ID A0A1U6GMF5_9GAMM Unreviewed; 731 AA.
AC A0A1U6GMF5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=fadB1 {ECO:0000313|EMBL:SLJ84712.1};
GN ORFNames=DABAL43B_1517 {ECO:0000313|EMBL:SLJ84712.1};
OS Psychrobacter sp. DAB_AL43B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1028416 {ECO:0000313|EMBL:SLJ84712.1, ECO:0000313|Proteomes:UP000190084};
RN [1] {ECO:0000313|EMBL:SLJ84712.1, ECO:0000313|Proteomes:UP000190084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAB_AL43B {ECO:0000313|EMBL:SLJ84712.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; LT799838; SLJ84712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U6GMF5; -.
DR STRING; 1028416.DABAL43B_1517; -.
DR KEGG; psyc:DABAL43B_1517; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000190084; Chromosome i.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:SLJ84712.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 332..510
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 513..613
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 731 AA; 79578 MW; BBCB73C7F457E80B CRC64;
MTTNTAGSAK DSVDTINKLA NFSAQSDDDG IITVTIDQSD RKMNVIGDGF TGAFALLTDS
FTNDESAKGL ILTSAKDTFV VGADIDQLSK IETAEQAFDL VEDLKSSLRK LETSGKPVVA
AMTGTALGGG LEIALACHYR IAIDSPKTKL GLPEVKLGLL PGGGGTQRLP RLVGIQKALE
LMTQGLELRP KAAIDIGLID ATATDNDDML VQAKEWIKAN PKVQQPWDKK GFKIPGGNSM
HPKVVQVFSI APAMAHQKSH GNYPAITHIM SCVFEGCIVD IDTGLKIESR YFVACVLSPE
SRNMIGTLWT QLNNIKKGQS RPEGFERYKT KKVGILGAGM MGAGIAYVTA KAGIDVVLLD
TEIAGAEKGK AYSTTILDKA ISRKRSTEEK KQALLARIKP TVSYDDLADC DLVIEAVFEN
REIKAKCTQQ SEAVIPESAV YASNTSTLPI TGLAEASKRP QQFIGLHFFS PVDKMPLVEI
IVGEKTDDET LAKAFDYVVQ IGKTPIVVND SRGFYTSRVF GTYVSEGVAM LGEGVHPRSI
EVAGMKTGMP MPPLALQDEV SLSLALHVIE QQQKDMEAEG RTMDMPPSYD ILNTFVNEHD
REGKKNGKGF YDYPEKGDKH LWSELTTLYP TTAEQPSQQD LVDRLMFIQA NESAKCYEEN
VVRSVADTNI GSIFGWGFSP HQGGTLQFIN SMGVDKFVAR SRELAEQYGE RFEPANILVK
MAEKDEEFVD G
//
