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Database: UniProt
Entry: A0A087DPV4_9BIFI
LinkDB: A0A087DPV4_9BIFI
Original site: A0A087DPV4_9BIFI 
ID   A0A087DPV4_9BIFI        Unreviewed;       320 AA.
AC   A0A087DPV4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KFI97554.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:KFI97554.1};
GN   ORFNames=BSTEL_0275 {ECO:0000313|EMBL:KFI97554.1};
OS   Bifidobacterium stellenboschense.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI97554.1, ECO:0000313|Proteomes:UP000029004};
RN   [1] {ECO:0000313|EMBL:KFI97554.1, ECO:0000313|Proteomes:UP000029004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI97554.1,
RC   ECO:0000313|Proteomes:UP000029004};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KFI97554.1}.
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DR   EMBL; JGZP01000012; KFI97554.1; -; Genomic_DNA.
DR   RefSeq; WP_034528382.1; NZ_JGZP01000012.1.
DR   AlphaFoldDB; A0A087DPV4; -.
DR   STRING; 762211.BSTEL_0275; -.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 3229174at2; -.
DR   Proteomes; UP000029004; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; 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:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 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   ECO:0000313|EMBL:KFI97554.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029004}.
FT   DOMAIN          10..189
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          194..292
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            147
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   320 AA;  34670 MW;  A6BD5C3ECB04E6F2 CRC64;
     MSKGIDDIRT VANVGTGTMG HAIALQFALA GYETRLVGRS DKSLDRATTN IRRDATAFAD
     AGLLKPGETV DDVLARITPV VGYERGVAGA DFVIESVAEN LDVKKSVWAE VERFAPEDAI
     FATNTSGLSP TAIASALARP ERFVVAHFWN PAQLMPLVEV VPGEKTTKEV VDTTFDLMTR
     IGKKPARLNK ESLGFIGNRL QMAVLREEFH IIQEGIADAA TVDDVMKYSL GRRWNLVGPV
     ASIDLGGLDV FYNISTYLFD DMDNGTGPSP LLAEKVKAGD LGAKTGRGFF SWQGEDGRRV
     IAQRDQVLLR ALKDDAAEGR
//
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