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Database: UniProt
Entry: E5C512_9BACE
LinkDB: E5C512_9BACE
Original site: E5C512_9BACE 
ID   E5C512_9BACE            Unreviewed;       364 AA.
AC   E5C512;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:EFS30536.1};
GN   ORFNames=BSGG_1236 {ECO:0000313|EMBL:EFS30536.1};
OS   Bacteroides sp. D2.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556259 {ECO:0000313|EMBL:EFS30536.1, ECO:0000313|Proteomes:UP000003135};
RN   [1] {ECO:0000313|EMBL:EFS30536.1, ECO:0000313|Proteomes:UP000003135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EFS30536.1,
RC   ECO:0000313|Proteomes:UP000003135};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA   Sibley C., White A., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D2.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:EFS30536.1}.
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DR   EMBL; ACGA02000062; EFS30536.1; -; Genomic_DNA.
DR   RefSeq; WP_009000579.1; NZ_JH636026.1.
DR   AlphaFoldDB; E5C512; -.
DR   HOGENOM; CLU_040168_4_0_10; -.
DR   OrthoDB; 9801783at2; -.
DR   Proteomes; UP000003135; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR005255; PdxA_fam.
DR   NCBIfam; TIGR00557; pdxA; 1.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   364 AA;  40386 MW;  2CE81F9D615B31FB CRC64;
     MEDNKIRIGI TQGDINGVGY EVILKTFSDP TMLELCTPII YGSPKVAAYH RKALDIQTNF
     SIVNSATEAG YNRLSVVNCT DDEVKVEFSK PDPEAGKAAL GALERAIEEY REGLIDVIVT
     APINKHTIQS EEFSFPGHTE YIEERLGNGD KSLMILMKND FRVALVTTHI PVREIATTIT
     KELIQEKLMI FHRCLKQDFG IGAPRIAVLS LNPHAGDGGL LGMEEQEVII PAMKEMEEKG
     ILCYGPYAAD GFMGSGNYTH FDGILAMYHD QGLAPFKALA MEDGVNYTAG LPVVRTSPAH
     GTAYDIAGKG LACEDSFRQA IYVAIDVFRN RQRERVARAN PLRKQYYEKR DDSDKLKLDT
     VDED
//
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