ID Q5BP14_PANTH Unreviewed; 322 AA.
AC Q5BP14;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=D-specific dehydrogenase {ECO:0000313|EMBL:AAX19283.1};
GN Name=vanH {ECO:0000313|EMBL:AAX19283.1};
OS Paenibacillus thiaminolyticus (Bacillus thiaminolyticus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=49283 {ECO:0000313|EMBL:AAX19283.1};
RN [1] {ECO:0000313|EMBL:AAX19283.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RSA1221 {ECO:0000313|EMBL:AAX19283.1};
RA Moodley A., van Nierop W., Marais E.;
RT "Paenibacillus thiaminolyticus RSA1221 vanA resistance gene cluster.";
RL Submitted (SEP-2009) 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; AY926880; AAX19283.1; -; Genomic_DNA.
DR RefSeq; WP_063856710.1; NG_048392.1.
DR AlphaFoldDB; Q5BP14; -.
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; cd12185; HGDH_LDH_like; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 38..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35477 MW; EFBDD2468040D1E5 CRC64;
MNNIGITVYG CEQDEADAFC ALSPRFGVMP SIINANVSES NAKSAPFNQC ISVGHKSEVS
ASILLALKRA GVKYISTRSI GCNHIDTTAA KRMGITVGNV AYSPDSVADY TMMLMLMAVR
NAKSIVRSVE KHDFRLDSVR GKVLSDMTVG VVGTGHIGKA VIERLRGFGC KVLAYSRSQS
IEANYVPFDE LLQNSDIVTL HVPLNADTRH IISHEQIQRM KQGAFIINTG RGPLVYTNEL
VKALENGKLG GAALDVLEGE EEFFYSDCSQ KPIDNQFLLK LQRMPNVIIT PHTAFYTEQA
LRDTVEKTNI NCLDFERSQE HE
//
