ID A0A1C6PSR2_9ACTN Unreviewed; 330 AA.
AC A0A1C6PSR2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SCK46275.1};
GN ORFNames=H180DRAFT_04110 {ECO:0000313|EMBL:SCK46275.1};
OS Streptomyces sp. WMMB 322.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK46275.1, ECO:0000313|Proteomes:UP000182082};
RN [1] {ECO:0000313|EMBL:SCK46275.1, ECO:0000313|Proteomes:UP000182082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK46275.1,
RC ECO:0000313|Proteomes:UP000182082};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
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DR EMBL; FMHI01000013; SCK46275.1; -; Genomic_DNA.
DR RefSeq; WP_074466899.1; NZ_FMHI01000013.1.
DR AlphaFoldDB; A0A1C6PSR2; -.
DR STRING; 1286821.GCA_001418285_04091; -.
DR Proteomes; UP000182082; 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; 2.
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}.
FT DOMAIN 13..217
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 220..316
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 64..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 174
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 330 AA; 34998 MW; 851CC8F659338CD9 CRC64;
MGERKDIGPA RPVGVVGAGT MGAGVAQCFA QTGHRVVVVD PDAEARRGGA ARLRAGLRLK
SLLRGRQTDG ARRQSGLPQN GGTPGQAEQS RAAEREEPAD PAALVEFTAD LSDLAQASFV
VECAREREPL KEEILRALDE LCPAETIFAS CTSAIPIARL GSFTGRPDRV VGTHFMNPAP
LKDAVEVARS PHTSDDTLAR TLRILEGIGK SPLVVGDGPG FVTNRVLMLT VNEAAYVLHG
GTADAETVDR VFQECFGHPM GPLRTGDLIG LDTVVDTLDV LREHTGDERF QPCPLLAELV
ADGSVGRKAG RGFHHYPKSP LVPRGETSHG
//
