ID D9S1Z9_THEOJ Unreviewed; 326 AA.
AC D9S1Z9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:ADL07426.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:ADL07426.1};
GN OrderedLocusNames=Toce_0654 {ECO:0000313|EMBL:ADL07426.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL07426.1, ECO:0000313|Proteomes:UP000000272};
RN [1] {ECO:0000313|EMBL:ADL07426.1, ECO:0000313|Proteomes:UP000000272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC {ECO:0000313|Proteomes:UP000000272};
RX PubMed=21304740;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
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}.
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DR EMBL; CP002131; ADL07426.1; -; Genomic_DNA.
DR RefSeq; WP_013275473.1; NC_014377.1.
DR AlphaFoldDB; D9S1Z9; -.
DR STRING; 555079.Toce_0654; -.
DR KEGG; toc:Toce_0654; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_9; -.
DR OrthoDB; 9801783at2; -.
DR Proteomes; UP000000272; Chromosome.
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:ADL07426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000272}.
SQ SEQUENCE 326 AA; 34625 MW; B3EF4414637FB6DE CRC64;
MRPLVAITMG DPAGVGPEIS LKAAASVDVS GVARPLILGS GPVLRYYADL LKLSVPLRSI
NSPEDYLDGF VNYIPVNNLS LTDFEVGKVS SLCGRAAYEY LEAGVKMALR GEVSAIATAP
LNKEALHRAG LEFAGHTEIL AKLTGTKDYA MMLVAGNLRV IHVSTHVAIR KACDLVKEER
VYKTVTMAAA AAGSLGIRDP RIAIAGLNPH AGEKGLFGDE EIKEIVPAVE KAREQGFDVY
GPLSPDTVFL KASRGEYDVV VAMYHDQGHI AVKMAGFEKG VNITVGLPII RTSVDHGTAF
DIAGNGIADE RSMVEAVKLA AQMAKK
//
