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Database: UniProt
Entry: A0A429X6X6_9BACI
LinkDB: A0A429X6X6_9BACI
Original site: A0A429X6X6_9BACI 
ID   A0A429X6X6_9BACI        Unreviewed;       794 AA.
AC   A0A429X6X6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:RST58953.1};
GN   ORFNames=D5F11_015015 {ECO:0000313|EMBL:RST58953.1};
OS   Siminovitchia terrae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX   NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST58953.1, ECO:0000313|Proteomes:UP000287296};
RN   [1] {ECO:0000313|EMBL:RST58953.1, ECO:0000313|Proteomes:UP000287296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29736 {ECO:0000313|EMBL:RST58953.1,
RC   ECO:0000313|Proteomes:UP000287296};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
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:RST58953.1}.
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DR   EMBL; QYTW02000015; RST58953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429X6X6; -.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000287296; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-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   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          7..205
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          208..305
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          491..620
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
SQ   SEQUENCE   794 AA;  87792 MW;  1CCA608BEC60E3D3 CRC64;
     MSFRIRKAAV LGSGVMGSGI AAHLANVGIP TLLLDIVPKE LTAREKAKGL TLEDREVRNR
     NTEEALKRLL KQKPAPLASK KNLNLITAGN LEDDLDQLKD VDWVIEVVVE NLEVKQKVFE
     QIDHCRKKGS IISSNTSGIS VEAMSEGRSD DFQKHFLGTH FFNPPRYLKL LEVIPTQKTA
     PEVLEFMKRF GEDVLGKGVV VAKDTPNFIA NRIGTYGLLI AVREMLKGGY SIGEVDSITG
     TLIGRPKSAT FRTLDVVGLD TFIHVANNVY ELVDGEEKEV FEVPGFMNKM REKGWLGSKS
     GQGFYVKKGK EILQLNPETF EYEPRKKFKT PGLELAKQEK GTKRKMKALM YSEDPAGKLL
     WNITAPVLAI SAELLGEIAD DIVAIDQAMK WGFGWELGPF ETWDAIGLEN SVAKMEQEGI
     KVPGWVKDML DGGHTSFYKE VDGIEYYFSN GEYKEIPKNP KVIDLKLLKK QGKVLKKNSG
     ASVIDVGDEV LLLEFHSKSN AIGFDIIQML NYAIEETERN YKGLIIGNQG KNFCVGANIA
     MILMAAQDDD IFEVDMVVRQ FQQAMMKIKY SEKPVVTAPF GMTLGGGSEV CLPSAHIQAS
     METYMGLVET GVGLIPGGGG NKELYIKTLK SMDNNVEFNL QQVANKVFET IAMAKVSTSA
     EEAVENNFLN QADGISVNGD HLIYDAKQAV LSLHEQGYKP PVREKIPVTG ETGYAALLLG
     AEAMKLSGYI SEHDMKIAKK LAYVIAGGKV PYGTMVDEQY LLDLEKEAFL SLVAEPKSQQ
     RMQHMLVKGK PLRN
//
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