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Database: UniProt
Entry: D4H0V7_DENA2
LinkDB: D4H0V7_DENA2
Original site: D4H0V7_DENA2 
ID   D4H0V7_DENA2            Unreviewed;       322 AA.
AC   D4H0V7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:ADD68620.1};
DE            EC=1.1.1.262 {ECO:0000313|EMBL:ADD68620.1};
GN   OrderedLocusNames=Dacet_1856 {ECO:0000313|EMBL:ADD68620.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD68620.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD68620.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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DR   EMBL; CP001968; ADD68620.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4H0V7; -.
DR   STRING; 522772.Dacet_1856; -.
DR   PaxDb; 522772-Dacet_1856; -.
DR   KEGG; dap:Dacet_1856; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_1_0_0; -.
DR   InParanoid; D4H0V7; -.
DR   OrthoDB; 9801783at2; -.
DR   Proteomes; UP000002012; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADD68620.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012}.
SQ   SEQUENCE   322 AA;  34780 MW;  BB4A5193CDFD4DAC CRC64;
     MTMKKPKIAI TTGDPSGIGP EIACRLASEL DGSEEYDAVF ISYENVIKSA FENIIKAPMP
     EMTIIEPDEK LDLKIEHGLI KPEYGKASML YVEKAVQMAM SGEVDAVVTC PINKASIKAG
     GYNYPGHTEF LGYLTRTRYF SMLMVGKNIR TVLATTHVPM AELVDKLDEN SIMNAIVNAH
     EAGQFFCGKR QPKIAVCGLN PHAGDNGALG DEEITLITPV IDIARAGGMD VEGPFPADSL
     FPKAAKGEYD FVVVMYHDQG LIPVKLEAFG NAVNVTLNLP IIRTSVDHGT AFEIAGKGIA
     DHHSLIRAID VAVEMVKNAQ SA
//
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