ID F6EUQ3_SPHCR Unreviewed; 725 AA.
AC F6EUQ3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:AEG48771.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:AEG48771.1};
GN ORFNames=Sphch_1081 {ECO:0000313|EMBL:AEG48771.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG48771.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG48771.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG48771.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-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 central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; CP002798; AEG48771.1; -; Genomic_DNA.
DR RefSeq; WP_013847034.1; NC_015593.1.
DR AlphaFoldDB; F6EUQ3; -.
DR STRING; 690566.Sphch_1081; -.
DR KEGG; sch:Sphch_1081; -.
DR HOGENOM; CLU_009834_16_2_5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000007150; Chromosome 1.
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:AEG48771.1};
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}.
FT DOMAIN 325..501
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 504..600
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 725 AA; 77203 MW; 51D0CDBD7FACA856 CRC64;
MQSINFDIDG DGIATLTIDV PGQSMNVIGP DFMADLDAAI TRIASEEAIK GAVIASGKDS
GFMAGMDLKY FGSMLGSESG KAPSPAAIFD KVFVLNQLFR RLETCGKPVA CAIEGTCVGG
GFELALACHR RVVGDSPKTQ LGLPEILIGL FPGGGGSQRL PRIMGVQASL MYMLQGKLFR
PAEAAMMKVV DEVVPQGTAV EKAREWVKAN PNASVQPWDV KGFKVPGGAG GFNPAFAQTM
AGALPMTLKQ TQRNMNAPVA LLSAVYEGIT LPMDRAVRIE SKYFAKVAAD PQAANMIRSL
FVNKQAAERG ARRPKDQPKA PTKKLAMLGA GMMGAGIATV AAQAGMEVVL FDRDQAYAEK
GKAHVEAVLQ KRLGKGLTPE KMAETLARVT PTTDYAALAG ADFVIEAVFE DVAIKAEVTK
KVEEVLGADV IFGSNTSTLP ITKLARAWSK PENFIGVHFF SPVEKMPLVE IILGKETGPA
AIAKALDFVS QIRKTPIVVN DARGFYTSRC FATYVQEGVE MVAEGINPAL IENAGRQLGM
PVGPLAVGDE VSLELGHKIM VAARKELGDA YVAQPSDAVM ERMVGLGRLG RKSAKGWYDY
PEGGKKHLWP GLAEMFPRAD VQPDVEAVKE RLLYRQLIEC ARCFEEGVLE TPEDGDIGAI
FGWGFAPYTG GPFSHMDTVG IGTVVAVLDR LAAAHGGRFA PTAQLREMAA SGATFYRPVS
SRAAA
//
