ID B2JVC5_PARP8 Unreviewed; 342 AA.
AC B2JVC5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:ACC74902.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:ACC74902.1};
GN OrderedLocusNames=Bphy_5837 {ECO:0000313|EMBL:ACC74902.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OG Plasmid pBPHY01 {ECO:0000313|EMBL:ACC74902.1,
OG ECO:0000313|Proteomes:UP000001192}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC74902.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0007829|PDB:4JQP}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ZINC.
RA Fairman J.W., Clifton M.C., Edwards T.E., Lorimer D.;
RT "X-ray crystal structure of a 4-hydroxythreonine-4-phosphate dehydrogenase
RT from Burkholderia phymatum.";
RL Submitted (MAR-2013) to the PDB data bank.
RN [2] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RC PLASMID=Plasmid pBPHY01 {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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DR EMBL; CP001045; ACC74902.1; -; Genomic_DNA.
DR PDB; 4JQP; X-ray; 1.65 A; A/B=1-342.
DR PDBsum; 4JQP; -.
DR AlphaFoldDB; B2JVC5; -.
DR SMR; B2JVC5; -.
DR KEGG; bph:Bphy_5837; -.
DR HOGENOM; CLU_040168_1_0_4; -.
DR Proteomes; UP000001192; Plasmid pBPHY01.
DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4JQP};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:4JQP};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACC74902.1}; Plasmid {ECO:0000313|EMBL:ACC74902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Zinc {ECO:0007829|PDB:4JQP}.
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:4JQP"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:4JQP"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:4JQP"
SQ SEQUENCE 342 AA; 36555 MW; 0AA7AD4FBFA4B485 CRC64;
MNSTYSRDQI MSNYLPVIGI TMGDAAGVGA EVVVKSLAHA SVYAQCRPLV IGDAKRLERA
NQIVGGEMKI RRIEDASEAR YEQGTIDCID LGLIPDDLPF GQLSAIAGDA AYQYIKRAVE
LAQSGKIDAI CTAPLNKEAL HAGGHKYPGH TEMLAHLTGV DEVSMMLVAP QLRVIHVTTH
IGIIDAIRKI EPGLVQRTIE RGNATLVKAG IERPRIGVCG INPHAGENGL FGYGEEEEKI
IPAVTLLQER GLDVTGPLPA DTLFFRAGRG DFDLVVAMYH DQGHGPVKVL GLEAGVNVTV
GLEVIRTSVD HGTAFDIAGK GVVDEGSMLE ALRQGAELAT RR
//
