ID A0A0F3LH47_9CAUL Unreviewed; 734 AA.
AC A0A0F3LH47;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KJV42915.1};
GN ORFNames=VH88_03150 {ECO:0000313|EMBL:KJV42915.1};
OS Brevundimonas sp. KM4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV42915.1, ECO:0000313|Proteomes:UP000033583};
RN [1] {ECO:0000313|EMBL:KJV42915.1, ECO:0000313|Proteomes:UP000033583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM4 {ECO:0000313|EMBL:KJV42915.1,
RC ECO:0000313|Proteomes:UP000033583};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Brevundimonas sp. KM4.";
RL Submitted (MAR-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:KJV42915.1}.
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DR EMBL; JZRG01000006; KJV42915.1; -; Genomic_DNA.
DR RefSeq; WP_045810038.1; NZ_JZRG01000006.1.
DR AlphaFoldDB; A0A0F3LH47; -.
DR PATRIC; fig|1628191.3.peg.2395; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000033583; 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}.
FT DOMAIN 323..501
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 504..600
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 734 AA; 78860 MW; 0E158A78D8FDDEEE CRC64;
MENFKIDVDA DNIALITFDV PGRSMNTLTS SVMKEIPELV ERIKTDDAIK GAVITSGKAS
GFCAGADLGD MAGGVLSGGG DLQKAFDAGW KLNGAFRALE TSGKPIAAAI NGLALGGGLE
FTLAAHYRVV ENDNKIQLGL PEIKVGLFPG GGGTQRLTRL VGVQNAMMAM SEGKSFRPND
AKGAGIVHEV VEKGQSVEAA KAWIKTKVES GGKAVQPWDE KSFKLPGGGP YHPAGIQNFM
VGNAMLRKQS YGNYPAVVNL MKAVYEGAQV PMDAALRIET RYFIKTLMTP QAQAMIRSLF
LSKQELDKGA VRPAGVPKSD PKKVTVIGAG MMGAGIAYVQ ALAGIETILI DQTQEAADKG
KAHVEELLKK RLSRGQLTQE KYDALLGSVT ATTDYDLIKG SDLVVEAVFE NREIKADVTK
RAEAQLADGA VFGSNTSTLP ITGLAEASVR PEDFIGIHFF SPVDKMMLVE IILGEKTGQA
AIAKALDYVL KIKKTPIVVN DSRGFYTSRC FSTFLMEGMA MLEEGYGPAL IDNVGRMTGM
PRGPLEMHDD VALDLSYKIA KQTALDLGDK YVPSEGADIV AKMVEGGRFG RKNGKGFYDY
DQKPKTIWKG LGELAPTTKG IDQPEEPTAF AQIDELKTRL LYRQAVEVAR CWEEGVIDDP
READLGAILG WGFAPWTGGP ISMIDGIGLA KFVETADRLA ATYGDRFEVP QLLRDMAAKN
ETFYGKFAPE KAAA
//
