3HIDH_PONAB
ID 3HIDH_PONAB Reviewed; 336 AA.
AC Q5R5E7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
DE Flags: Precursor;
GN Name=HIBADH;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; CR860914; CAH93019.1; -; mRNA.
DR RefSeq; NP_001127621.1; NM_001134149.1.
DR RefSeq; XP_009241202.1; XM_009242927.1.
DR AlphaFoldDB; Q5R5E7; -.
DR SMR; Q5R5E7; -.
DR STRING; 9601.ENSPPYP00000019832; -.
DR Ensembl; ENSPPYT00000020615; ENSPPYP00000019832; ENSPPYG00000017693.
DR GeneID; 100174700; -.
DR GeneID; 100189883; -.
DR CTD; 11112; -.
DR eggNOG; KOG0409; Eukaryota.
DR GeneTree; ENSGT00940000155255; -.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; Q5R5E7; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 812358at2759; -.
DR TreeFam; TF314043; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
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.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Branched-chain amino acid catabolism; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 37..336
FT /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000290341"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT BINDING 40..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 103..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 95
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 141
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 297
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
SQ SEQUENCE 336 AA; 35299 MW; DA243D775F84AF48 CRC64;
MAASLRLLGA ASGLRYWSRR LRPAAGSFAA VCSRSVASKT PVGFIGLGNM GNPMAKNLMK
HGYPLIIYDV FPDACKEFQD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL
KKVKKGSLLI DSSTIDPAVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVED
EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNMLLAISM IGTAEAMNLG IRLGLDPKLL
AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGAT LMAKDLGLAQ DSATSTKSPI
LLGSLAHQIY RMMCAKGYSK KDFSSVFQFL REEETF
