ID A0A1E7RD17_9GAMM Unreviewed; 318 AA.
AC A0A1E7RD17;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Bifunctional glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:OEY97065.1};
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:KAA8734978.1};
GN ORFNames=BJI46_11070 {ECO:0000313|EMBL:OEY97065.1}, F4V57_04265
GN {ECO:0000313|EMBL:KAA8734978.1};
OS Acinetobacter qingfengensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY97065.1, ECO:0000313|Proteomes:UP000185895};
RN [1] {ECO:0000313|EMBL:OEY97065.1, ECO:0000313|Proteomes:UP000185895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY97065.1,
RC ECO:0000313|Proteomes:UP000185895};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8734978.1, ECO:0000313|Proteomes:UP000323633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8734978.1,
RC ECO:0000313|Proteomes:UP000323633};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) 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:OEY97065.1}.
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DR EMBL; VXKN01000002; KAA8734978.1; -; Genomic_DNA.
DR EMBL; MKKK01000014; OEY97065.1; -; Genomic_DNA.
DR RefSeq; WP_070069515.1; NZ_VXKN01000002.1.
DR AlphaFoldDB; A0A1E7RD17; -.
DR STRING; 1262585.BJI46_11070; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000185895; Unassembled WGS sequence.
DR Proteomes; UP000323633; 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; cd05301; GDH; 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; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 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|RuleBase:RU003719};
KW Pyruvate {ECO:0000313|EMBL:OEY97065.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185895}.
FT DOMAIN 5..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 35301 MW; 8EA7CA88130406CA CRC64;
MKKKVVIFSN IFPEFEEKLK QQFEVVKINP KLGDVDQQIR DAVQYAHGMI GAGRRLGASQ
LETASQLEII STVSVGYDNY DVAYLKQKGI LLAHTPHVLT ETTADTAFTL LVSAARRVVE
LDGWARAGHW QKTVSTQEFG VDIHAKTLGI IGLGNIGAAI ARRGYYGFNM NVVYHGRQEK
PEIANAFNAR FLALDELLQQ ADFVVVTVDL NETTRHLLSN AQFAKMQKHA VLVNISRGAV
IDEQALIHAL QQKQIFAAGL DVFEHEPLQQ SPLFELDNVV ITPHIGSATL QTRQAMNQLA
YDNLVAQLTG KKARYLVN
//