ID A0A0N0T0P8_9ACTN Unreviewed; 727 AA.
AC A0A0N0T0P8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KOV66536.1};
GN ORFNames=ADL00_17050 {ECO:0000313|EMBL:KOV66536.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV66536.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV66536.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV66536.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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:KOV66536.1}.
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DR EMBL; LGDU01000163; KOV66536.1; -; Genomic_DNA.
DR RefSeq; WP_053759019.1; NZ_LGDU01000163.1.
DR AlphaFoldDB; A0A0N0T0P8; -.
DR PATRIC; fig|1519489.3.peg.3885; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000037758; 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; 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 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:UP000037758}.
FT DOMAIN 322..500
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 503..603
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 727 AA; 78163 MW; 72C725DC71F919D1 CRC64;
MTESTTIRWE QDDTGVVTLV LDDPAQSANT MNQAFRDSLA AITDRLEAEQ DSIRGIILTS
AKKTFFAGGD LRDLIRVTPE TAQQLFDGGL AIKRHLRRIE TLGKPVVAAL NGAALGGGYE
IALACHHRVA LDAPGSKIGC PEVTLGLLPG GGGVVRTVRL LGIADALLKV LLQGTQYSPR
RALENGLIDD VADTREELLA KARAFIDANP ESQQPWDRPG HRIPGGTPAN PKFAANLPAF
PAGLRKQTNN APYPAPRAIL AAAVEGSQVN FETAQVIEAR YFVELAAGQT AKNMIQAFFF
DLQAVNSGAN RPKGVEPRQV RKAAVLGAGM MGAGIAYACA RAGIDVVLKD VSLEAALKGK
AYSEKLCAKS VAKGRTTQEK ADALLARITP TAEIQDLEGC DAVIEAVFED TALKHKVFQE
IEQVVAPDAL LCSNTSTLPI SALAEGVQRQ TDFIGLHFFS PVDKMPLVEI IKGERTGDEA
LARAFDLVRQ INKTPIVVND SRGFFTSRVI GHFINEGVAM VGEGIEPASV EQAAAQAGYP
AKVLSLMDEL TLTLPRKIRN ESRRAVEEAG GTWQAHPAES VIDRMVDEFG RTGRSGGAGF
YEYGPDGSRT GLWPGLREHF TREDARIPFE DMQERMLFSE ALDTVRLLEE GVLTSVADAN
IGSVFGIGFP GWTGGVLQYV NGYRDGAGVP AFVARARELA ERYGERFTPP AMLVDMAEKG
ETFTDAR
//
