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Database: UniProt
Entry: I0KFB6_9BACT
LinkDB: I0KFB6_9BACT
Original site: I0KFB6_9BACT 
ID   I0KFB6_9BACT            Unreviewed;       608 AA.
AC   I0KFB6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:CCH02819.1};
DE            EC=1.1.1.262 {ECO:0000313|EMBL:CCH02819.1};
GN   Name=pdxA {ECO:0000313|EMBL:CCH02819.1};
GN   ORFNames=FAES_4820 {ECO:0000313|EMBL:CCH02819.1};
OS   Fibrella aestuarina BUZ 2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH02819.1, ECO:0000313|Proteomes:UP000011058};
RN   [1] {ECO:0000313|EMBL:CCH02819.1, ECO:0000313|Proteomes:UP000011058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX   PubMed=22689241; DOI=10.1128/JB.00550-12;
RA   Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT   "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT   Bacterium.";
RL   J. Bacteriol. 194:3555-3555(2012).
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DR   EMBL; HE796683; CCH02819.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0KFB6; -.
DR   STRING; 1166018.FAES_4820; -.
DR   KEGG; fae:FAES_4820; -.
DR   PATRIC; fig|1166018.3.peg.1790; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_498660_0_0_10; -.
DR   OrthoDB; 9801783at2; -.
DR   Proteomes; UP000011058; 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:CCH02819.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011058}.
FT   REGION          1..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..78
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   608 AA;  67525 MW;  E7B566850B3BB938 CRC64;
     MEQQPPNTEG RETPASGESN NGQERRSRNR NRNRNRNRNR DKNGQPRGEQ ASAIDDDLEF
     EEIDTSFIGA EDDTDESGNV PEPAGTQAEP ASQRPPRSER NRPERGERAQ SERNERNNQR
     QPTDRGDRAE RPARPERERN RPERSERPER PERTQPERTQ PERSAFDRSG SRPVELRQAQ
     PSVQPPQPER QERYEPMAVD RYAGASVFEA DDELDGSHRS GDRAPISETA QKERLIIGIT
     LGDYNGVGPE VILKALQYNQ LQKICTPVIY GSMRVLNRYR NLLNLKDWNL NGIQQVDQAS
     HKMTNVITCF SENTPPPVPQ PTVAEGDPPA DGEAETPAPV VEKPAPLPVD IQPGKVTPEA
     GIAAFACLSR GVEDLKAGKI HALVTAPINK HNIQSEAFKF PGHTEYLASA FGVADNLMFM
     VSETLKVGVV TGHVPLGRVR QGIHKGAILQ KIDLMTKSLK QDFGIRRPKI AVLGLNPHAG
     ENGLLGNEEK EIITPLINEL RQKGQLVYGP FPADGFFGTR AYRKYDAVLA MYHDQGLIPF
     KSIAFDEGVN FTAGMPAVRT SPDHGTAYDI AGKGLADETS MIQAIYTACD VARRRIDYQE
     LEANALKK
//
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