ID A0A095ZLY7_9MICC Unreviewed; 703 AA.
AC A0A095ZLY7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KGF19622.1};
GN ORFNames=HMPREF2128_09535 {ECO:0000313|EMBL:KGF19622.1};
OS Pseudoglutamicibacter albus DNF00011.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudoglutamicibacter.
OX NCBI_TaxID=1401063 {ECO:0000313|EMBL:KGF19622.1, ECO:0000313|Proteomes:UP000053528};
RN [1] {ECO:0000313|EMBL:KGF19622.1, ECO:0000313|Proteomes:UP000053528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00011 {ECO:0000313|EMBL:KGF19622.1,
RC ECO:0000313|Proteomes:UP000053528};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF19622.1}.
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DR EMBL; JRNH01000031; KGF19622.1; -; Genomic_DNA.
DR RefSeq; WP_035757683.1; NZ_JRNH01000031.1.
DR AlphaFoldDB; A0A095ZLY7; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000053528; 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:UP000053528}.
FT DOMAIN 334..513
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 517..595
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 703 AA; 75312 MW; 35A4E0DF16E039F5 CRC64;
MRSAAPNEIV TRVEVEDHEV GGHTIALMTM VAEKEGHPAT LGPAGLAKIG RAAEAQVKRA
EAGEIDAIAI TGTGRTFAAG ADLSTIRTLS DPDDGRRLAE LGHVAYDVIA DADVPSFAFI
NGQSLGGGFE TALAFKHRTV NTAARALGLP EAGLGLIPGW GGVYRFPRIV GIENGLKVML
ENPLKGNRFL TGNELVEMGG AHVGFGPENF LQDSLDWAAS VLDGTAPEAQ RELEDPSDPE
VSARWDAALK YARGLVEKAT HAETRPAPTA LLDALDANRS MTQKQSAELE VDTLARLMFT
PAFQNTIYSF LELFQARAKR PAGVPAVEPQ KISKVGVVGA GLMAAQLALV FAQKLQVPVM
MTDMDEQRAQ AGLDHVAGYL AKNVERGRMK EEDARAIQQL ITAGTDKGVY ADADFVIEAV
FEEIGVKQQV FREVEKIVRP DAILATNTSS LSVKEMAEVL EHPERLVGFH FFNPVAQMPL
IEIVRGPETS DQVLATAFAA AKGLGKTAVL VKDAPAFVVN RLLLLLLGLV MDAFDQGMDP
HEADSALDPL GLPMSPFDLL AMVGLPVAQH VAETLNTSFP ERFPLSKNLQ TLIDNKITSI
WSKDEKGRKF IPEEHLALLE RGDATITKDQ LLTTVLDALA TEIRIMLDEG VVAGPQDIDL
CMILGAGWPQ HLGGITPFLD QSGGSTRANG EAFGAWSLPA STK
//
