ID A0A0Q2QX13_MYCGO Unreviewed; 714 AA.
AC A0A0Q2QX13;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KQH76486.1};
GN ORFNames=AO501_28045 {ECO:0000313|EMBL:KQH76486.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH76486.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH76486.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH76486.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-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:KQH76486.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKTM01000350; KQH76486.1; -; Genomic_DNA.
DR RefSeq; WP_055580591.1; NZ_LKTM01000350.1.
DR AlphaFoldDB; A0A0Q2QX13; -.
DR STRING; 1778.A9W97_19860; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000051677; 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:UP000051677}.
FT DOMAIN 322..500
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 503..602
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 714 AA; 76352 MW; 911DAFD3C4C6DC2A CRC64;
MTDNTIQWDK DDDGIVTLTL DDPSGSANVM NEAYIESMGK AVERLVAEKD SITGVVITSA
KKTFFAGGDV KSMIQIGPEN AGEAFDLVEN VKKQLRTLET LGKPVVAALN GAALGGGLEI
ALACHHRIAA DVKGSQFGFP EATLGLLPGA GGVTRSVRMF GIQNAFMNVL SQGTRFKPAK
AKELGLIDEL LPTVEELVPA AKAWIKANPD SHEQPWDKKG YKMPGGTPSS PALASILPSF
PALLRKQIKG APMPAPKAIL AAAVEGAQVD FDTASRIESR YFTTLVTGQV SKNMIQAFFF
DLQAINAGKS RPDGIEPVKI NKIGVLGAGM MGAGIAYVSA KAGYDVVLKD VSIEAAQKGK
GYSEKLEAKA LERGRTTQEK SDALLARITP TADPADFKGV DFVIEAVFES QDLKHKVFQE
IEDIVEPNAL LGSNTSTLPI TGLATGVKRQ EDFIGIHFFS PVDKMPLVEI IKGEKTSDEA
LARVFDYTLA IGKTPIVVND SRGFFTSRVI GTFVNEALAM LGEGVEPASI EQAGSQAGYP
APPLQLSDEL NLELMHKIAV ATRKGVEDAG GKYEPHPAEA VVEKMIEVGR SGRLKGAGFY
EYPEGKRSGL WPGLRETFKS GSSEPPLQDM IDRMLFAEAL ETQKCLDENV LMTTADANIG
SIMGIGFPPW TGGSAQYIVG YEGPLGRGKE AFVARARELA KKYGDRFLPP DSLT
//
