NCBI Conserved Domain Search
New Search PubMed Nucleotide Protein Structure CDD Taxonomy Help? 


RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: lcl|tmpseq_0 unnamed protein product
         (274 letters)

Database: cdd.v2.00
gnl|CDD|16974 pfam01488, Shikimate_DH, Shikimate / quinate 5-dehydrogenase. This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate gnl|CDD|17595 pfam05200, GlutR_NAD_bind, Glutamyl-tRNAGlu reductase, NAD(P) binding domain. This family use NADPH as a cofactor. This family is related to other NADPH binding domains gnl|CDD|10044 COG0169, AroE, Shikimate 5-dehydrogenase [Amino acid transport and metabolism] gnl|CDD|10247 COG0373, HemA, Glutamyl-tRNA reductase [Coenzyme metabolism]
 Domain Relatives
    .. This CD alignment includes 3D structure. To display structure, download Cn3D!
  PSSMs producing significant alignments: Score
(bits)		 E
value
 
gnl|CDD|16974 pfam01488, Shikimate_DH, Shikimate / quinate 5-dehydrogenase. ... 258 5e-70
gnl|CDD|17595 pfam05200, GlutR_NAD_bind, Glutamyl-tRNAGlu reductase, NAD(P) ... 43.3 3e-05
  gnl|CDD|10044 COG0169, AroE, Shikimate 5-dehydrogenase [Amino acid transport... 270 1e-73
gnl|CDD|10247 COG0373, HemA, Glutamyl-tRNA reductase [Coenzyme metabolism] 51.8 9e-08

gnl|CDD|16974, pfam01488, Shikimate_DH, Shikimate / quinate 5-dehydrogenase. This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. 
             CD-Length = 240 residues, 100.0% aligned
             Score =  258 bits (661), Expect = 5e-70

Query:  20   HRLFAEQTGEALVYDAQLAPLDDFPGFARRFFEQG-KGANVTVPFKEEAYRLVDELSERA  78
Sbjct:  1    HNAAFEQLGLNHVYLAFETPPDDLRGAVEGFFALGFKGANVTIPFKEEAMPLLDELTPRA  60

Query:  79   TRAGAVNTLIRLADGRLRGDNTDGAGLLRDLTANAGVELRGKRVLLLGAGGAVRGVLEPF  138
Sbjct:  61   KLIGAVNTLIREGDGKLRGDNTDGIGIRAALEEGLGFVRKGKTALILGAGGAARAVAYAL  120

Query:  139  LGECPAELLIANRTARKAVDLAERFADLGAVRGCGFAEVEG-PFDLVVNGTSASLAG--D  195
Sbjct:  121  LKLGVAKIYIANRTVEKAEALAERFGRYGAISVVSVSDLEGQAFDIIINATSVGLEPEID  180

Query:  196  VPPLAQSVIEPGRTVCYDMMYAKEPTAFNRWAAERGAARTLDGLGMLVEQAAEAFFLWRG  255
Sbjct:  181  DPPLSLSLLFKEGGVVYDMVYNPLTTPLLREAQARG-WKVIDGLGMLVEQGAEQFELWTG  239

Query:  256  V  256
Sbjct:  240  V  240
gnl|CDD|17595, pfam05200, GlutR_NAD_bind, Glutamyl-tRNAGlu reductase, NAD(P) binding domain. This family use NADPH as a cofactor. This family is related to other NADPH binding domains. 
             CD-Length = 155 residues, only  48.4% aligned
             Score = 43.3 bits (102), Expect = 3e-05

Query:  116  ELRGKRVLLLGAGGAVRGVLEPFLGECPAELLIANRTARKAVDLAERFADLGAVRGCGFA  175
Sbjct:  19   SLSDKKVLVIGAGEMGELVAKHLLAKGVKKITIANRTLERAQALAEKL----GGEALPLN  74

Query:  176  EVE---GPFDLVVNGTSAS  191
Sbjct:  75   ELNEYLAEADVVISATSAP  93
gnl|CDD|10044, COG0169, AroE, Shikimate 5-dehydrogenase [Amino acid transport and metabolism] 
             CD-Length = 283 residues,  97.5% aligned
             Score =  270 bits (691), Expect = 1e-73

Query:  1    MDRYCVFGNPIGHSKSPLIHRLFAEQTGEALVYDAQLAPLDDFPGFARRFFEQG-KGANV  59
Sbjct:  6    TKLFGVIGNPISHSLSPRMHNAAFRALGLDYVYLAFEVPPEDLPEAVSGIRALGFRGLNV  65

Query:  60   TVPFKEEAYRLVDELSERATRAGAVNTLIRLADGRLRGDNTDGAGLLRDLT-ANAGVELR  118
Sbjct:  66   TIPFKEAALPLLDELSPRARLIGAVNTLVREDDGKLRGYNTDGIGFLRALKEFGLPVDVT  125

Query:  119  GKRVLLLGAGGAVRGVLEPFLGECPAELLIANRTARKAVDLAERFADLG-AVRGCGFAEV  177
Sbjct:  126  GKRVLILGAGGAARAVAFALAEAGAKRITVVNRTRERAEELADLFGELGAAVEAAALADL  185

Query:  178  EG--PFDLVVNGTSASLAGD-VPPLAQSVIEPGRTVCYDMMYAKEPTAFNRWAAERGAAR  234
Sbjct:  186  EGLEEADLLINATPVGMAGPEGDSPVPAELLPKGAIVYDVVYNPLETPLLREARAQG-AK  244

Query:  235  TLDGLGMLVEQAAEAFFLWRGVRPASAPVLETLRRQL  271
Sbjct:  245  TIDGLGMLVHQAAEAFELWTGVEPPVDVMKEALIEAL  281
gnl|CDD|10247, COG0373, HemA, Glutamyl-tRNA reductase [Coenzyme metabolism] 
             CD-Length = 414 residues, only  18.1% aligned
             Score = 51.8 bits (124), Expect = 9e-08

Query:  117  LRGKRVLLLGAGGAVRGVLEPFLGECPAELLIANRTARKAVDLAERFADLGAVRGCGFAE  176
Sbjct:  176  LKDKKVLVIGAGEMGELVAKHLAEKGVKKITIANRTLERAEELAKKL----GAEAVALEE  231

Query:  177  VE---GPFDLVVNGTSASL  192
Sbjct:  232  LLEALAEADVVISSTSAPH  250
Citing CD-Search: Marchler-Bauer A, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, Panchenko AR, Rao BS, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003), "CDD: a curated Entrez database of conserved domain alignments", Nucleic Acids Res. 31:383-387.

Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH