ID B9L5H1_THERP Unreviewed; 737 AA.
AC B9L5H1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN OrderedLocusNames=trd_A0098 {ECO:0000313|EMBL:ACM06621.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OG Plasmid Tros {ECO:0000313|Proteomes:UP000000447}.
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM06621.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM06621.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RC PLASMID=Tros {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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 -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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DR EMBL; CP001276; ACM06621.1; -; Genomic_DNA.
DR RefSeq; WP_012642608.1; NC_011961.1.
DR AlphaFoldDB; B9L5H1; -.
DR KEGG; tro:trd_A0098; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_010448_0_0_0; -.
DR OrthoDB; 145983at2; -.
DR Proteomes; UP000000447; Plasmid Tros.
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 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; 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 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ACM06621.1};
KW Plasmid {ECO:0000313|EMBL:ACM06621.1}.
FT DOMAIN 4..183
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 186..281
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 737 AA; 79833 MW; E78105A9D1060AEE CRC64;
MIEKVGVLGA GSMGAAVAAL AASAGLEVIL LDVKGEGDPA GPARRGLERA VKQRAFLDPS
AAGRVQVGNV EDDLPLLAGC DWVLEAIIEE REAKRTLFQR LAAILPPQTI VTTNTSTFTL
HALLPDELGA WRDRFFVTHF FNPPRALLLC EVTAFPEGEG ERFFGFVRFL EQRLGRRALL
VRDTPGFVAN RFGIYALAHA VRLTTELGLT PEEVDALTGP LLGRPRSATF RTIDLTGVDI
LVLGTRSLQE STGDDYAVPD WILELYQAKR LGDKTGGGIY RREGEQQLTY DPLQHGDRPF
RPAAIPGLDD LLRQPFPERL VGALDLPSPY GDYVRHLLGR TFGYVLARTR DAARDIASVD
RALEWGFGWA AGPYAQMQFL GLERVRELLQ DAGVPVSDLL ALAEERGGFF RDGRVLDPAS
GELIPEEQLP STRRTRQIRL REALDRQGTH DLGDGILAVR VRSLEALPEL VAGTLAHGPS
ALVLVPAFAG LGYPYEDLLE LAERGEWETI EQRLVTLQEA LRAVARLPVP VVTALDGEGR
GAATTLALWS DATVAFLTTP LGFPGATVGL LPLGALTALR VRAEAREYGL QAPLRAEFGV
VSALTAFLAS ERVESAQRAG ISGLLGDRWL ATMDRDGLLD AAAGLARALA RSVPRRPLGD
AVELGTAGEQ VTAGLRLAEL EPATRQVVEA LVRAVRRSGN VDDLLAAERA VLRELLRDGE
YRQRARATLQ ALAAARR
//
