ID F2I6I2_AERUA Unreviewed; 327 AA.
AC F2I6I2; A0A9Q4H1P4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:AEA00631.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:AEA00631.1};
GN Name=pdxB {ECO:0000313|EMBL:AEA00631.1};
GN OrderedLocusNames=HMPREF9243_0276 {ECO:0000313|EMBL:AEA00631.1};
OS Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC Aerococcus incertae sedis.
OX NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA00631.1, ECO:0000313|Proteomes:UP000008129};
RN [1] {ECO:0000313|Proteomes:UP000008129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL Submitted (FEB-2011) 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; CP002512; AEA00631.1; -; Genomic_DNA.
DR RefSeq; WP_013668883.1; NZ_JAOTMI010000012.1.
DR AlphaFoldDB; F2I6I2; -.
DR STRING; 866775.HMPREF9243_0276; -.
DR KEGG; aur:HMPREF9243_0276; -.
DR PATRIC; fig|866775.3.peg.256; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000008129; Chromosome.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12177; 2-Hacid_dh_12; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AEA00631.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008129}.
FT DOMAIN 20..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 117..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 327 AA; 35910 MW; 936A9861FF19BFA2 CRC64;
MTDYKIALVN SSSFGKWFPE HIEALEKIGP VDSFRFDNDI DGKSLAEKLH GYNLIISSVT
PFFTKEFFEN KDELLIISRH GIGYNNIDLD AAKEHGTLVT IVPPLVERDT VAENAVAQLL
ALVRQTLPAA QAAKDNKWKD RAQFMGHELS GKNVGVIGCG NIGSRVAEIL KYGFNANLYV
CDPKVDPEWV EKHGAKVVEL DELLAKADII SLNASLDEDS YHILNEEAFS KMKKGVYITN
TARGALVDEE AVIDAIEAGI VLGLATDVME EEPADNSHPY FSNDKILVTP HISAYTYECI
KGMGDKCVDD IQKVVNGEEP GGIVSPK
//
