ID A0A3N6MMI3_9BURK Unreviewed; 716 AA.
AC A0A3N6MMI3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=fadB {ECO:0000313|EMBL:RQH05054.1};
GN ORFNames=D1Y85_16780 {ECO:0000313|EMBL:RQH05054.1};
OS Paraburkholderia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH05054.1, ECO:0000313|Proteomes:UP000272778};
RN [1] {ECO:0000313|EMBL:RQH05054.1, ECO:0000313|Proteomes:UP000272778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOA04 {ECO:0000313|EMBL:RQH05054.1,
RC ECO:0000313|Proteomes:UP000272778};
RA Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT "Paraburkholderia sp. DHOA04, isolated from soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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:RQH05054.1}.
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DR EMBL; RQIS01000011; RQH05054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6MMI3; -.
DR OrthoDB; 5287258at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000272778; Unassembled WGS sequence.
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; IPR006180; 3-OHacyl-CoA_DH_CS.
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:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 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.
DR PROSITE; PS00067; 3HCDH; 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000272778}.
FT DOMAIN 317..494
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 496..591
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 627..710
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 716 AA; 76951 MW; DFB2819D369E6616 CRC64;
MFKGQSIRVQ ALGDGYVELC FDREGDSINK LDARTVDELR RATAEIAGVA GLRGVLVTSA
KNVFIVGADI TEFGEMFKLP VPDLAAHNAR SNEVFNAFED LPVPTVVALN GFALGGGLEM
AMSACYRIMS SEAQVGLPEV KLGLFPGFGG TVRLPRLASP AVAIDWIASG KPSKADGALA
AGVVDTVAQP EALRDVALDH LKRAAEGKLD WRARQNAKRS PLAQSPQDLA KLFDEARAKV
AKSSGKHQPA ALSAVEMMER AARMDRAGAL DEEGLAFARI AKTQAADALV QTFLSDQVLK
KLFKQHAKQA RAVGQGAVLG AGIMGGGIAY TSALRGVPVR LKDIAQAQLD LGISEAEKQL
AKQIKAGRLA QSKAHDVLRA IVPSLAYTDF DKVDVVVEAV VENLGVKHKV LRELEGVVRS
DTVIASNTSS LRIDDIAQPL QRPENFVGMH FFNPVPVMPL VEVIKGSRTS DAAVSTAVGY
AVAMGKTPIV VKDCPGFLVN RILTAYMRGF LQLVSDGADF ERVDQVMEAF GWPMGPAYLE
DVVGMDTGSH VSDIISAGYA ERMPYLEHDA LRLMSTNKRF GQKNGVGFYR YETDPNGKPR
RSVADDTRAL LAQIQPNGTR DFSDNEIIER MMLPLIIEAA HALEDGVVAS PVELDMALLL
GIGFPAYLGG ALKYADWLGL AHVVERAEAY AALGPGYRPT ERMRAMAAQG QRFYGN
//
