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Database: UniProt
Entry: A0A1A7QS14_9FLAO
LinkDB: A0A1A7QS14_9FLAO
Original site: A0A1A7QS14_9FLAO 
ID   A0A1A7QS14_9FLAO        Unreviewed;       797 AA.
AC   A0A1A7QS14;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:RAJ27822.1};
GN   ORFNames=LX77_00396 {ECO:0000313|EMBL:RAJ27822.1};
OS   Gelidibacter algens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gelidibacter.
OX   NCBI_TaxID=49280 {ECO:0000313|EMBL:RAJ27822.1, ECO:0000313|Proteomes:UP000248987};
RN   [1] {ECO:0000313|EMBL:RAJ27822.1, ECO:0000313|Proteomes:UP000248987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12408 {ECO:0000313|EMBL:RAJ27822.1,
RC   ECO:0000313|Proteomes:UP000248987};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-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   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
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:RAJ27822.1}.
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DR   EMBL; QLLQ01000001; RAJ27822.1; -; Genomic_DNA.
DR   RefSeq; WP_066438201.1; NZ_QLLQ01000001.1.
DR   AlphaFoldDB; A0A1A7QS14; -.
DR   STRING; 49280.A9996_17410; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000248987; 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:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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; IPR001753; Enoyl-CoA_hydra/iso.
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; PF00378; ECH_1; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          8..206
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          209..308
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   797 AA;  88350 MW;  92F7B15C7B3D8D30 CRC64;
     MSKRRIKKVA IIGSGIMGSG IACHFANIGV DVLLLDIVPR ELTDAEKAKG LTLEDKAVRN
     RIVNDSLTAS LKSKPSPIYH PSFASRITTG NLEDDIAKVK DVDWIMEVVV ERLDIKKQVF
     EKLEKYRTPG TLITSNTSGI PIHFMSEGRS EDFQKHFCGT HFFNPARYLK LFEIIPGPKT
     SQEVLDFLKI YGEKFLGKTS VIAKDTPAFI GNRIGIFGIQ SLFHQVKEMD LTVEEVDKLT
     GPVIGRPKSA TFRTVDVVGL DTLVHVANGI YENCPEDEAH ELFKLPDFIN TMMENKWLGS
     KTGQGFYKKE GKDIRTLDLN TLEYRDRKSA KFATLELTKT VDKVVDRFPI LISGKDKAGE
     FYRKNFAAMF AYVSNRIPEI TDELYKIDDA MKAGFGWEHG PFQIWDAVGV EKGIELIKAE
     GLEPAAWVNE MLESGNKSFY TVKEGSTFFY DIPSKKQEKV PGQDAFIILD NIRKSKEVYK
     NSGVVVEDLG DGILNVEFQS KMNTIGGDVL SGLNKAIDIA EKDFAGLVVG NQAANFSVGA
     NIGMIFMMAA EQEYDELNAA IKYFQDSMMR MRYSAIPTIA APHGMALGGG CELSMHADKV
     VAAAETYMGL VEFGVGVIPG GGGSKEMALR AQDLFRKGDV ELNTLQEYFL TIAMAKVSTS
     AYEAFDLGVL QKGKDIIVVN KDRQLAMAKA HAKLMADAGY TQPIKRTDIK VLGRQALGMF
     MVGTDAMEDS NYISAHDQKI ANKLAYVMAG GDLSEPTLVS EQYLLDLERE AFLSLATERK
     TLERIQHMLK TGKPLRN
//
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