3HIDH_DICDI
ID 3HIDH_DICDI Reviewed; 321 AA.
AC Q54CX6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
DE Flags: Precursor;
GN Name=hibA; ORFNames=DDB_G0292566;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
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DR EMBL; AAFI02000194; EAL61086.1; -; Genomic_DNA.
DR RefSeq; XP_629544.1; XM_629542.1.
DR AlphaFoldDB; Q54CX6; -.
DR SMR; Q54CX6; -.
DR STRING; 44689.DDB0216217; -.
DR PaxDb; Q54CX6; -.
DR EnsemblProtists; EAL61086; EAL61086; DDB_G0292566.
DR GeneID; 8628802; -.
DR KEGG; ddi:DDB_G0292566; -.
DR dictyBase; DDB_G0292566; hibA.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; Q54CX6; -.
DR OMA; WSSEVNN; -.
DR PhylomeDB; Q54CX6; -.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00362; -.
DR PRO; PR:Q54CX6; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Branched-chain amino acid catabolism; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..321
FT /note="Probable 3-hydroxyisobutyrate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000327881"
FT ACT_SITE 192
FT /evidence="ECO:0000250"
FT BINDING 23..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 86..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 33936 MW; 10F0626EFAB0AB7A CRC64;
MFSSKKSLLL FKNVRYMSTS SSKTVGFIGL GNMGGHQAIN LIKKGHNLIV FDMSKDNMNR
LKEKGAKIAN SPAEVAKEAD VIVTMLPASA HVKNVYCGEN GIFQTVRPGT LLLDSSTIDP
ATAREVASIA KKHQSTMLDC PVSGGTGGAE AGTLTFMVGG SEQDFNTAKT YLECMGKNIV
HCGDVGTGQV AKVCNNLVLG ISMIAVSEAM NLGVKQGMDP KKLAGIFNTS SARCWTSELY
NPCPGVIETS PASRGYTGGF GSALMTKDLG LAVDSAKSIG EPLLLGNSAH QLYTLLVAKG
DGQKDFSVVY DFLNKNFKNS N
