ID A0A0S1Y0N6_9BORD Unreviewed; 328 AA.
AC A0A0S1Y0N6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:ALM83615.1};
GN ORFNames=ASB57_12100 {ECO:0000313|EMBL:ALM83615.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83615.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM83615.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM83615.1,
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; ALM83615.1; -; Genomic_DNA.
DR RefSeq; WP_057652461.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y0N6; -.
DR STRING; 1746199.ASB57_12100; -.
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; cd12169; PGDH_like_1; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 23..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 122..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35978 MW; 39E569ED0084C5B1 CRC64;
MSKVFQHRAR VAILDDYQGL ALTSADWTAL RERCDVNVFH EAIPPDEAPA RLTDFDVLCT
MRERMALPAG LLERLPKLKF IAVTGPHHRT LDLAAARRLG ITVSCTPRPE TGQFATAELA
WGLILALTRH IPQETQGMRV GGWQHTVGKA LYGRTLGLLG LGRLGAHMVP VARAFGMDVI
AWSQNLTDEA ARAAGARRVG KHELFARSDV LSVHLVLSER TRHIVDRAAL QAMKPGAYLV
NTARGGLIEQ EALVDALEDG PLGGAALDTF EVEPLPADHV LRRLPKLLLT PHLGYTVEET
FAWFYRLSIE NIAAWLDGAP IRLLQAPA
//
