SitesBLAST
Comparing WP_014026888.1 NCBI__GCF_000223395.1:WP_014026888.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 hits to proteins with known functional sites (download)
Q9UXR8 Glutamyl-tRNA reductase; GluTR; EC 1.2.1.70 from Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) (see paper)
39% identity, 83% coverage: 44:390/419 of query aligns to 43:383/404 of Q9UXR8
- C48 (= C49) mutation to S: Complete loss of activity.
- H84 (= H93) mutation to A: Complete loss of activity.; mutation to N: 30% of wild-type reductase activity. 15% of wild-type esterase activity.
1gpjA Glutamyl-tRNA reductase from methanopyrus kandleri (see paper)
39% identity, 83% coverage: 44:390/419 of query aligns to 43:378/399 of 1gpjA
- active site: S48 (≠ C49), H84 (= H93)
- binding glutamic acid: T47 (= T48), N49 (= N50), R50 (= R51), S94 (= S103), E99 (= E108), E101 (= E110), I102 (= I111), Q105 (= Q114)
- binding (2r,3r,4s,5s)-4-amino-2-[6-(dimethylamino)-9h-purin-9-yl]-5-(hydroxymethyl)tetrahydro-3-furanol: S48 (≠ C49), E101 (= E110)
P0A6X1 Glutamyl-tRNA reductase; GluTR; EC 1.2.1.70 from Escherichia coli (strain K12) (see 2 papers)
29% identity, 86% coverage: 35:395/419 of query aligns to 36:403/418 of P0A6X1
- T49 (= T48) mutation to V: 10% and 5% of wild-type reductase and esterase activity, respectively.
- C50 (= C49) mutation to S: Loss of activity.
- R52 (= R51) mutation to K: 5% and 4% of wild-type reductase and esterase activity, respectively.; mutation to Q: Loss of activity.
- E54 (= E53) mutation to K: 6% and 2% of wild-type reductase and esterase activity, respectively.
- C74 (≠ R74) mutation to S: No effect.
- H99 (= H93) mutation to N: 5% and 4% of wild-type reductase and esterase activity, respectively.
- G106 (= G100) mutation to N: Loss of activity.
- S109 (= S103) mutation to A: 28% and 25% of wild-type reductase and esterase activity, respectively.
- E114 (= E108) mutation to K: Loss of activity.
- Q116 (≠ E110) mutation to L: Loss of reductase activity. 30% of wild-type esterase activity.
- S145 (≠ A139) mutation to F: Loss of activity.
- C170 (≠ V164) mutation to S: No effect.
- G191 (= G185) mutation to D: Loss of reductase activity. Retains esterase activity.
- R314 (= R302) mutation to C: Loss of activity.
Sites not aligning to the query:
- 7 G→D: Loss of activity.
5yjlB Crystal structure of arabidopsis glutamyl-tRNA reductase in complex with NADPH and gbp (see paper)
34% identity, 51% coverage: 39:253/419 of query aligns to 40:256/415 of 5yjlB
- active site: C50 (= C49), H99 (= H93)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: C50 (= C49), A162 (≠ S156), G187 (= G185), K188 (≠ E186), M189 (≠ A187), N209 (= N207), R210 (= R208), S211 (= S209), R214 (= R212), T249 (≠ I246), A250 (≠ T247), S251 (≠ V248)
Sites not aligning to the query:
Query Sequence
>WP_014026888.1 NCBI__GCF_000223395.1:WP_014026888.1
MKTLDSLYMVGVDWKMVDTAKLAVLEGRVDDVYELLYPHVDELVVLPTCNRFEVYMVRGN
GCSMCIEEVLRFIRLHVGVEKPRVLRGVEAARHLFRVASGLESMVLGEPEILGQVKRAFE
YALKRAYTGKLLDLVFRYAIKTGKRVRSETGIGKGSIGIPGAAVILAEEKLGTLKDKIVG
VIGAGEAGSIIASLAAKKGAAKILIANRSFERARSLAKSLGEIAEPVEWGLLERLMTESD
VVFAAITVDRPVIPASVSRSARRGLVVIDISNVPVFESLPEWVEYHGFNEVVEVARRMAE
VRRSEVPKAEKIIEEELNKLMRAVKKRIADEAIETMMKFAKAMVDNEVRRAVSVLRGRGI
DVGAVEDVLRDLAWSSVRKSLRPLIIALQEAAEAGRIRMLEEVRTVFEKEYAKVVAKID
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory