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Database: UniProt
Entry: A0A062VRX5_9MICO
LinkDB: A0A062VRX5_9MICO
Original site: A0A062VRX5_9MICO 
ID   A0A062VRX5_9MICO        Unreviewed;       302 AA.
AC   A0A062VRX5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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};
GN   ORFNames=DC31_16065 {ECO:0000313|EMBL:KDA05330.1};
OS   Microbacterium sp. CH12i.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA05330.1, ECO:0000313|Proteomes:UP000027096};
RN   [1] {ECO:0000313|EMBL:KDA05330.1, ECO:0000313|Proteomes:UP000027096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH12i {ECO:0000313|EMBL:KDA05330.1,
RC   ECO:0000313|Proteomes:UP000027096};
RA   Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT   "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT   shallow groundwater in Cape Hallet, Antarctica.";
RL   Submitted (MAR-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|RuleBase:RU910714};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|RuleBase:RU910714}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080, ECO:0000256|RuleBase:RU910714}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDA05330.1}.
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DR   EMBL; JHET01000008; KDA05330.1; -; Genomic_DNA.
DR   RefSeq; WP_036280031.1; NZ_JHET01000008.1.
DR   AlphaFoldDB; A0A062VRX5; -.
DR   STRING; 1479651.DC31_16065; -.
DR   OrthoDB; 3185659at2; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000027096; 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|RuleBase:RU910714};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU910714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027096}.
FT   DOMAIN          3..165
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          168..294
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   302 AA;  30509 MW;  AB8CDBFAE3CD37EB CRC64;
     MTNIAFLGLG HMGGPMAANL VKAGHRVIGF DPVPAALEAA RVAGIEISSD AVSAVADVDI
     VITMLPSGAH VIAAYSGAAG APGLLASARP GTLFIDSSTI AVDEARKAHD LALEAGHRAA
     DAPVSGGVVG AEKGTLAFMV GASDEDFQTI QPILEVMGGR IVHCGGSGLG QAAKVCNNMI
     LGITQIAVAE AFVLGERLGL SHQALFDVAS NASGQCWALT TNCPVPGPVA TSPANNDYEP
     GFAGALMSKD LGLAESAIEL TGVDAQLGRH AREIYRAFAD GDGARKDFSG IINTIRAQSA
     DA
//
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