ID G8S0P0_ACTS5 Unreviewed; 676 AA.
AC G8S0P0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:AEV83395.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:AEV83395.1};
GN Name=fadB {ECO:0000313|EMBL:AEV83395.1};
GN OrderedLocusNames=ACPL_2500 {ECO:0000313|EMBL:AEV83395.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV83395.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-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; CP003170; AEV83395.1; -; Genomic_DNA.
DR RefSeq; WP_014689467.1; NZ_LT827010.1.
DR AlphaFoldDB; G8S0P0; -.
DR STRING; 134676.ACPL_2500; -.
DR KEGG; ase:ACPL_2500; -.
DR PATRIC; fig|134676.3.peg.2420; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_3_11; -.
DR OrthoDB; 3216872at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005440; Chromosome.
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:AEV83395.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440}.
FT DOMAIN 317..477
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 480..576
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 676 AA; 71427 MW; BC96AEF77A4AC79A CRC64;
MISYDKDEAG IVTLTMNDPD QSANTMNATY VAAMSAALDR LEAERDQVTG VIVSSAKSTF
FAGGDLPTMS RARPEDAGAL FDLLGTIKKD LRRLETYGRP VVAAINGAAL GGGFEIALAC
HHRIALDAPG TRVGFPEVTL GLLPGAGGVT RTVRMLGLAP ALTVWLLTGK RVKPAAAREA
GMIDEVVSSQ DEMMARAREW IAANPDAAQP WDRPGYRMPG GTPATPKLAV QLPAFPATLR
KQLKGNRMPA PEAILATAVE GAQVDIETAF TIETRRLITL LTGRIAKNMI GAFFFDMRAV
NGGAARPRVD VAPATRIAVL GAGMMGAGIA YACAQAGLEV VVKDVSREAA ARAVAEGDPA
VLARITPTAD VEDLRGCDVV IEAVFEDPKL KHQVFAEVEP VLAAGALLAS NTSTLPITGL
AEGVTRPGDF IGMHFFSPVG KMPLLEIMVG EQTSDAAIAR AFDLGRRIGK TPIVVNDGRG
FFTSRVIGQF MNEAVAMLAE GVPAASIEQA ALQAGYPTGP LALADEVTLT LMHKIHKAYA
AAGTTAGPAK AHALIQEMLE RHDRPGRSSG RGFYTYENGR RGRLWDGLAG LATDEGRAIP
FADVQERLLF SEALDALRCR AEGVLRTDAD GNIGSILGIG FPAWTGGVLR YVEQHPDFKG
RAAELAARYG DRFAPA
//
