYRALDI IEAAKDGDLQ KGFDAEDQAL
ADLIMGGELR SGIYAFNLVQ KRGKRPAGAP DKSLARPVTK VGVVGAGLMA SQLALLFLRR
LEVPVVLTDI DQERVDKGVG YVHGEIEKLL GKGRINQDKA NRLKGLVSGV LDKAAGFADA
DFIIEAVFEE MSVKQKVFAE VEAVAPAHAI LATNTSSLSV SEMASKLQHP ERVVGFHFFN
PVAILPLLEI VRGEQTDDAS LATAFGVAKK LKKTAVLTKD APAFVVNRIL TRFMGEIQNV
IDEGTPVETA EKAIEPLGLP MSPLVLLELV GPAIGLHVSE TLNRAFPERF TVSPNLKRVV
EAGKRGFYVY NAENGFKPEL DPEVAALLVQ GDSVLTEEQV RDRVLDAVAQ EIGLMLEEGV
VAEAQDIDLC LITGAGWPFH LGGITPYLDR EGVSERVNGK RFLAQGVASV PA
//
