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Database: UniProt
Entry: A0A1M6AY81_9CLOT
LinkDB: A0A1M6AY81_9CLOT
Original site: A0A1M6AY81_9CLOT 
ID   A0A1M6AY81_9CLOT        Unreviewed;       278 AA.
AC   A0A1M6AY81;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SHI41391.1};
GN   ORFNames=SAMN02745176_00177 {ECO:0000313|EMBL:SHI41391.1};
OS   Lutispora thermophila DSM 19022.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX   NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHI41391.1, ECO:0000313|Proteomes:UP000184442};
RN   [1] {ECO:0000313|EMBL:SHI41391.1, ECO:0000313|Proteomes:UP000184442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19022 {ECO:0000313|EMBL:SHI41391.1,
RC   ECO:0000313|Proteomes:UP000184442};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; FQZS01000003; SHI41391.1; -; Genomic_DNA.
DR   RefSeq; WP_073023532.1; NZ_FQZS01000003.1.
DR   AlphaFoldDB; A0A1M6AY81; -.
DR   STRING; 1122184.SAMN02745176_00177; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000184442; 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:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
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:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 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:UP000184442}.
FT   DOMAIN          2..177
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          180..276
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         43
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         50
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         113
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   SITE            134
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   278 AA;  30424 MW;  08B5BF77DD00B5A3 CRC64;
     MKVFVVGSGT MGTGIVQTFA QAGIEVTMRE RTPGKGMNVI TKSLDKLVQK GKMAEEEKNR
     ILGNIKAVQN LEEAKDADLI IEAAVEELHL KKELFAELDK ICKPEAILAT NTSSLSITEI
     ASATNRPDKV IGMHFFNPVP MMKLVEVIKG IATSQETRDK IFEISEKVGK KPIEVEEAPG
     FVVNRILIPM INEAVGILAD GVAKAEDIDE AMKLGANHPM GPLALADLIG NDVCLAIMEV
     LYTEFGDSKY RPHPLLRKMV RGNLLGRKTG KGFYDYSK
//
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