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Database: UniProt
Entry: A0A0J1FB47_9FIRM
LinkDB: A0A0J1FB47_9FIRM
Original site: A0A0J1FB47_9FIRM 
ID   A0A0J1FB47_9FIRM        Unreviewed;       335 AA.
AC   A0A0J1FB47;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase 2 {ECO:0000313|EMBL:KLU60577.1};
DE            EC=1.1.1.262 {ECO:0000313|EMBL:KLU60577.1};
GN   Name=pdxA2_2 {ECO:0000313|EMBL:KLU60577.1};
GN   ORFNames=CEB3_c29600 {ECO:0000313|EMBL:KLU60577.1};
OS   Peptococcaceae bacterium CEB3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU60577.1, ECO:0000313|Proteomes:UP000035957};
RN   [1] {ECO:0000313|EMBL:KLU60577.1, ECO:0000313|Proteomes:UP000035957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEB3 {ECO:0000313|EMBL:KLU60577.1,
RC   ECO:0000313|Proteomes:UP000035957};
RA   Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA   Muehling M.;
RT   "Genome sequence of the moderately acidophilic sulfate reducing
RT   Peptococcaceae bacterium strain CEB3.";
RL   Submitted (JUN-2015) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KLU60577.1}.
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DR   EMBL; LDXJ01000059; KLU60577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1FB47; -.
DR   STRING; 999898.CEB3_c29600; -.
DR   PATRIC; fig|999898.3.peg.3330; -.
DR   OrthoDB; 9801783at2; -.
DR   Proteomes; UP000035957; 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   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:KLU60577.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035957}.
SQ   SEQUENCE   335 AA;  35893 MW;  0BD54981B66ABC8E CRC64;
     MKPIVAITIG DAAGIGPEIV TQALAKEYVY DMCRPLIIGD QNVLQKANDL LNLHLQMRTV
     GDPAEGHYEL GTIDLVDCKN IDSASFQGGK PDEMTGRAMI EYTNRAMGFL KANAVHAAIG
     GPHSKKAVDQ AGIRFAGYPN LITELTSAKR AFLMLVAGDL RVASATLHVS MRKACDLINK
     DLVLDIVAKV NEAVKLLGVE RPRIAVAGLN PHAGEEGMFG DEEIFHISPA IEAARVQGID
     VCGPFAGDSL FYKCLEHKYD AYVGMYHDQG HIALKTLALD KSCGLIIGTP VLFATVGHGC
     AQDIAWKGIA DPGSMLETIR VVSSMHMNRS ALSAN
//
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