ID W4V324_9FIRM Unreviewed; 283 AA.
AC W4V324;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=3-hydroxyacyl-coa dehydrogenase {ECO:0000313|EMBL:GAE87601.1};
GN ORFNames=JCM21531_986 {ECO:0000313|EMBL:GAE87601.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE87601.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE87601.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE87601.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
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:GAE87601.1}.
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DR EMBL; BAVR01000008; GAE87601.1; -; Genomic_DNA.
DR RefSeq; WP_038287413.1; NZ_BAVR01000008.1.
DR AlphaFoldDB; W4V324; -.
DR STRING; 1294263.JCM21531_986; -.
DR OrthoDB; 9815331at2; -.
DR Proteomes; UP000019109; 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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 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 NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019109}.
FT DOMAIN 5..184
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 187..283
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 141
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 283 AA; 31698 MW; CEE7D13A4DEFAEF9 CRC64;
MQNKTIAIIG AGVMGSATAL HIARYGYRVI LKDISTEILE KARKNIRNEY RSACMMNKEY
SSVSLDTILQ NISFQEDYNG VEAADIIIEN ITEDMEKKIA EYKRLGEVCN KDAFFALNTS
CISITKLASY LPDPQRVIGT HLMNPVPLKE MVEVIKGYHT SKETEEEIVS FLKSLGKKPI
VIGDLPGFVS NRISHLFMNE AAFIVQDGIA TPEQVDNIIK LGFNHKMGPL ETADLIGLDT
VVNSLEVLYE SYQDPKYRCC PLLKKMVDAG HLGRKSGKGF YKY
//
