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Database: UniProt
Entry: A0A246IT25_9BURK
LinkDB: A0A246IT25_9BURK
Original site: A0A246IT25_9BURK 
ID   A0A246IT25_9BURK        Unreviewed;       303 AA.
AC   A0A246IT25;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OWQ83366.1};
GN   ORFNames=CDN99_26300 {ECO:0000313|EMBL:OWQ83366.1};
OS   Roseateles aquatilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ83366.1, ECO:0000313|Proteomes:UP000197468};
RN   [1] {ECO:0000313|EMBL:OWQ83366.1, ECO:0000313|Proteomes:UP000197468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ83366.1,
RC   ECO:0000313|Proteomes:UP000197468};
RX   PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA   Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT   "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT   nov., in the class Betaproteobacteria, and emended description of the genus
RT   Roseateles.";
RL   Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:OWQ83366.1}.
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DR   EMBL; NIOF01000021; OWQ83366.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246IT25; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000197468; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197468}.
FT   DOMAIN          6..301
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          100..272
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   303 AA;  31867 MW;  CCADC2FA91EC35CE CRC64;
     MPMAEQHQAQ LRQRYDVIHA PTAESRAKAV AEQGADIEIV LTIGAVGLRG EEIAAMPRLA
     AAAALGAGYE AIDVAAAKAR GLTLWNGAGT NDACVADHAM ALLLASVRAL PQQEKALRAG
     IWRDDLPLRP SVNGRRLGIV GMGTIGLRIA RRALAFDMAV GYHNRRERDD AAGCQYFGSL
     IALATWADFL VVAAPGGPTT RHIVNAEVLS ALGPQGHVVN IARGSLVDTE ALARALAAGQ
     LAGAALDVYE TEPKPPEALL GFPNVILTPH IAGWSPESVQ ATVDLFLANA RRWEAGEPVL
     TPL
//
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