(data stored in SCRATCH zone)

SWISSPROT: B4SSP6_STRM5

ID   B4SSP6_STRM5            Unreviewed;       296 AA.
AC   B4SSP6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 70.
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   OrderedLocusNames=Smal_0223 {ECO:0000313|EMBL:ACF49928.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49928.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49928.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49928.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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,
CC         ChEBI:CHEBI:11805, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57700, 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|RuleBase:RU910714}.
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DR   EMBL; CP001111; ACF49928.1; -; Genomic_DNA.
DR   RefSeq; WP_004136647.1; NC_011071.1.
DR   STRING; 391008.Smal_0223; -.
DR   EnsemblBacteria; ACF49928; ACF49928; Smal_0223.
DR   KEGG; smt:Smal_0223; -.
DR   eggNOG; ENOG4105CF3; Bacteria.
DR   eggNOG; COG2084; LUCA.
DR   HOGENOM; HOG000219610; -.
DR   KO; K00020; -.
DR   OMA; VTMIATC; -.
DR   OrthoDB; 1245550at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01125-MONOMER; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000001867; Chromosome.
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; 1.10.1040.10; -; 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; 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.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSP6.
DR   SWISS-2DPAGE; B4SSP6.
KW   Branched-chain amino acid catabolism {ECO:0000256|RuleBase:RU910714};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   NAD {ECO:0000256|RuleBase:RU910714};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU910714,
KW   ECO:0000313|EMBL:ACF49928.1}.
FT   DOMAIN        3    162       NAD_binding_2. {ECO:0000259|Pfam:
FT                                PF03446}.
FT   DOMAIN      165    292       NAD_binding_11. {ECO:0000259|Pfam:
FT                                PF14833}.
FT   ACT_SITE    171    171       {ECO:0000256|PIRSR:PIRSR000103-1}.
SQ   SEQUENCE   296 AA;  29850 MW;  595139E5AC1F677F CRC64;
     MSRIAFIGLG NMGGPMAANL VKNGHTVRVF DLVPAAVQAA VDAGASAAAS ARETLADAEV
     VISMLPASRH VEGVYLGDDG ILAAIPAGAL VIDCSTIAPA SARKVSEAAA ARGLQMIDAP
     VSGGTAGAQA GTLTFIVGGE EDALERARPV LQAMGKNIFH VGASGAGQVA KLCNNMALGV
     IMAVTGEAIA LGVAHGLDPK VLSQMMAVST GRSWATEVCN PWPGVLENAP ASRGYSGGFG
     SDLMLKDMGL AVEAAMSVGA SIPLGEVARN LYSMNHQAGR GKLDFSSVVQ LITSEK
//

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