ID B4FQL1_MAIZE Unreviewed; 376 AA.
AC B4FQL1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE Short=HIB-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE Short=HIBYL-CoA-H {ECO:0000256|RuleBase:RU369070};
DE EC=3.1.2.4 {ECO:0000256|RuleBase:RU369070};
DE AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase {ECO:0000256|RuleBase:RU369070};
GN ORFNames=ZEAMMB73_Zm00001d046456 {ECO:0000313|EMBL:AQL04330.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF84404.1};
RN [1] {ECO:0000313|EMBL:ACF84404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACF84404.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EMBL:AQL04330.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL04330.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC catabolite. Has high activity toward isobutyryl-CoA. Could be an
CC isobutyryl-CoA dehydrogenase that functions in valine catabolism.
CC {ECO:0000256|RuleBase:RU369070}.
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|RuleBase:RU369070};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|RuleBase:RU369070}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU369070}.
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DR EMBL; BT039399; ACF84404.1; -; mRNA.
DR EMBL; BT063945; ACN28642.1; -; mRNA.
DR EMBL; CM000785; AQL04330.1; -; Genomic_DNA.
DR RefSeq; NP_001140702.1; NM_001147230.1.
DR AlphaFoldDB; B4FQL1; -.
DR GeneID; 100272777; -.
DR KEGG; zma:100272777; -.
DR OMA; AYRNNEH; -.
DR OrthoDB; 3639304at2759; -.
DR ExpressionAtlas; B4FQL1; baseline and differential.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd06558; crotonase-like; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR032259; HIBYL-CoA-H.
DR PANTHER; PTHR43176:SF5; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-LIKE PROTEIN 4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF16113; ECH_2; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369070}.
FT DOMAIN 20..365
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 376 AA; 40702 MW; C209876BB778971D CRC64;
MAATAADEFV KGRVFPNGVA VITLDRPKAL NAMNLEMDVR YKALLDEWET NPSVKCILVE
SSSSRAFSAG GDVKRLANDC TMPEIIEVFT VEYSLICKIH EYAKPYICLM DGVTMGFGIG
LSGHGRYRII TERTLLAMPE NGIGLFPDVG FAYIGAKAPG GGAVGVYLGI TGKRISSPAD
AMFIGLGTHY VPSANLGSLK ESLLSANFTN DPHRDVESVL TGYKKEPESE PQLKKLLPYI
ISSFSPDKSV AESVEELKKC SRSGDAAVAE WANEALAGIE KGAPFSLCLT QKHFSQVASA
YGTSEHYLSK LAGVMKLEYR IALRSSIRND FVEGVRAVLV DKDQNPKWNP ATLEEVNMAE
VESVFEPLGA EAELSV
//