ID G4HP84_9BACL Unreviewed; 334 AA.
AC G4HP84;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:EHB48921.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:EHB48921.1};
GN ORFNames=PaelaDRAFT_5795 {ECO:0000313|EMBL:EHB48921.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB48921.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB48921.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB48921.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) 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 ---------------------------------------------------------------------------
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; AGIP01000024; EHB48921.1; -; Genomic_DNA.
DR RefSeq; WP_007132942.1; NZ_AGIP01000024.1.
DR AlphaFoldDB; G4HP84; -.
DR STRING; 743719.PaelaDRAFT_5795; -.
DR PATRIC; fig|743719.3.peg.5892; -.
DR eggNOG; COG1995; Bacteria.
DR OrthoDB; 9801783at2; -.
DR Proteomes; UP000003891; 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:EHB48921.1}.
SQ SEQUENCE 334 AA; 35831 MW; C7BBB109D85FF414 CRC64;
MSERKPIIGI TMGDAAGVGP EIILKSLKHG EMYEISRPFV IGDRKILERA KTFVNSDLAI
ESIAADELEQ ADYCLGTVYV LDLDLLPGDL PVGQVSAEAG HAAFKYLERA IELAKENRIQ
AICTAPLNKE ALHKGGHKYP GHTEILADLT GTQDFSMMLS APNLKVIHVT THVGLIDAVK
MITPERVYHV IKLAHETLRK AGIDAPKIAV CGINPHAGEN GLFGYGEEEE KVIPAVEKAQ
AEGIEVVGPL PADTLFFRTV RGDFDIVVAM YHDQGHGPVK VLGLDAGVNI TVGLPIIRTS
VDHGTAFDIA GTGIADEKSL MEAIRQGAEL APKA
//