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Database: UniProt
Entry: A0A0A8JHS1_BACSX
LinkDB: A0A0A8JHS1_BACSX
Original site: A0A0A8JHS1_BACSX 
ID   A0A0A8JHS1_BACSX        Unreviewed;       283 AA.
AC   A0A0A8JHS1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:BAQ09872.1};
GN   ORFNames=OXB_1401 {ECO:0000313|EMBL:BAQ09872.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ09872.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAQ09872.1, ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ09872.1,
RC   ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL   Genome Announc. 3:e00025-15(2015).
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; AP013294; BAQ09872.1; -; Genomic_DNA.
DR   RefSeq; WP_041073084.1; NZ_AP013294.1.
DR   AlphaFoldDB; A0A0A8JHS1; -.
DR   STRING; 98228.OXB_1401; -.
DR   KEGG; baco:OXB_1401; -.
DR   HOGENOM; CLU_009834_2_0_9; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000031651; Chromosome.
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   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031651}.
FT   DOMAIN          5..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         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   283 AA;  31389 MW;  C4227A447A494CCA CRC64;
     MEIKKVMVIG AGQMGGGIAQ VCAQAGFEVT LNDIKEELYD RGLAVITKNL SRNVEKGRMT
     EDEKNEVLGR ITKSLDLQDA SGVDMVIEAA VENMDIKKSI FEQLDKIAPD HAILATNTSS
     LPITEIAAVT DRPEKVIGMH FMNPVPVMKL VEIIRGLATA DEVYQAVEEM TVKLDKTPVE
     VNDFPGFVAN RILMPMINEA IYTLYEGVAK EEAIDEVMKL GMNHPMGPLQ LADFIGLDTC
     LYIMETLYEG FGDSKYRPCP LLRKYVKAGW LGKKSGRGFY VYE
//
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