ID A0A1W1Z308_9LACT Unreviewed; 302 AA.
AC A0A1W1Z308;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:SMC42471.1};
GN ORFNames=SAMN04487984_1059 {ECO:0000313|EMBL:SMC42471.1};
OS Aerococcus suis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=371602 {ECO:0000313|EMBL:SMC42471.1, ECO:0000313|Proteomes:UP000243884};
RN [1] {ECO:0000313|Proteomes:UP000243884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21500 {ECO:0000313|Proteomes:UP000243884};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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; FWXK01000005; SMC42471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1Z308; -.
DR STRING; 371602.SAMN04487984_1059; -.
DR Proteomes; UP000243884; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
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; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43561; -; 1.
DR PANTHER; PTHR43561:SF3; HYDROXYACYL-COENZYME A DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000243884}.
FT DOMAIN 4..183
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 186..284
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 139
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 302 AA; 33459 MW; 734562936FF4A652 CRC64;
MFKNITIAGG GVLGSQIAFQ TAYFGYEVKL YDINEDAVKA ADEKLDKLVA RYTEFFGDQS
KAENARKRIS TTANLEDALQ DSDLLIEAIP EKKEIKADFY TNVAKVAPEK TIFASNSSMM
VPSDFAEYTG RPEKFLALHF ANEVWKNNIG EVMGHAGTDK KYEEEVLKFA ESIGLIPLHV
LKETPGYISN SILVPFLEAG KKLYVSGVAD IETIDKTWMA ATGMNMGPFG ALDVIGLNTD
YSITLANAEK NNDELLLKFA NLMKEEYIDK GNLGVSTGKG FYTYPNPSFK SEDFIVRQGQ
EK
//
