ID A0A088QGZ8_9CORY Unreviewed; 743 AA.
AC A0A088QGZ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Enoyl-CoA hydratase/isomerase family protein {ECO:0000313|EMBL:AIN82757.1};
GN ORFNames=DR71_927 {ECO:0000313|EMBL:AIN82757.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN82757.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN82757.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) 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: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; CP008913; AIN82757.1; -; Genomic_DNA.
DR RefSeq; WP_038626854.1; NZ_CP008913.1.
DR AlphaFoldDB; A0A088QGZ8; -.
DR STRING; 1487956.DR71_927; -.
DR GeneID; 64052137; -.
DR KEGG; coa:DR71_927; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_0_11; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000029247; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:AIN82757.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000029247}.
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 743 AA; 79999 MW; 5F0E3B5969AC24C2 CRC64;
MSTDNMFRWD QDDAGIVTLT MDDPNAPVNT MNKTFQDDIR ATVERLENEI GDGSETSIKG
IVITSAKKTF FAGGDIKQMS KATEDDAADM FNMVEDMKAS LRRLEKLPVP IVAAINGAAL
GGGLEVALAA NHRVAADARG SKIGLPEVTL GLLPGGGGVS RVVRMLGIQD ALMKVILTGA
QMNPGKALAA GLVDEVVAPE QLIDTARAWL TSEDAKAAQP WDEKGFKIPG GDPKTPKFAM
NLPSFPANLT KQLKGSPMKA PRLAMQAAIE GSQVDIDTAL RVESRYFTEL VTGTQSKNMM
QAFFFDLNHA QGGGSRPLQA DGTPYPKREF KKVAVVGAGM MGAGIAYVCA KAGMEVVLKD
ISLENAERGK AYSEGLEAKA LKRGRTTEEK SAALLNRIKP TESYDDLSDV DLVIEAVFEN
TDLKHKVHAE IEAAVPETCI LGSNTSTLPI TELASHVKRE KDFIGLHFFS PVDKMQLIEI
ISGDNTDPAI LAASLDFAVA IRKIPIVVTD SRGFYTSRVI GTVINEALRM VAEGYDPAII
EAAGRQAGYP APQLQLADEL NLKLMEKIAG ETRAAAEAAG QSLDEGGVPA LVEAMLHKFE
RPGKLEGKGF YEYVDGKRSG LWPGLFNELR EELNITPIAP EDTDLQELVD RMLFIEAIET
QKCVDEGVLL HDADGNIGSI FGIGYPAWTG GTRQFIKNYD GATVVDPAAA RPERRGVAGF
VERAEELAAK HGERFNAPES LKK
//
