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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//