SitesBLAST
Comparing WP_068865835.1 NCBI__GCF_001677335.1:WP_068865835.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P83788 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Pseudomonas fluorescens (see paper)
48% identity, 100% coverage: 1:407/407 of query aligns to 1:416/416 of P83788
- T97 (= T97) binding pyridoxal 5'-phosphate
- S98 (= S98) binding pyridoxal 5'-phosphate
- D132 (= D128) mutation to A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity.; mutation to E: Enhances binding to pyridoxal phosphate.
- T172 (= T165) binding pyridoxal 5'-phosphate
- D201 (= D194) binding pyridoxal 5'-phosphate; mutation to E: Enhances binding to pyridoxal phosphate.
- H204 (= H197) binding pyridoxal 5'-phosphate
1qz9A The three dimensional structure of kynureninase from pseudomonas fluorescens (see paper)
49% identity, 95% coverage: 10:395/407 of query aligns to 9:403/404 of 1qz9A
- active site: F128 (= F125), D200 (= D194), Y225 (= Y219), K226 (= K220), R374 (= R366)
- binding pyridoxal-5'-phosphate: T95 (≠ S96), T96 (= T97), S97 (= S98), F128 (= F125), D131 (= D128), T171 (= T165), D200 (= D194), A202 (≠ S196), H203 (= H197), C223 (= C217), Y225 (= Y219), K226 (= K220)
3e9kA Crystal structure of homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex (see paper)
29% identity, 96% coverage: 2:392/407 of query aligns to 20:446/446 of 3e9kA
- active site: F160 (= F125), D245 (= D194), Y270 (= Y219), K271 (= K220), R420 (= R366)
- binding 3-Hydroxyhippuric acid: S70 (= S36), F160 (= F125), H248 (= H197), K271 (= K220), R420 (= R366)
- binding pyridoxal-5'-phosphate: L132 (≠ T97), T133 (≠ S98), F160 (= F125), D163 (= D128), D245 (= D194), A247 (≠ S196), H248 (= H197), Y270 (= Y219), K271 (= K220)
2hzpA Crystal structure of homo sapiens kynureninase (see paper)
30% identity, 96% coverage: 2:392/407 of query aligns to 20:447/447 of 2hzpA
- active site: F160 (= F125), D245 (= D194), Y270 (= Y219), K271 (= K220), R421 (= R366)
- binding pyridoxal-5'-phosphate: L132 (≠ T97), T133 (≠ S98), F160 (= F125), D163 (= D128), D245 (= D194), A247 (≠ S196), H248 (= H197), Y270 (= Y219), K271 (= K220)
P70712 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Rattus norvegicus (Rat) (see paper)
28% identity, 97% coverage: 2:394/407 of query aligns to 25:462/464 of P70712
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Q16719 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Homo sapiens (Human) (see 4 papers)
29% identity, 97% coverage: 2:394/407 of query aligns to 25:462/465 of Q16719
- T138 (≠ S98) binding pyridoxal 5'-phosphate
- T198 (vs. gap) to A: in HYXKY; reduced 3-hydroxykynureninase activity; dbSNP:rs606231307
- D250 (= D194) binding pyridoxal 5'-phosphate
- H253 (= H197) binding pyridoxal 5'-phosphate
- Y275 (= Y219) binding pyridoxal 5'-phosphate
- W305 (= W249) binding pyridoxal 5'-phosphate
- N333 (≠ T275) binding pyridoxal 5'-phosphate
- K412 (≠ A343) to E: in dbSNP:rs9013
Sites not aligning to the query:
- 156:465 natural variant: Missing (in VCRL2; strongly reduced 3-hydroxykynureninase activity)
5b87A Crystal structure of a cysteine desulfurase from thermococcus onnurineus na1 in complex with alanine at 2.3 angstrom resolution (see paper)
25% identity, 73% coverage: 20:315/407 of query aligns to 7:307/397 of 5b87A
- active site: H113 (≠ F125), D189 (= D194), A191 (≠ S196), Q192 (≠ H197), K215 (= K220)
- binding alanine: A23 (≠ S36), N164 (≠ Y169), K215 (= K220)
- binding pyridoxal-5'-phosphate: N84 (≠ S96), T85 (= T97), S86 (= S98), H113 (≠ F125), N164 (≠ Y169), D189 (= D194), A191 (≠ S196), Q192 (≠ H197), S212 (≠ C217), H214 (≠ Y219), K215 (= K220)
Sites not aligning to the query:
5b7uA Apo structure of cysteine desulfurase from thermococcus onnurineus na1 at 1.89a (see paper)
25% identity, 73% coverage: 20:315/407 of query aligns to 13:313/402 of 5b7uA
Sites not aligning to the query:
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
27% identity, 60% coverage: 105:347/407 of query aligns to 86:317/377 of 1vjoA
Sites not aligning to the query:
3lvmB Crystal structure of e.Coli iscs (see paper)
30% identity, 38% coverage: 68:220/407 of query aligns to 50:212/394 of 3lvmB
- active site: H110 (≠ N124), D186 (= D194), T188 (≠ S196), Q189 (≠ H197), K212 (= K220)
- binding pyridoxal-5'-phosphate: G80 (vs. gap), A81 (vs. gap), T82 (≠ S96), H110 (≠ N124), D186 (= D194), T188 (≠ S196), Q189 (≠ H197), H211 (≠ Y219), K212 (= K220)
Sites not aligning to the query:
P0A6B7 Cysteine desulfurase IscS; NifS protein homolog; ThiI transpersulfidase; TusA transpersulfidase; EC 2.8.1.7 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 38% coverage: 68:220/407 of query aligns to 44:206/404 of P0A6B7
- Q183 (≠ H197) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CGY 217:219) binding pyridoxal 5'-phosphate
- K206 (= K220) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 243 binding pyridoxal 5'-phosphate
- 328 active site, Cysteine persulfide intermediate; C→A: Loss of cysteine desulfurization.
- 376:404 mutation Missing: Normal cysteine desulfurase activity, decreased binding to IscU, decreased sulfur transfer to IscU, decreased Fe-S cluster assembly.
P0A6B9 Cysteine desulfurase IscS; EC 2.8.1.7 from Escherichia coli O157:H7 (see paper)
30% identity, 38% coverage: 68:220/407 of query aligns to 44:206/404 of P0A6B9
- W45 (= W69) mutation to R: No binding to TusA, decreased binding to ThiI. 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-thiouridine produced.
- E49 (= E71) mutation to A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced.
- D52 (≠ G74) mutation D->A,M,R,Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced.
- D65 (≠ A87) mutation to F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced.
- AT 75:76 (≠ -S 96) binding pyridoxal 5'-phosphate
- F89 (≠ L109) mutation to E: Decreased binding to ThiI.
- R112 (≠ A133) mutation to E: Decreased binding to IscX.
- R116 (≠ A137) mutation to E: Decreased binding to CyaY, IscX, ThiI.
- Q183 (≠ H197) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CGY 217:219) binding pyridoxal 5'-phosphate
- K206 (= K220) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 39 R→E: Decreased binding to CyaY.
- 220 R→E: No binding to CyaY, IscX, ThiI.
- 223 R→E: No binding CyaY, IscX, decreased binding to ThiI.
- 223:225 RVR→EVE: No binding to IscX.
- 225:227 RIE→EIR: No binding to CyaY, IscX.
- 234 G→L: Decreased binding to CyaY, IscX.
- 237:239 RGM→EGE: No binding to CyaY, IscX, ThiI.
- 243 binding pyridoxal 5'-phosphate
- 311 E→R: Decreased binding to ThiI.
- 327 A→V: No binding to IscX, decreased binding to CyaY, IscU, ThiI.
- 328 C→S: Retains binding to IscU, ThiI.
- 340 R→E: No binding to CyaY, ThiI, decreased binding to IscX, TusA.
5wgbA Crystal structure of the human mitochondrial cysteine desulfurase in complex with isd11 and e. Coli acp1 protein at 2.75a (see paper)
24% identity, 49% coverage: 60:257/407 of query aligns to 17:215/291 of 5wgbA