ID G0L4E9_ZOBGA Unreviewed; 348 AA.
AC G0L4E9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=4-Hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:CAZ95667.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:CAZ95667.1};
GN Name=pdxA {ECO:0000313|EMBL:CAZ95667.1};
GN OrderedLocusNames=zobellia_1612 {ECO:0000313|EMBL:CAZ95667.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ95667.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ95667.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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DR EMBL; FP476056; CAZ95667.1; -; Genomic_DNA.
DR RefSeq; WP_013992975.1; NZ_JAHKQS010000037.1.
DR AlphaFoldDB; G0L4E9; -.
DR STRING; 63186.ZOBELLIA_1612; -.
DR KEGG; zga:ZOBELLIA_1612; -.
DR PATRIC; fig|63186.3.peg.1597; -.
DR HOGENOM; CLU_040168_4_0_10; -.
DR OrthoDB; 9801783at2; -.
DR Proteomes; UP000008898; 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:CAZ95667.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898}.
SQ SEQUENCE 348 AA; 38049 MW; AA7A402E0E8AB3A9 CRC64;
MQEEGKIRLG ISIGDLNGIG CEVVLKTFED ARMLDFCTPV IFASNKTISF QKKELGLDIN
YHGVSDASKA VDGKINVVNV WKEVPKIKFG EATPEAGKFA IASLRAAVEA LKNDSIDVLV
TAPINKNNIQ ADDFKFPGHT DFLAQELEGE SLMFMVTDDL KVGLLTDHLA VKDVSAAINP
ILIRDKVRTI EKSLQMDFGI RAPKIALLGI NPHSGDNGVI GKEDDEVLKP VIKEMSDAGH
LVFGPYSADS FFGSDAYKSF DAILAAYHDQ GLIPFKTLSF GKGVNYTAGL SKVRTSPDHG
TAYEIAGKGE ADPSSFKEAV FTALHIFKNR KEYQELTANP LQKQRIRR
//
