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Database: UniProt
Entry: A0A2M9HPQ6_9BIFI
LinkDB: A0A2M9HPQ6_9BIFI
Original site: A0A2M9HPQ6_9BIFI 
ID   A0A2M9HPQ6_9BIFI        Unreviewed;       337 AA.
AC   A0A2M9HPQ6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:PJM78794.1};
GN   ORFNames=CUU80_07435 {ECO:0000313|EMBL:PJM78794.1};
OS   Bifidobacterium scaligerum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM78794.1, ECO:0000313|Proteomes:UP000228755};
RN   [1] {ECO:0000313|EMBL:PJM78794.1, ECO:0000313|Proteomes:UP000228755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA   Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT   "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT   from tamarins, belonging to four potential novel Bifidobacterium species.";
RL   Submitted (NOV-2017) 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:PJM78794.1}.
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DR   EMBL; PGLQ01000004; PJM78794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9HPQ6; -.
DR   OrthoDB; 3229174at2; -.
DR   Proteomes; UP000228755; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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   Reference proteome {ECO:0000313|Proteomes:UP000228755}.
FT   DOMAIN          22..200
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          205..303
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            158
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   337 AA;  36539 MW;  6B65D5317F0A180E CRC64;
     MAQEQDGTLP LNVKNAKDIK VIANVGTGTM GHAIALQFAL AGYETRLVGR SEASLDRSMG
     RIRADAETFA GAGLLHAGET VEDVLARITP IVGYEQGVAG ADFVIESVAE NLEVKQSVWR
     EIEKFAPKDA IFATNTSGLS PTAIQSVLER PERFVVAHFW NPAQLMPLVE VVPGAHTDPH
     VVDVTFDLMN LIGKKPAKIK KESLGFVGNR LQMAVLREEF HIIQEGIADA ATVDDVMKYS
     LGRRWNLVGP VASIDLGGLD VFYNISTYLF DDMDNGTGPS PLLAEKVKEG NLGAKTGRGF
     FSWQGEDGKR VIEQRDKALL RALKEDAAEV GKQPAEV
//
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