SitesBLAST
Comparing GFF3379 FitnessBrowser__Phaeo:GFF3379 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
59% identity, 100% coverage: 1:341/342 of query aligns to 1:340/341 of P07913
- C38 (= C38) mutation to D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+).; mutation to S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+).
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
60% identity, 100% coverage: 1:341/342 of query aligns to 2:338/339 of 5kiaA
- active site: C37 (= C38), G38 (= G39), T39 (= T40), H42 (= H43), H61 (= H63), E62 (= E64), C91 (≠ Q93), C94 (≠ S96), C97 (≠ S99), C105 (≠ D107), V109 (≠ R111), P147 (= P149), A151 (= A153), K333 (= K336)
- binding calcium ion: D146 (= D148), N150 (= N152), E288 (= E291)
- binding zinc ion: C91 (≠ Q93), C94 (≠ S96), C97 (≠ S99), C105 (≠ D107)
O58389 L-threonine 3-dehydrogenase; L-ThrDH; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see 2 papers)
42% identity, 99% coverage: 1:339/342 of query aligns to 5:345/348 of O58389
- C42 (= C38) binding
- T44 (= T40) mutation to A: Total loss of enzymatic activity.
- H67 (= H63) binding
- E68 (= E64) binding
- C97 (≠ Q93) binding
- C100 (≠ S96) binding
- C103 (≠ S99) binding
- C111 (≠ D107) binding
- E152 (≠ D148) mutation E->A,Q: Almost complete loss of enzymatic activity.; mutation to C: 120-fold decrease in catalytic efficiency.; mutation to D: Shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD(+), compared to wild-type.; mutation to K: Total loss of enzymatic activity.
- L179 (≠ I175) binding
- E199 (≠ D195) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (= R200) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ LGI 263:265) binding
- IT 291:292 (≠ VY 287:288) binding
- R294 (= R290) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
42% identity, 99% coverage: 1:339/342 of query aligns to 3:343/346 of 2dfvA
- active site: C40 (= C38), G41 (= G39), T42 (= T40), H45 (= H43), H65 (= H63), E66 (= E64), C95 (≠ Q93), C98 (≠ S96), C101 (≠ S99), C109 (≠ D107), K113 (≠ R111), P151 (= P149), A155 (= A153), K340 (= K336)
- binding nicotinamide-adenine-dinucleotide: G175 (= G173), P176 (= P174), L177 (≠ I175), E197 (≠ D195), P198 (≠ I196), R202 (= R200), F241 (≠ M240), S242 (= S241), A244 (≠ S243), L264 (= L263), G265 (= G264), L266 (≠ I265), I289 (≠ V287), T290 (≠ Y288)
- binding zinc ion: C95 (≠ Q93), C101 (≠ S99), C109 (≠ D107)
2ejvA Crystal structure of threonine 3-dehydrogenase complexed with NAD+
43% identity, 99% coverage: 1:339/342 of query aligns to 1:339/343 of 2ejvA
- active site: C38 (= C38), G39 (= G39), T40 (= T40), H43 (= H43), H63 (= H63), E64 (= E64), C93 (≠ Q93), C96 (≠ S96), C99 (≠ S99), C107 (≠ D107), Q111 (≠ R111), P149 (= P149), A153 (= A153), K336 (= K336)
- binding nicotinamide-adenine-dinucleotide: G172 (= G171), G174 (= G173), P175 (= P174), I176 (= I175), S195 (≠ T194), D196 (= D195), P197 (≠ I196), R201 (= R200), F238 (≠ M240), S239 (= S241), N241 (≠ S243), A244 (= A246), L261 (= L263), G262 (= G264), I263 (= I265)
- binding zinc ion: C38 (= C38), H63 (= H63), E64 (= E64), C96 (≠ S96), C99 (≠ S99), C107 (≠ D107)
2dq4A Crystal structure of threonine 3-dehydrogenase
43% identity, 99% coverage: 1:339/342 of query aligns to 1:339/343 of 2dq4A
- active site: C38 (= C38), G39 (= G39), T40 (= T40), H43 (= H43), H63 (= H63), E64 (= E64), C93 (≠ Q93), C96 (≠ S96), C99 (≠ S99), C107 (≠ D107), Q111 (≠ R111), P149 (= P149), A153 (= A153), K336 (= K336)
- binding zinc ion: C38 (= C38), H63 (= H63), E64 (= E64), C93 (≠ Q93), C96 (≠ S96), C107 (≠ D107)
Q5SKS4 L-threonine 3-dehydrogenase; TDH; EC 1.1.1.103 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
43% identity, 99% coverage: 1:339/342 of query aligns to 1:339/343 of Q5SKS4
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
41% identity, 99% coverage: 1:339/342 of query aligns to 3:343/347 of 3gfbA
- active site: C40 (= C38), G41 (= G39), T42 (= T40), H45 (= H43), H65 (= H63), E66 (= E64), C95 (≠ Q93), C98 (≠ S96), C101 (≠ S99), C109 (≠ D107), K113 (≠ R111), P151 (= P149), A155 (= A153), K340 (= K336)
- binding nicotinamide-adenine-dinucleotide: G173 (= G171), G175 (= G173), P176 (= P174), L177 (≠ I175), S196 (≠ T194), E197 (≠ D195), P198 (≠ I196), R202 (= R200), F241 (≠ M240), S242 (= S241), A244 (≠ S243), L264 (= L263), G265 (= G264), L266 (≠ I265), I289 (≠ V287), T290 (≠ Y288)
Q5JI69 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
41% identity, 99% coverage: 1:339/342 of query aligns to 5:345/350 of Q5JI69
Q00796 Sorbitol dehydrogenase; SDH; (R,R)-butanediol dehydrogenase; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Ribitol dehydrogenase; RDH; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.4; EC 1.1.1.14; EC 1.1.1.56; EC 1.1.1.9 from Homo sapiens (Human) (see 10 papers)
30% identity, 96% coverage: 13:341/342 of query aligns to 20:350/357 of Q00796
- C45 (= C38) binding
- H70 (= H63) binding
- E71 (= E64) binding
- R110 (≠ K103) to P: in SORDD; results in protein aggregation
- H135 (≠ L127) to R: in SORDD; results in protein aggregation
- A153 (= A145) to D: in SORDD; uncertain significance; results in protein aggregation; dbSNP:rs145813597
- I184 (= I175) binding
- D204 (= D195) binding
- R209 (= R200) binding
- Q239 (≠ E227) to L: in dbSNP:rs1042079
- N269 (≠ K259) to T: in dbSNP:rs930337
- VGL 273:275 (≠ LGI 263:265) binding
- VF--R 297:299 (≠ VYGRE 287:291) binding
- V322 (≠ I313) to I: in SORDD; uncertain significance; dbSNP:rs149975952
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pl6A Human sdh/nadh/inhibitor complex (see paper)
30% identity, 96% coverage: 13:341/342 of query aligns to 19:349/356 of 1pl6A
- active site: C44 (= C38), G45 (= G39), S46 (≠ T40), H49 (= H43), H69 (= H63), E70 (= E64), R99 (≠ Q93), D102 (≠ S96), C105 (≠ S99), S113 (≠ D107), F117 (≠ R111), P156 (= P149), G160 (≠ A153), K344 (= K336)
- binding 4-[2-(hydroxymethyl)pyrimidin-4-yl]-n,n-dimethylpiperazine-1-sulfonamide: C44 (= C38), S46 (≠ T40), I56 (≠ W50), F59 (≠ H53), H69 (= H63), E155 (≠ D148), L274 (≠ I265), F297 (≠ Y288)
- binding nicotinamide-adenine-dinucleotide: G181 (= G173), P182 (= P174), I183 (= I175), D203 (= D195), L204 (≠ I196), R208 (= R200), C249 (≠ M240), T250 (≠ S241), V272 (≠ L263), G273 (= G264), L274 (≠ I265), F297 (≠ Y288), R298 (≠ E291)
- binding zinc ion: C44 (= C38), H69 (= H63)
P27867 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 from Rattus norvegicus (Rat) (see paper)
31% identity, 94% coverage: 19:341/342 of query aligns to 26:350/357 of P27867
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
30% identity, 92% coverage: 21:333/342 of query aligns to 22:347/357 of 7y9pA
3qe3A Sheep liver sorbitol dehydrogenase (see paper)
31% identity, 96% coverage: 13:341/342 of query aligns to 14:344/351 of 3qe3A
- active site: C39 (= C38), G40 (= G39), S41 (≠ T40), H44 (= H43), H64 (= H63), E65 (= E64), R94 (≠ I92), D97 (= D95), C100 (≠ S99), S108 (≠ D107), F112 (≠ R111), P151 (= P149), G155 (≠ A153), K339 (= K336)
- binding glycerol: Y45 (≠ I44), F54 (≠ H53), T116 (≠ V115), R293 (≠ E291)
- binding zinc ion: C39 (= C38), H64 (= H63), E65 (= E64)
B6HI95 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) (see paper)
29% identity, 97% coverage: 7:337/342 of query aligns to 15:365/385 of B6HI95
- DI 212:213 (= DI 195:196) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ K330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
P07846 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 from Ovis aries (Sheep) (see paper)
31% identity, 96% coverage: 13:341/342 of query aligns to 18:347/354 of P07846
- C43 (= C38) binding
- Y49 (≠ I44) binding
- H67 (= H63) binding
- E68 (= E64) binding
- E153 (≠ D148) binding
- R296 (≠ E291) binding
- Y297 (≠ M292) binding
A2QAC0 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) (see 2 papers)
29% identity, 97% coverage: 7:337/342 of query aligns to 16:366/386 of A2QAC0
- M70 (≠ H53) mutation to F: Abolishes enzyme activity.
- DI 213:214 (= DI 195:196) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
- Y318 (≠ R290) mutation to F: Increases affinity for D-sorbitol.
- A359 (≠ K330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214.
Q7SI09 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see 2 papers)
29% identity, 97% coverage: 7:337/342 of query aligns to 14:355/363 of Q7SI09
- C53 (= C38) binding
- F59 (≠ I44) mutation F->A,S,Y: No effect.
- H78 (= H63) binding
- E79 (= E64) binding
- C108 (≠ Q93) binding
- C111 (≠ S96) binding
- C114 (≠ S99) binding
- C122 (≠ T110) binding
- E163 (≠ D148) binding
- PI 190:191 (= PI 174:175) binding
- D211 (= D195) binding
- DI 211:212 (= DI 195:196) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (= R200) binding
- I282 (≠ L263) binding
- QY--R 306:308 (≠ VYGRE 287:291) binding
- S348 (≠ K330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
3m6iA L-arabinitol 4-dehydrogenase (see paper)
29% identity, 97% coverage: 7:337/342 of query aligns to 10:351/358 of 3m6iA
- active site: C49 (= C38), G50 (= G39), S51 (≠ T40), H54 (= H43), H74 (= H63), E75 (= E64), C104 (≠ Q93), C107 (≠ S96), C110 (≠ S99), C118 (≠ T110), D122 (≠ G114), P160 (= P149), A164 (= A153)
- binding nicotinamide-adenine-dinucleotide: C49 (= C38), V163 (≠ N152), G185 (= G173), P186 (= P174), I187 (= I175), D207 (= D195), R212 (= R200), C255 (≠ M240), T256 (≠ S241), I278 (≠ L263), G279 (= G264), V280 (≠ I265), R304 (≠ E291)
- binding zinc ion: C49 (= C38), H74 (= H63), C104 (≠ Q93), C107 (≠ S96), C110 (≠ S99), C118 (≠ T110)
Sites not aligning to the query:
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
29% identity, 97% coverage: 7:337/342 of query aligns to 27:369/377 of Q96V44
- DI 224:225 (= DI 195:196) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ K330) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
Query Sequence
>GFF3379 FitnessBrowser__Phaeo:GFF3379
MKALEKSHPREGLWMVQAPVPEIGPDEVLIKIRTTGICGTDIHIWNWDEWASHTVPVPMI
TGHEFAGEIVEIGRNVTDLAVGQRCSGEGHLIQTDSRQSRAGKFHLDPGTRGIGVNEQGA
FAQYLKLPAFNVVPLPEDIPDEIGAILDPLGNAVHTALSFDLLGEDVLITGAGPIGVMAA
AVARHAGARHVVITDINPDRLALAEHVVPAVRAVNVAEEDLQDVVRELGLKQGFDVGLEM
SGSQAALDQMVEALVMGGKIALLGIPPGKSPVDWSRIVFKAITIKGVYGREMFETWYKMI
AMLQNGLDVSRVITHRFDVEDFAEGFAAMKSGRSGKVVLRWP
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