ID A0A1Y2GSF8_9FUNG Unreviewed; 762 AA.
AC A0A1Y2GSF8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN ORFNames=BCR41DRAFT_421462 {ECO:0000313|EMBL:ORZ19290.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ19290.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ19290.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ19290.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:ORZ19290.1}.
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DR EMBL; MCFF01000014; ORZ19290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GSF8; -.
DR STRING; 64571.A0A1Y2GSF8; -.
DR InParanoid; A0A1Y2GSF8; -.
DR OrthoDB; 1359537at2759; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:InterPro.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR032259; HIBYL-CoA-H.
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 SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648}.
FT DOMAIN 393..544
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
FT REGION 656..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 84454 MW; 4C023AAD993CE73C CRC64;
MATDLEKYTE QATLPFSSSE LGAFHRFHAY NWDGDEHFQA GLRTITQAQP LPPSLSELLK
MKQYYFSTRL GTHINLDNYL SWRKHLEKPS DDPNVLIFKR FDEYDFDNDP RFQSGLPNIV
SQLVKDGKST LDKAALQKEM TKAKAFYYAR FIELFDFPAY LNWKELEKSQ DGPACPFAHL
WQNKSEGSSS ELAEDAQKFL TTTAPVSTGA LQIHIHSPAT KNVWTGVRLA KMNQAISDAN
DKDTITSILL TANSGAPTQD RRDPESLIVT KDEKWFSGGL VTSGSTEMQD KQDPAKFKEL
QRQYFSVVDQ LTAINCHHHK PVVCVADGIV SLSAAYLAFG SGGQRVITEN ATLSFTPLKA
IELPPNEALN PFAGLHLLAQ IQTHAKSDSG ARSLPKNIGH YLAFCPDNIL RGPDLRKLGL
ADFFISSSKK NDIEKAVLSV AGCPPPHTVQ AIRMALNAEV VYPGPPKIDV WRSEIKECFD
DAASLDDVVT KLEKYNNNWS KSIREYIASL EPVFAKLLFE AITKASEMAS FQERARLEYR
LNVRYKDYLL SKDTTAEDDI KDLQVFFEPI EEEESELFTF PFTEWIKEHG NENEFTNTVK
TNGNSIEEQD ATQACPYLRS KTDGDRHTAM PSDHPTIITG AELNDPEAVK TCPFLSAKKS
GQDSTASNST GVGVPDDHPK IPGVDFSDAK AAEACPFLAA KKAQDDDEKK DLQPVTATTS
PTTVTTAVSS TVPNDHPVIP GVDFSNPAAM ASCPFLASQK TK
//