SitesBLAST

Comparing WP_011606295.1 NCBI__GCF_000058485.1:WP_011606295.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
58% identity, 89% coverage: 52:499/504 of query aligns to 1:449/454 of 6ienB

• binding argininosuccinate: S97 (= S147), R98 (= R148), N99 (= N149), T144 (= T194), H145 (= H195), S266 (= S316), S267 (= S317), M269 (= M319), K272 (= K322), Y306 (= Y356), Q311 (= Q361), K314 (= K364)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
57% identity, 89% coverage: 52:499/504 of query aligns to 1:447/452 of 6ienA

• binding argininosuccinate: R98 (= R148), N99 (= N149), V102 (= V152), T144 (= T194), H145 (= H195), Y304 (= Y356), Q309 (= Q361), K312 (= K364)
• binding fumaric acid: S266 (= S316), S267 (= S317), K270 (= K322), N272 (= N324)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
54% identity, 89% coverage: 52:499/504 of query aligns to 1:413/418 of 6ienC

• binding arginine: R98 (= R148), N99 (= N149), V102 (= V152), Y306 (= Y356), Q311 (= Q361), K314 (= K364)
• binding argininosuccinate: T144 (= T194), H145 (= H195), S266 (= S316), S267 (= S317), M269 (= M319), K272 (= K322)
• binding fumaric acid: S97 (= S147), R98 (= R148), N99 (= N149)

P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
43% identity, 91% coverage: 42:502/504 of query aligns to 9:468/468 of P24058

• W11 (= W44) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
• S29 (= S62) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D66) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D122) mutation to N: Loss of activity.
• N116 (= N149) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D150) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T194) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
• H162 (= H195) mutation to E: Loss of activity.
• R238 (= R271) mutation to Q: Loss of activity.
• T281 (= T314) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S316) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
• N291 (= N324) binding in chain B; mutation to L: Loss of activity.
• D293 (= D326) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E329) mutation to D: Loss of activity.
• Y323 (= Y356) binding in chain A
• K325 (≠ R358) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q361) binding in chain A
• D330 (= D363) mutation to N: Loss of activity.
• K331 (= K364) binding in chain A; mutation to Q: Loss of activity.

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
46% identity, 91% coverage: 42:500/504 of query aligns to 7:464/464 of P04424

• R12 (= R47) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D66) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (≠ R86) mutation to N: 2-fold reduction in activity.
• K69 (≠ D104) modified: N6-acetyllysine
• E73 (≠ A108) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D122) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H124) mutation to Q: 10-fold reduction in activity.
• R94 (= R129) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (≠ G130) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R148) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D155) to E: in ARGINSA; severe
• V178 (≠ Q213) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ V216) to S: in a breast cancer sample; somatic mutation
• R182 (= R217) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R221) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G235) to V: in a breast cancer sample; somatic mutation
• R236 (= R271) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D272) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q321) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K323) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
• R297 (= R332) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ G341) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q361) to L: in ARGINSA; severe
• V335 (≠ A370) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (≠ L395) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ V418) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R421) to L: in ARGINSA; severe
• H388 (= H424) to Q: in ARGINSA; severe
• A398 (≠ C434) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (= R492) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 88% coverage: 56:499/504 of query aligns to 6:448/450 of 1k7wD

• active site: E71 (= E121), T144 (= T194), H145 (= H195), A266 (≠ S316), S267 (= S317), K272 (= K322), E279 (= E329)
• binding argininosuccinate: R98 (= R148), N99 (= N149), V102 (= V152), T144 (= T194), H145 (= H195), Y306 (= Y356), Q311 (= Q361), K314 (= K364)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
43% identity, 88% coverage: 56:499/504 of query aligns to 4:446/447 of 1hy0A

• active site: E69 (= E121), T142 (= T194), H143 (= H195), S264 (= S316), S265 (= S317), K270 (= K322), E277 (= E329)
• binding sulfate ion: S264 (= S316), M267 (= M319), N272 (= N324)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
42% identity, 91% coverage: 42:502/504 of query aligns to 7:466/466 of P02521

Sites not aligning to the query:

• 2 modified: Blocked amino end (Ala)

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
48% identity, 87% coverage: 51:488/504 of query aligns to 1:440/450 of 2e9fB

• active site: E71 (= E121), T146 (= T194), H147 (= H195), S268 (= S316), S269 (= S317), K274 (= K322), E281 (= E329)
• binding arginine: R98 (= R148), N99 (= N149), V102 (= V152), Y308 (= Y356), Q313 (= Q361), K316 (= K364)

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
43% identity, 88% coverage: 47:489/504 of query aligns to 1:444/451 of 1tj7B

• active site: H150 (= H195), S271 (= S316), K277 (= K322), E284 (= E329)
• binding phosphate ion: S271 (= S316), M274 (= M319), K277 (= K322)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
34% identity, 86% coverage: 71:501/504 of query aligns to 37:467/496 of 6g3iA

• binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S316), S277 (= S317), M279 (= M319), K282 (= K322), N284 (= N324), D286 (= D326)
• binding fumaric acid: R290 (≠ L330)

Sites not aligning to the query:

• binding fumaric acid: 22

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
34% identity, 86% coverage: 71:501/504 of query aligns to 37:467/497 of 6g3hA

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: S276 (= S316), S277 (= S317), M279 (= M319), K282 (= K322), N284 (= N324), D286 (= D326), R290 (≠ L330)

Sites not aligning to the query:

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: 22

6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
34% identity, 86% coverage: 71:501/504 of query aligns to 37:467/497 of 6g3gA

• binding succinic acid: S276 (= S316), S277 (= S317), M279 (= M319), K282 (= K322), N284 (= N324)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
34% identity, 86% coverage: 71:501/504 of query aligns to 37:467/497 of 6g3fA

• binding fumaric acid: S276 (= S316), S277 (= S317), M279 (= M319), K282 (= K322), N284 (= N324)

Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
25% identity, 63% coverage: 118:433/504 of query aligns to 62:383/431 of Q9X0I0

• H141 (= H195) active site, Proton donor/acceptor

2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 63% coverage: 118:433/504 of query aligns to 61:382/427 of 2x75A

• active site: H67 (= H124), T139 (= T194), H140 (= H195), S261 (= S316), S262 (= S317), K267 (= K322), E274 (= E329)
• binding adenosine monophosphate: N275 (≠ L330)

Sites not aligning to the query:

• binding adenosine monophosphate: 3, 4

P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 54% coverage: 126:395/504 of query aligns to 72:341/431 of P12047

• H89 (≠ R143) mutation to Q: Abolishes enzyme activity.
• H141 (= H195) mutation to Q: Abolishes enzyme activity.
• Q212 (≠ A267) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
• N270 (= N324) mutation N->D,L: Abolishes enzyme activity.
• R301 (= R358) mutation R->K,Q: Abolishes enzyme activity.

5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
22% identity, 70% coverage: 110:463/504 of query aligns to 49:395/419 of 5hw2A

• active site: H67 (vs. gap), S140 (≠ T194), H141 (= H195), K256 (= K322), E263 (= E329)
• binding fumaric acid: H67 (vs. gap), H89 (≠ R143), T93 (≠ S147), S94 (≠ R148)

3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
23% identity, 42% coverage: 128:341/504 of query aligns to 119:340/463 of 3r6vG

• active site: H185 (= H195), S315 (= S316), K321 (= K322), E328 (= E329)
• binding aspartic acid: G314 (= G315), S315 (= S316), S316 (= S317)

Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
23% identity, 42% coverage: 128:341/504 of query aligns to 122:343/468 of Q9LCC6

• H134 (≠ K141) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
• S140 (= S147) binding L-aspartate; mutation to A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
• T141 (≠ R148) binding L-aspartate; mutation to A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
• N142 (= N149) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation to Q: 3000-fold decrease in catalytic efficiency.
• K183 (≠ A190) mutation to A: Loss of activity. Does not affect tertiary structure.
• T187 (= T194) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
• H188 (= H195) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
• S318 (= S316) mutation to A: Loss of activity.
• S319 (= S317) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
• I320 (= I318) mutation to A: 50-fold decrease in catalytic efficiency.
• M321 (= M319) mutation to A: 338-fold decrease in catalytic efficiency.
• P322 (= P320) mutation to A: Almost no change in catalytic efficiency.
• K324 (= K322) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
• N326 (= N324) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.

Sites not aligning to the query:

• 101 binding L-aspartate; T→A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→S: 80-fold decrease in catalytic efficiency.

Query Sequence

>WP_011606295.1 NCBI__GCF_000058485.1:WP_011606295.1
MTSTDHSEEAAVPKPPAGGATDADAPAGGVLAGGASAGAPMRLWGGRFAGGPAEALARLS
VSVQFDWRLAPYDLLASKSHARVLHRAGLLDDAELAAMLAAIDDLSDAVAQGRFRPTVED
EDVHTALERGLLERLGALGGKLRAGRSRNDQVATDLRLYLREHARQVAARLTELSQALVT
VAEQHVDTPAPGMTHLQHAQPISFGHQLLAHVQAFVRDTDRLRDWDRRASVSALGAGALA
GSSLPLDPRGVAAELGFDRAFDNSLDAVSDRDFAAEFLFVAALIGVHLSRLGEEIVLWTT
REFGWVELDDAFATGSSIMPQKKNPDVAELARGKSGRLIGGLTGFLATLKGLPLAYDRDL
QEDKEPVFDAVDTLLLVLPALTGTVATMRVRRERLAAAAPDGFALATDVAEYLVRRGVPF
RQAHEAVGQLVSWCVAHDVDLDGVSDDDLAVINPLLTPDVRGVLSVSGALQARSAPGGTA
PDRVREQLAALRPVLDRDRAWAVD