TAS_ECOLI
ID TAS_ECOLI Reviewed; 346 AA.
AC P0A9T4; Q2MA03; Q46933;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein tas;
GN Name=tas; Synonyms=ygdS; OrderedLocusNames=b2834, JW2802;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B/R / WU3610;
RX PubMed=9560382; DOI=10.1093/genetics/148.4.1627;
RA Timms A.R., Bridges B.A.;
RT "Reversion of the tyrosine ochre strain Escherichia coli WU3610 under
RT starvation conditions depends on a new gene tas.";
RL Genetics 148:1627-1635(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NADPH.
RX PubMed=14517983; DOI=10.1002/prot.10367;
RA Obmolova G., Teplyakov A., Khil P.P., Howard A.J., Camerini-Otero R.D.,
RA Gilliland G.L.;
RT "Crystal structure of the Escherichia coli Tas protein, an NADP(H)-
RT dependent aldo-keto reductase.";
RL Proteins 53:323-325(2003).
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; Y14609; CAA74961.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40481.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75873.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76903.1; -; Genomic_DNA.
DR PIR; C65066; C65066.
DR RefSeq; NP_417311.1; NC_000913.3.
DR RefSeq; WP_001199295.1; NZ_STEB01000034.1.
DR PDB; 1LQA; X-ray; 1.60 A; A/B=1-346.
DR PDBsum; 1LQA; -.
DR AlphaFoldDB; P0A9T4; -.
DR SMR; P0A9T4; -.
DR BioGRID; 4263141; 13.
DR DIP; DIP-48107N; -.
DR IntAct; P0A9T4; 3.
DR STRING; 511145.b2834; -.
DR TCDB; 8.A.5.1.5; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR jPOST; P0A9T4; -.
DR PaxDb; P0A9T4; -.
DR PRIDE; P0A9T4; -.
DR EnsemblBacteria; AAC75873; AAC75873; b2834.
DR EnsemblBacteria; BAE76903; BAE76903; BAE76903.
DR GeneID; 66673299; -.
DR GeneID; 947306; -.
DR KEGG; ecj:JW2802; -.
DR KEGG; eco:b2834; -.
DR PATRIC; fig|1411691.4.peg.3900; -.
DR EchoBASE; EB2898; -.
DR eggNOG; COG0667; Bacteria.
DR HOGENOM; CLU_023205_2_0_6; -.
DR InParanoid; P0A9T4; -.
DR OMA; PPYSLFW; -.
DR PhylomeDB; P0A9T4; -.
DR BioCyc; EcoCyc:G7462-MON; -.
DR EvolutionaryTrace; P0A9T4; -.
DR PRO; PR:P0A9T4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; TAS:EcoliWiki.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:EcoliWiki.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..346
FT /note="Protein tas"
FT /id="PRO_0000070386"
FT ACT_SITE 53
FT /note="Proton donor"
FT BINDING 234..244
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:14517983"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1LQA"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1LQA"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1LQA"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:1LQA"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1LQA"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:1LQA"
SQ SEQUENCE 346 AA; 38500 MW; 111692D06CA07CD7 CRC64;
MQYHRIPHSS LEVSTLGLGT MTFGEQNSEA DAHAQLDYAV AQGINLIDVA EMYPVPPRPE
TQGLTETYVG NWLAKHGSRE KLIIASKVSG PSRNNDKGIR PDQALDRKNI REALHDSLKR
LQTDYLDLYQ VHWPQRPTNC FGKLGYSWTD SAPAVSLLDT LDALAEYQRA GKIRYIGVSN
ETAFGVMRYL HLADKHDLPR IVTIQNPYSL LNRSFEVGLA EVSQYEGVEL LAYSCLGFGT
LTGKYLNGAK PAGARNTLFS RFTRYSGEQT QKAVAAYVDI ARRHGLDPAQ MALAFVRRQP
FVASTLLGAT TMDQLKTNIE SLHLELSEDV LAEIEAVHQV YTYPAP
