ID A0A0S1Y0I7_9BORD Unreviewed; 312 AA.
AC A0A0S1Y0I7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:ALM83507.1};
GN ORFNames=ASB57_11475 {ECO:0000313|EMBL:ALM83507.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83507.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM83507.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM83507.1,
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|RuleBase:RU003719}.
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DR EMBL; CP013111; ALM83507.1; -; Genomic_DNA.
DR RefSeq; WP_057652353.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y0I7; -.
DR STRING; 1746199.ASB57_11475; -.
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; 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:UP000064621}.
FT DOMAIN 14..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..281
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 33123 MW; 8CE89DE5531E74D4 CRC64;
MIVSKPAVLM VTKNSAMHIE WMRAHFDMTV AADAAQRERL IQEQGERFRC VLTNGSEGFT
AVEMAAMPNL QLICVQGIGY ENVDVAAARA LGIKVVNGAG SNAVTVADHA FALLFTIVRR
IPMLDTYARA GGWRSGLTPI PVVSGLRLGL CGMGAIGQII GRRAAAFDMP VGYFSRSPKP
DAGEYFPDIG SLAAWADILI VALPGGPETH HLVDAEVLRA LGPEGYLINV GRGSVVDTQA
LVAALTDQRL AGAGLDVYEG EPAFPAAFEG CPNLVVTPHV GGWSQQALDN AVRRFIVNAR
RHFAGEPLIG VL
//
