ID A0A0S1XWM9_9BORD Unreviewed; 319 AA.
AC A0A0S1XWM9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:ALM82138.1};
GN ORFNames=ASB57_03415 {ECO:0000313|EMBL:ALM82138.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM82138.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM82138.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM82138.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP013111; ALM82138.1; -; Genomic_DNA.
DR RefSeq; WP_057650575.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1XWM9; -.
DR STRING; 1746199.ASB57_03415; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000064621; Chromosome.
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 CDD; cd12156; HPPR; 1.
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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 24..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34151 MW; 4BB48CAE1FCAB99F CRC64;
MTAKPRILQV GSYAGSPTAN DRLARAYDIV ELWKFPDRKA ALAEHGKGIN ALVTSANYGC
SAELIDALPD LKAICSWGVG YETLDIKAAH ARGIQVSNTP DVLTDCVADL AWGLMLAGAR
RIAHGDRFVR ANQWGQVHGG IPLGTRVSGK KLGIVGLGRI GEAIAKRGLG FDMDVRYHSR
REREGVPYKY EASLVELAKW ADFLVVATVG GPATFHLINK EVLEALGPTG TIINIARGPV
IDEAALVEAL ESGKLGNAAL DVFEQEPKVP DALKANEKAV LLPHIGSATV ETRKAMEDLM
VENLESFLKT GKVITPVEG
//
