ID R1G8W6_9PSEU Unreviewed; 723 AA.
AC R1G8W6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EOD67847.1};
GN ORFNames=H480_14215 {ECO:0000313|EMBL:EOD67847.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD67847.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD67847.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD67847.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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:EOD67847.1}.
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; AOUO01000188; EOD67847.1; -; Genomic_DNA.
DR RefSeq; WP_003079574.1; NZ_AOUO01000188.1.
DR AlphaFoldDB; R1G8W6; -.
DR PATRIC; fig|1292037.4.peg.2712; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 3229174at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000014139; 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..604
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 723 AA; 77260 MW; C92A8804F9FC8C2B CRC64;
MAESKTIRWE QDSDGIVTLT LDDPNQSANT MNAEFRESLG VTVDRLEAEK DNITGVVITS
AKKTFFAGGD LNDLIQAKPE NAVELTEGSG AMKGQMRRIE QLGKPVVAAI NGAALGGGLE
IALATHHRIA ADVKGSQIGL PEVTLGLLPG GGGVVRTVRL LGIQSALLNV LLQGQRHRPA
KALELGLVHK LVGTVEELVP AAKAWIKANP EGGVQPWDVK GYKIPGGTPS NPSFAANLPA
FPANLRKQIK GANMPAPRAI LAAAIEGAQV DFDTAIQIET RYFIHLATGQ VSKNMTKAFF
FDLQTINSGG SRPDGFEKYT ARKVGVLGAG MMGAAIAYVS AKAGIDVVLK DVSQEAAEKG
KGYAEKLEQK ALSRGKTTQE KSDALLAKIK PTADPADFAG VDFVIEAVFE SVELKHKVFG
EIESVVNADA VLGSNTSTLP ITTLAEGVQR TEDFIGIHFF SPVDKMPLVE IICGEKTSPA
TLAKVFDYTL QIKKTPIVVN DSRGFFTSRV IGTFINEAVA ALGEGVEPAS IEQAGSQAGY
PAPPLQLMDE LTLTLPRKIR KETREAIEAA GGTWKAHASE TVIDRMVEEF DRKGRSTGAG
FYEYDSEGKR AGLWPGLRDA FKSGSAEVPF EDLKERMLFA EALETVKCFD EGVLTSVADA
NIGSIFGIGF PAWTGGVIQY INQYEGGLQG FVDRARELAA RYGDHFEPPA SLVEKAAKGE
IYE
//
