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Database: UniProt
Entry: A0A101P078_9ACTN
LinkDB: A0A101P078_9ACTN
Original site: A0A101P078_9ACTN 
ID   A0A101P078_9ACTN        Unreviewed;       282 AA.
AC   A0A101P078;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KUN02538.1};
GN   ORFNames=AQI95_27430 {ECO:0000313|EMBL:KUN02538.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN02538.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN02538.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN02538.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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:KUN02538.1}.
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DR   EMBL; LMWN01000038; KUN02538.1; -; Genomic_DNA.
DR   RefSeq; WP_067129316.1; NZ_KQ948216.1.
DR   AlphaFoldDB; A0A101P078; -.
DR   STRING; 67386.AQI95_27430; -.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000053127; 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; IPR006180; 3-OHacyl-CoA_DH_CS.
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:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053127}.
FT   DOMAIN          4..183
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          186..282
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         48
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         55
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         118
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   SITE            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   282 AA;  30278 MW;  CBC1DC02AE1CD0CA CRC64;
     MARKLAVIGA GLMGSGISQV AARAGWDVVM RDVTDEALTR GTDGIKASFD KFVSKGKMEA
     HDADTALARI TTTTDLDAAA DADIVVEAVF EKLEVKHEIF RALDKLVRPD TVLASNTSAI
     PITKIAAATE HPERVVGVHF FSPVPMMRLV ELVRGYKTSD ETLATAREFA ESVGKTCIVV
     NRDVAGFVTT RLISALVVEA IKLYESGVAT AEDIDLACKL GFGHAMGPLA TTDLTGVDIL
     LHATGNIYTE SQDEKFAPPE LMRRMVDAGD IGRKSGQGFY KY
//
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