ID A0A1H4QM89_9MICO Unreviewed; 711 AA.
AC A0A1H4QM89;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SEC20770.1};
GN ORFNames=SAMN04489806_2860 {ECO:0000313|EMBL:SEC20770.1};
OS Microbacterium humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=640635 {ECO:0000313|EMBL:SEC20770.1, ECO:0000313|Proteomes:UP000199183};
RN [1] {ECO:0000313|EMBL:SEC20770.1, ECO:0000313|Proteomes:UP000199183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21799 {ECO:0000313|EMBL:SEC20770.1,
RC ECO:0000313|Proteomes:UP000199183};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNRY01000001; SEC20770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4QM89; -.
DR STRING; 640635.SAMN04489806_2860; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000199183; 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:UP000199183}.
FT DOMAIN 344..523
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 526..617
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 711 AA; 76962 MW; 1B7669401ACBF76D CRC64;
MTNDTRARFS ALLDISGDEV VTHSFVRDVS LPTGKTLALL TLDNGKDHTR PNTFGPIGLI
ELDDALETQR ERASRGEIAG LAITGKPFIL AAGADLSKVN DIPSREVANL LPQLGHHVFG
KLEDLGVPTF VFINGLALGG GLEIGLNANY RTIDSSAAAI ALPEVFLGLV PGWGGAYLLP
NLIGIENALK VIIENPLKMN RMLKAPQAFE LGIADVMFPS ARYLEDSIAW ASGVIEGAIK
PERKNTPGKI ERMVKWDAAT GIARKMLESK IGTVPVAPYK ALDLLKAAKS GTKAEGFARE
DEALADLIAG EQFRASVYAF NLVQKRAKRP AGAPDKELAR KITKVGVIGA GLMATQFALL
FVRRLQVPVV ITDLDQERVD KGVQTIRSEI DALLAKKRIS PDEANRLKAL VHGTTDKADF
ADCDWVIEAV FEELTVKQDV FADVEKHIAP EAVLATNTSS LSVEQIGAKL EHPERLVGFH
FFNPVAVMPL IEVVRTPQTS DEVLATAMAT AKNLKKNAVI TRDTPGFVVN RVLAKLLGEA
MHAVELGTSF ADVDAALAPL GLPMPPSELL DLVGLRVGAH VLDTHHRAFP DRFYDSEKLH
KLAEYGTLFE KDKKGAIKGF DKGALKIISG GREPMSREEL LRRVQDGLAD EIHRMLDDDV
VEAAEDIDLC LILGAGYPFQ MGGVTPYLDR VGASERVFGD TFHHPPLLGL S
//