ID A0A1R4K3K4_9SPHI Unreviewed; 704 AA.
AC A0A1R4K3K4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Enoyl-CoA hydratase [isoleucine degradation] / 3-hydroxyacyl-CoA dehydrogenase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SJN38774.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:SJN38774.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:SJN38774.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:SJN38774.1};
GN ORFNames=FM107_09785 {ECO:0000313|EMBL:SJN38774.1};
OS Sphingobacterium sp. JB170.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1434842 {ECO:0000313|EMBL:SJN38774.1, ECO:0000313|Proteomes:UP000195951};
RN [1] {ECO:0000313|EMBL:SJN38774.1, ECO:0000313|Proteomes:UP000195951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB170 {ECO:0000313|EMBL:SJN38774.1,
RC ECO:0000313|Proteomes:UP000195951};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; FUKU01000030; SJN38774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4K3K4; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000195951; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:SJN38774.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:SJN38774.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:SJN38774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195951}.
FT DOMAIN 306..484
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 488..580
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 704 AA; 78337 MW; F0E1010E54C70DAF CRC64;
MDNTASQYFD IQQIAANIYW IKPRTTEIPS IDHFFDKLHQ FMDLATKLIA EPATRGIIYS
PPVEDLDYLA LYKAAENNTD FYNKLSKLVL SSTIFQTARK PIIGLLDRSC RGTAFSIMLW
ASYRIAFQDL EIGFLEAKYG LFPGFGATIV TSRLLGPEQA IPLLTQGVSY SALEGYQHGI
INRLLTPEQD PIASAVECIE NFAEITQEQI ALRGQRSLEI DEEQLVQAST FVIKRTNGLN
PGINACIEVV KRTLGLPIKD ALLVEAEVFS MSWKSPQTLS MLRTHYMGIK QALTHNLSAA
PFKVNKIGII GAGMMGAGIA YQAAKSGVTA ILCDQDILSA EQGKQYAEKI TNKQIQRHQI
CKLQQNELLA RIYPTADYDK LTGTQLIIEA IFEDRNLKIE VSRQHARYLH EEGIFATNTT
SIPITDLCES VPHPERYLGM HFFSPVDKMP LVEIIKGKKT SDETVAKALH VAYQLNKIPI
VVHDGPAFFT SRIFFNYILE AITMLLEGIS GAKIEQAARE AGFAVGPLAV LDEVSVSLMI
NVYDQLPQMH ASQQRCYNYL TKLVELGRNG RKTGQGLYDY DVTASTKKVW IDQDLVALNE
QYSDGTIKNR LLHVMALDSF RCLNEGILAN AIDGDIGSVL GVGYPAHTGG VFSHIDQIGV
HIFLEQCAAF RSLGQQWEIP STLEDLASTN FSFYNKFTPC PLPI
//
