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3HID3_ARATH
ID   3HID3_ARATH             Reviewed;         318 AA.
AC   Q949M8; Q9C990;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Probable 3-hydroxyisobutyrate dehydrogenase-like 3, mitochondrial;
DE            Short=HIBADH-like;
DE            EC=1.1.1.31;
GN   OrderedLocusNames=At1g71180; ORFNames=F23N20.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC         oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:57945; EC=1.1.1.31;
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51699.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC016972; AAG51699.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE35169.1; -; Genomic_DNA.
DR   EMBL; AY051005; AAK93682.1; -; mRNA.
DR   EMBL; AY113980; AAM45028.1; -; mRNA.
DR   PIR; E96736; E96736.
DR   RefSeq; NP_565014.1; NM_105787.2.
DR   AlphaFoldDB; Q949M8; -.
DR   SMR; Q949M8; -.
DR   STRING; 3702.AT1G71180.1; -.
DR   iPTMnet; Q949M8; -.
DR   PaxDb; Q949M8; -.
DR   PRIDE; Q949M8; -.
DR   ProteomicsDB; 245156; -.
DR   EnsemblPlants; AT1G71180.1; AT1G71180.1; AT1G71180.
DR   GeneID; 843458; -.
DR   Gramene; AT1G71180.1; AT1G71180.1; AT1G71180.
DR   KEGG; ath:AT1G71180; -.
DR   Araport; AT1G71180; -.
DR   TAIR; locus:2026351; AT1G71180.
DR   eggNOG; KOG0409; Eukaryota.
DR   HOGENOM; CLU_035117_1_0_1; -.
DR   InParanoid; Q949M8; -.
DR   OMA; METPYPK; -.
DR   OrthoDB; 812358at2759; -.
DR   PhylomeDB; Q949M8; -.
DR   BioCyc; ARA:AT1G71180-MON; -.
DR   UniPathway; UPA00362; -.
DR   PRO; PR:Q949M8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q949M8; baseline and differential.
DR   Genevisible; Q949M8; AT.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029154; NADP-bd.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..318
FT                   /note="Probable 3-hydroxyisobutyrate dehydrogenase-like 3,
FT                   mitochondrial"
FT                   /id="PRO_0000421119"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000250"
FT   BINDING         35..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  33378 MW;  5566711F836645D3 CRC64;
     MFYQSSSSLT QILHSFCGNT EMETPYPKLI DPSKTRIGWI GIGIMGSAMV SHIIAAGYSV
     TVYARDLRKT KDLQTKGARI ANSPKELAEM SDVVFTIVGN FNDVRSLLLG DDGVLSGLTP
     GGVTVDMTSS KPGLAREIHA EARRRNCWAV DAPVSGGDAG AREGTLGIFA GGDSEIVEWL
     SPVMKNIGTV TYMGEAGSGQ SCKIGNQIAG ASNLVGLAEG IVFAEKAGLD TVKWLEAVKD
     GAAGSAVMRL FGEMIVKRDY RATGFAEYMV KDLGMAAEAA MPGAALSKQL FTGMVANGDG
     KLGIQGVVSV IRRLNGIS
 
 
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