ID B1FA11_9BURK Unreviewed; 337 AA.
AC B1FA11;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:EDT05577.1};
GN ORFNames=BamIOP4010DRAFT_0870 {ECO:0000313|EMBL:EDT05577.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT05577.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT05577.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT05577.1,
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|ARBA:ARBA00005854,
CC 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:EDT05577.1}.
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DR EMBL; ABLC01000010; EDT05577.1; -; Genomic_DNA.
DR RefSeq; WP_006750081.1; NZ_ABLC01000010.1.
DR AlphaFoldDB; B1FA11; -.
DR PATRIC; fig|396596.7.peg.7061; -.
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; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 20..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 337 AA; 37393 MW; 69065F0E38E5F818 CRC64;
MKIAILDDYQ DAVRKLNCFE MLAEHDVKVF NNTVRGLGQL ASRLAEVEAL VLIRERTPIS
SQLLAKLPNL RMISQTGRIS SHIDLEACTD RGIAVLEGTG SPVAPAELTW ALVMAAQRRI
PQYVANLKQG AWQQSGLKTS AMPPNFGLGQ VLRGQTLGIW GYGKIGRLVA GYGKAFGMNV
LIWGREHSLE AARADGYTAA ESREALFEQS DVLSLHLRMH DDTRGIVKQE DLMRMKPTSL
LVNTSRAELL EENALVNALS HNRPGMVAID VFESEPILQG YSLLRMENVI CTPHIGYVER
ESYELYFSAA FRNILAFDQG DMSSVVNPEA LTPRRVR
//
