ID Q2BCV4_9BACI Unreviewed; 324 AA.
AC Q2BCV4;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 13-SEP-2023, entry version 73.
DE SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:EAR67857.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:EAR67857.1};
GN Name=pdxA {ECO:0000313|EMBL:EAR67857.1};
GN ORFNames=B14911_13872 {ECO:0000313|EMBL:EAR67857.1};
OS Bacillus sp. NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR67857.1, ECO:0000313|Proteomes:UP000004554};
RN [1] {ECO:0000313|EMBL:EAR67857.1, ECO:0000313|Proteomes:UP000004554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR67857.1,
RC ECO:0000313|Proteomes:UP000004554};
RA Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily.
CC {ECO:0000256|ARBA:ARBA00009464}.
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:EAR67857.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAOX01000003; EAR67857.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2BCV4; -.
DR HOGENOM; CLU_040168_1_0_9; -.
DR Proteomes; UP000004554; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAR67857.1}.
SQ SEQUENCE 324 AA; 34697 MW; 1C8C5115A62EBFD7 CRC64;
MGDAAGVGPE IILKTLADQE IYQICNPLVI GDRKILERAK GFVDSQLTIE TVNEQDLEGL
DYQLGTVYCL DLDLLPADLP VGQVSPEAGH AAFEFVRTAI ELAEQKKIAA ICTAPLNKEA
MQKGGHKYPG HTEILADLTN TQDYSMMLSA PNLKVIHVTT HVGILDAVKM INPERVYHVI
KLAHETLTKA GIDSPKIAVC GINPHAGENG LFGYGEEEEK VIPGVEKAQA EGINAIGPLP
ADTLFFRAVR GDFDIVVAMY HDQGHGPVKV LGLDAGVNIT VGLPIIRTSV DHGTAFDIAG
KGIADEKSLV EAMRQAVELA PKSV
//