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Database: UniProt
Entry: B4FQL1_MAIZE
LinkDB: B4FQL1_MAIZE
Original site: B4FQL1_MAIZE 
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
//
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