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Database: UniProt
Entry: A0A091I184_CALAN
LinkDB: A0A091I184_CALAN
Original site: A0A091I184_CALAN 
ID   A0A091I184_CALAN        Unreviewed;       306 AA.
AC   A0A091I184;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|RuleBase:RU910714};
DE            Short=HIBADH {ECO:0000256|RuleBase:RU910714};
DE            EC=1.1.1.31 {ECO:0000256|RuleBase:RU910714};
DE   Flags: Fragment;
GN   ORFNames=N300_01078 {ECO:0000313|EMBL:KFP01200.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP01200.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP01200.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP01200.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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         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   EMBL; KL218015; KFP01200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091I184; -.
DR   STRING; 9244.A0A091I184; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
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|PIRSR:PIRSR000103-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU910714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT   DOMAIN          12..170
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          173..299
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
FT   BINDING         10..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-2"
FT   BINDING         73..74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-2"
FT   BINDING         78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-2"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-2"
FT   BINDING         254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP01200.1"
FT   NON_TER         306
FT                   /evidence="ECO:0000313|EMBL:KFP01200.1"
SQ   SEQUENCE   306 AA;  32241 MW;  A48711BC3B57DFDF CRC64;
     VCFRAMASKT PVGFIGLGNM GNPMAKNLVK HGYPVITYDV FPEACKEFQD LGAQVTDSPA
     DVAERADRII TMLPSSPNAI EAYTGANGIL KKVKKGSLLI DSSTIDPAVS KELAKAVEKM
     GAVFMDAPVS GGVGAARAGN LTFMVGGAEQ EFDAAKELLT CMGSNVIYCG EVGTGQAAKI
     CNNMLLAISM IGTAEAMNLG IRLGLDPKLL AKILNMSSGR CWSSDTYNPV PGVMEGVPSA
     NNYQGGFGTT LMAKDLGLAQ ISATNTKTPV PLGSQAHQIY RMMCAKGYSL KDFSAVFQFL
     REEEAL
//
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