ID G6F1C7_9PROT Unreviewed; 713 AA.
AC G6F1C7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=CIN_12800 {ECO:0000313|EMBL:EHD13921.1};
OS Commensalibacter intestini A911.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD13921.1, ECO:0000313|Proteomes:UP000005939};
RN [1] {ECO:0000313|EMBL:EHD13921.1, ECO:0000313|Proteomes:UP000005939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A911 {ECO:0000313|EMBL:EHD13921.1,
RC ECO:0000313|Proteomes:UP000005939};
RA Lee W.-J., Kim E.-K.;
RT "Genome Sequence of Commensalibacter intestini A911, isolated from
RT Drosophila gut.";
RL Submitted (OCT-2011) 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:EHD13921.1}.
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DR EMBL; AGFR01000007; EHD13921.1; -; Genomic_DNA.
DR RefSeq; WP_008854270.1; NZ_AGFR01000007.1.
DR AlphaFoldDB; G6F1C7; -.
DR STRING; 1088868.CIN_12800; -.
DR PATRIC; fig|1088868.3.peg.1285; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005939; 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 Oxidoreductase {ECO:0000313|EMBL:EHD13921.1}.
FT DOMAIN 314..492
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 494..589
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 626..704
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 713 AA; 78382 MW; FC6BC007C8F37A51 CRC64;
MYQGQFFQVA TRDQFLELVF DSKIDQVNII NKAALEDLQK AVNSIKTSGG KGLIIRSGKQ
LFSAGVDIKE FRHLIHQDDK TLSNYIVWAN EIFNSIEDLN MPKVAILNGN IVSAAAELTL
TADYRIATQD TKISLPEITL GIMPCYGAMT RLPRITGLDT ALQWFTAGKP FTADTALEHH
VIDGVIADKI DPIEQAVILL KSCVAGDLDW TARHNEKKAP LTLNKYELAM SISIARSMAF
KTAGKHYPAP NIILDTQEKS ANCERDAALA LDREGLIQCI KTGVADALIN VSLNDTLVRE
KAKGLVKDLK EFSNVGVIGA GIMGGGIAYV TADKGADVVL KDINKEGLNL GLNEANSILS
KQVERGRKTP KAMGDTLNHI HATLHNVELE ETDLIVEAVV ENLKLKKAVL TELEGVATKA
VIATNTSTLK VSDIAQALKS PENFCGIHFF NPVPKMPLVE VVRGEKTSDE TIKKAVKYVT
QLGKTPILVN DCHGFLVNRC LVPYFHAFNK LILDGANMST VDKVMSKEFG WPMGPAMLLD
VIGLDTAEHC MDVMGEAFPD RMTKPEKNLI GSLFDMKHYG QKNGEGFYTH APDKRGRLKA
SDNDTANKLI ASFASPAQDF SADDIIMRMM LPMMFEAIRC LDEGIIASPA EGDIAMMYGT
GFPPFRGGLF YYMDQIGLSK LVEASEKYKN ISNLYHTPES LIQRLKNNQK FYA
//
