ID A0A364L1U8_9EURO Unreviewed; 782 AA.
AC A0A364L1U8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN ORFNames=BHQ10_005713 {ECO:0000313|EMBL:RAO69701.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69701.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO69701.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO69701.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001709};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528}.
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:RAO69701.1}.
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DR EMBL; MIKG01000010; RAO69701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364L1U8; -.
DR STRING; 1196081.A0A364L1U8; -.
DR OrthoDB; 3639304at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 3.40.1370.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR032259; HIBYL-CoA-H.
DR InterPro; IPR002136; Ribosomal_uL4.
DR InterPro; IPR013005; Ribosomal_uL4-like.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR NCBIfam; TIGR03953; rplD_bact; 1.
DR PANTHER; PTHR43176:SF3; 3-HYDROXYISOBUTYRYL-COA HYDROLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF16113; ECH_2; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 349..692
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..617
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 43..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 87683 MW; B4F3BF342F2CEE25 CRC64;
MPSSEALRTL RWLTRSVNGA LQQPQTVIQG CASSSTRLMA TVSEASSKTS TQTDSRTPWQ
PPAPALVTIH SFPSMTPLRF EEYSPDHLLV PLRRDLLHRA VVYEGDKTRQ GTASTKWRDD
VHGSGRKLAP QKGTGHARVG DKKSPIRRGG GVAHGPHPRD FSTDLPRKMY DKAWRIALSY
RYTRGSLLVV DNIAMPENSS PWFWKRFFEA TPWGKHHGGC TFVKDRMDED LFSAIAEFHQ
HSRILDRPDL DVKDILKNGK MIIEKKALDK ILRDHSRDLP TPPPKATYPE GIASTPLSRL
SRSTFSAMPL RAKVTNPAFA SKMSQSTSAA SNPAVDSDDV LFYSTYGLRL IELNRPKKLN
SLNGSMCQQI IPRLLEWENS QLANIIMISG RGEKALCAGG DVAALAVNNK EGPEGVKRSQ
DYFAQEYQLD HLIATYSKPF VAVMDGITMG GGVGLSVHAP FRIATERTLF AMPETTIGFF
PDVGGSFFLP RLDGEIGTYL ALTSERLNGV QAFYTGIATH YVDSSVLGNL TNRLAELVFK
DYANLQERND LVNKTIAEFA TGLPSIEQEP IHLRYKLRQA IDRCFKYNTV EEIVKALEKE
EDQKEWAQKT LETLTSRSPT SLKVTLRQLR LGKNWSIKET FQREHAIASV FMNHPDFVEG
VSARLISKPA RTPEWQPSRL EDVTSQAVDA FFKIEGEPLS TFHDNDYKQY PHAKYALPTE
ADIEAFVRSN RTTGADAVKE FVQNWGQKEG VKAKVSEVLG RRTEKTDKGL RWIEEEGKED
KE
//
