ID A0A0N4ZQF7_PARTI Unreviewed; 297 AA.
AC A0A0N4ZQF7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|ARBA:ARBA00012991, ECO:0000256|RuleBase:RU910714};
DE Short=HIBADH {ECO:0000256|RuleBase:RU910714};
DE EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991, ECO:0000256|RuleBase:RU910714};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001075500.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001075500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000062,
CC ECO:0000256|RuleBase:RU910714};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|ARBA:ARBA00005109, ECO:0000256|RuleBase:RU910714}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
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DR AlphaFoldDB; A0A0N4ZQF7; -.
DR STRING; 131310.A0A0N4ZQF7; -.
DR WBParaSite; PTRK_0001075500.1; PTRK_0001075500.1; PTRK_0001075500.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000038045; Unplaced.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01692; HIBADH; 1.
DR PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456,
KW ECO:0000256|RuleBase:RU910714};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU910714};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU910714}.
FT DOMAIN 5..161
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 166..293
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 297 AA; 31678 MW; FD011742351B1613 CRC64;
MSGLIGFVGL GNMGAFMVKN LMKNGKKVIV YDINKKILEQ FKSLGAEVAK HPADISAASK
MIVTMVPEGK DVKHTFTADN GLLKNNQEGT LYIDSSTIAQ SDVFDIADIV KKHKSTFIDA
PVSGGVTGAE AGTLTFMIGA DGENYKKACE LLQYMGKNLV KCEKLGSGQA AKICNNMLLA
IHMIGVSETM NLGMKMGLDA KLLASIINTS TGRCWSGDTY NPVPGVIEGV PSSRGYSGGF
GNALIAKDLG LAQTASTLTK SPTPLGSLAH QIYRILAKDK EYQGKDFSSV YQYIKDN
//
