SitesBLAST
Comparing RR42_RS15385 FitnessBrowser__Cup4G11:RR42_RS15385 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 17 hits to proteins with known functional sites (download)
P83788 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Pseudomonas fluorescens (see paper)
72% identity, 99% coverage: 5:418/418 of query aligns to 3:416/416 of P83788
- T97 (= T99) binding
- S98 (= S100) binding
- D132 (= D134) mutation to A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity.; mutation to E: Enhances binding to pyridoxal phosphate.
- T172 (= T174) binding
- D201 (= D203) binding ; mutation to E: Enhances binding to pyridoxal phosphate.
- H204 (= H206) binding
1qz9A The three dimensional structure of kynureninase from pseudomonas fluorescens (see paper)
73% identity, 96% coverage: 5:406/418 of query aligns to 2:403/404 of 1qz9A
- active site: F128 (= F131), D200 (= D203), Y225 (= Y228), K226 (= K229), R374 (= R377)
- binding pyridoxal-5'-phosphate: T95 (= T98), T96 (= T99), S97 (= S100), F128 (= F131), D131 (= D134), T171 (= T174), D200 (= D203), A202 (= A205), H203 (= H206), C223 (= C226), Y225 (= Y228), K226 (= K229)
3e9kA Crystal structure of homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex (see paper)
28% identity, 94% coverage: 10:403/418 of query aligns to 26:446/446 of 3e9kA
- active site: F160 (= F131), D245 (= D203), Y270 (= Y228), K271 (= K229), R420 (= R377)
- binding 3-Hydroxyhippuric acid: S70 (= S38), F160 (= F131), H248 (= H206), K271 (= K229), R420 (= R377)
- binding pyridoxal-5'-phosphate: L132 (≠ T99), T133 (≠ S100), F160 (= F131), D163 (= D134), D245 (= D203), A247 (= A205), H248 (= H206), Y270 (= Y228), K271 (= K229)
2hzpA Crystal structure of homo sapiens kynureninase (see paper)
28% identity, 94% coverage: 10:403/418 of query aligns to 26:447/447 of 2hzpA
- active site: F160 (= F131), D245 (= D203), Y270 (= Y228), K271 (= K229), R421 (= R377)
- binding pyridoxal-5'-phosphate: L132 (≠ T99), T133 (≠ S100), F160 (= F131), D163 (= D134), D245 (= D203), A247 (= A205), H248 (= H206), Y270 (= Y228), K271 (= K229)
P70712 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Rattus norvegicus (Rat) (see paper)
27% identity, 94% coverage: 10:403/418 of query aligns to 31:460/464 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)
27% identity, 95% coverage: 10:407/418 of query aligns to 31:464/465 of Q16719
- T138 (≠ S100) binding
- T198 (vs. gap) to A: in HYXKY; reduced 3-hydroxykynureninase activity; dbSNP:rs606231307
- D250 (= D203) binding
- H253 (= H206) binding
- Y275 (= Y228) binding
- W305 (= W258) binding
- N333 (≠ T284) binding
- K412 (≠ G354) 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)
28% identity, 52% coverage: 80:297/418 of query aligns to 66:280/397 of 5b87A
- active site: H113 (≠ F131), D189 (= D203), A191 (= A205), Q192 (≠ H206), K215 (= K229)
- binding alanine: N164 (≠ Y178), K215 (= K229)
- binding pyridoxal-5'-phosphate: N84 (≠ T98), T85 (= T99), S86 (= S100), H113 (≠ F131), N164 (≠ Y178), D189 (= D203), A191 (= A205), Q192 (≠ H206), S212 (≠ C226), H214 (≠ Y228), K215 (= K229)
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)
28% identity, 39% coverage: 80:243/418 of query aligns to 56:218/404 of P0A6B7
- Q183 (≠ H206) binding
- SGH 203:205 (≠ CTY 226:228) binding
- K206 (= K229) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 243 binding
- 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)
28% identity, 39% coverage: 80:243/418 of query aligns to 56:218/404 of P0A6B9
- D65 (≠ G89) mutation to F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced.
- AT 75:76 (≠ TT 98:99) binding
- F89 (≠ R112) mutation to E: Decreased binding to ThiI.
- R112 (≠ Q139) mutation to E: Decreased binding to IscX.
- R116 (≠ Q146) mutation to E: Decreased binding to CyaY, IscX, ThiI.
- Q183 (≠ H206) binding
- SGH 203:205 (≠ CTY 226:228) binding
- K206 (= K229) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 39 R→E: Decreased binding to CyaY.
- 45 W→R: No binding to TusA, decreased binding to ThiI. 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-thiouridine produced.
- 49 E→A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced.
- 52 mutation D->A,M,R,Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced.
- 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
- 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.
5b7uA Apo structure of cysteine desulfurase from thermococcus onnurineus na1 at 1.89a (see paper)
28% identity, 52% coverage: 80:297/418 of query aligns to 72:286/402 of 5b7uA
Sites not aligning to the query:
3lvmB Crystal structure of e.Coli iscs (see paper)
28% identity, 40% coverage: 80:248/418 of query aligns to 62:231/394 of 3lvmB
- active site: H110 (≠ F131), D186 (= D203), T188 (≠ A205), Q189 (≠ H206), K212 (= K229)
- binding pyridoxal-5'-phosphate: G80 (vs. gap), A81 (≠ T98), T82 (= T99), H110 (≠ F131), D186 (= D203), T188 (≠ A205), Q189 (≠ H206), H211 (≠ Y228), K212 (= K229)
Sites not aligning to the query:
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 25% coverage: 136:240/418 of query aligns to 103:216/377 of 1vjoA
Sites not aligning to the query:
8odqD Sufs-sufu complex from mycobacterium tuberculosis (see paper)
28% identity, 39% coverage: 82:242/418 of query aligns to 75:237/410 of 8odqD
- binding pyridoxal-5'-phosphate: N91 (vs. gap), A92 (vs. gap), T93 (= T98), H125 (≠ N130), N175 (≠ Y178), D200 (= D203), C202 (≠ A205), Q203 (≠ H206), S223 (≠ C226), H225 (≠ Y228), K226 (= K229)
P96060 2-aminoethylphosphonate--pyruvate transaminase; 2-aminoethylphosphonate aminotransferase; AEP transaminase; AEPT; EC 2.6.1.37 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
24% identity, 43% coverage: 89:268/418 of query aligns to 56:225/367 of P96060
- D168 (= D203) mutation to A: Loss of enzymatic activity.
- K194 (= K229) mutation K->L,R: Loss of enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 340 mutation R->A,K: Decreased affinity for all of the substrates.
1m32B Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
24% identity, 43% coverage: 89:268/418 of query aligns to 52:221/362 of 1m32B
Sites not aligning to the query:
1m32A Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
24% identity, 43% coverage: 89:268/418 of query aligns to 51:220/361 of 1m32A
Sites not aligning to the query:
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
28% identity, 38% coverage: 77:233/418 of query aligns to 59:213/396 of 4hf8A
- active site: R59 (= R77), Y112 (≠ N130), D184 (= D203), K209 (= K229)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (≠ N102), I88 (≠ L103), Y112 (≠ N130), E155 (≠ T174), N159 (≠ Y178), D184 (= D203), S206 (≠ C226), K209 (= K229)
Sites not aligning to the query:
Query Sequence
>RR42_RS15385 FitnessBrowser__Cup4G11:RR42_RS15385
MTAMTREQCLALDQEDPLRRLRDQFALPQGVIYLDGNSLGARPRSAAARAAEVVSEEWGT
GLIRSWNTAGWFELPQRLGNMLAPLIGAGEDEVVVTDTTSSNLFKVLAAALRVQQTRDPK
RKVIVSEASNFPTDLYIAQGLADLLQQGYSLRLVNAPEEIDAAVDADTAVLMLTHVNYKT
GEMLDMASVTEMAHARGALTVWDLAHSAGAVPVALKASGADYAVGCTYKYLNGGPGSPAF
LWVAPSLRDAFWQPLSGWWGHAAPFAMEPGYRPREGVARFLCGTQPIASLAMVECGLDIY
AQTDMAVLRAKSLMLTDLFIALVETRCAAHPLELVTPRAHARRGSHVSFAHPDGFAVVQA
LIERGVIGDYREPRIARFGFTPLYTSFTEVWDAVEILRDVLDSGTYKAERHQTRGLVT
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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