ID B1FJT5_9BURK Unreviewed; 324 AA.
AC B1FJT5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:EDT02185.1};
GN ORFNames=BamIOP4010DRAFT_4296 {ECO:0000313|EMBL:EDT02185.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT02185.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT02185.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT02185.1,
RC ECO:0000313|Proteomes:UP000005463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria
RT IOP40-10.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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:EDT02185.1}.
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DR EMBL; ABLC01000130; EDT02185.1; -; Genomic_DNA.
DR RefSeq; WP_006753448.1; NZ_ABLC01000130.1.
DR AlphaFoldDB; B1FJT5; -.
DR PATRIC; fig|396596.7.peg.3219; -.
DR Proteomes; UP000005463; 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 CDD; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; 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 32..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 34764 MW; 117E60624B64CF0B CRC64;
MFSSSSPAKI VFLDRATLSP RTVLKPFPFP HDLRTFERTA AHEVAARIGD ADVVVTNKVR
LDAAVLDDAP RVRMIAIAAT GTDIVDLDAC AARGIVVSNI RGYAARTVPE HTFALIFALR
RSLVAYRDAV RAGRWLDSGQ FCFFDHPIRD LAGATLGIVG AGLLGRAVAA LARALGMRVR
FAAHGDARGD DHVPLDTLLR DSDVITLHCP LTPTTRNLID AAAFARMARR PLLINTARGG
LVDERALVDA LQSGQIAGAG FDVLTQEPLP VAHPFHAILS HPAFILTPHV AWASDEAMQA
LADQLVDNVA AFARGEPRQV VMAD
//
