ID A0A378UGS7_BERDE Unreviewed; 302 AA.
AC A0A378UGS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 Name=Hgd {ECO:0000313|EMBL:STZ76588.1};
GN ORFNames=NCTC10295_01362 {ECO:0000313|EMBL:STZ76588.1};
OS Bergeriella denitrificans (Neisseria denitrificans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Bergeriella.
OX NCBI_TaxID=494 {ECO:0000313|EMBL:STZ76588.1, ECO:0000313|Proteomes:UP000254651};
RN [1] {ECO:0000313|EMBL:STZ76588.1, ECO:0000313|Proteomes:UP000254651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10295 {ECO:0000313|EMBL:STZ76588.1,
RC ECO:0000313|Proteomes:UP000254651};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; UGQS01000002; STZ76588.1; -; Genomic_DNA.
DR RefSeq; WP_066078269.1; NZ_UGQS01000002.1.
DR AlphaFoldDB; A0A378UGS7; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000254651; 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:UP000254651}.
FT DOMAIN 6..164
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 167..293
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 302 AA; 31517 MW; 78440155DF92F3E6 CRC64;
MDKQPKIAFI GLGNMGAPMA ANLLKKGYKL TVFDLNPEIV SHLAAQGAAS VAHPLEMADA
DIIITMLPSG NIVKSVLLGE QGLLRALSAG TLVIDCSTTA AEDAKLLAQE AASCRIALLD
APVSGGIAGA TAGTLSFLVG GAQADFERAK PILEAMGKNI FHAGGNGAGQ TAKICNNMLL
GVLMSATAEA IALGVKNGLD PKTLSDIMAA SSGGNWVLNG YNPYPGIMEN APAARGYRGG
FMSKLMLKDL ELAHELADQT PCDTPMGDQA RELYRRFTAQ HDGDLDFSAI LGLYLDEVWD
DK
//
