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Database: UniProt
Entry: A0A1H4QM89_9MICO
LinkDB: A0A1H4QM89_9MICO
Original site: A0A1H4QM89_9MICO 
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
//
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