SitesBLAST
Comparing PP_0209 FitnessBrowser__Putida:PP_0209 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)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
45% identity, 81% coverage: 27:255/283 of query aligns to 21:253/257 of 8wm7D
Sites not aligning to the query:
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
45% identity, 81% coverage: 27:255/283 of query aligns to 19:251/256 of 8w9mD
- binding adenosine-5'-triphosphate: H40 (≠ P48), S41 (= S49), G42 (= G50), G44 (= G52), K45 (= K53), S46 (= S54), T47 (= T55), Q82 (= Q90), Q135 (= Q141), S137 (= S143), G139 (= G145), M140 (= M146), H194 (= H200)
- binding magnesium ion: S46 (= S54), Q82 (= Q90)
Sites not aligning to the query:
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
39% identity, 90% coverage: 27:282/283 of query aligns to 20:293/658 of 8wm7C
Sites not aligning to the query:
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
41% identity, 82% coverage: 27:259/283 of query aligns to 20:256/256 of 8w9mC
- binding adenosine-5'-triphosphate: Y20 (≠ F27), S42 (= S49), G43 (= G50), G45 (= G52), K46 (= K53), S47 (= S54), T48 (= T55), Q83 (= Q90), K132 (≠ R137), E136 (≠ Q141), S138 (= S143), G140 (= G145), H195 (= H200)
- binding magnesium ion: S47 (= S54), Q83 (= Q90)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 70% coverage: 28:225/283 of query aligns to 31:229/378 of P69874
- F45 (= F42) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C51) mutation to T: Loss of ATPase activity and transport.
- L60 (= L57) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V73) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
44% identity, 70% coverage: 28:225/283 of query aligns to 16:214/358 of 8y5iA
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
42% identity, 66% coverage: 30:216/283 of query aligns to 42:237/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
42% identity, 66% coverage: 30:216/283 of query aligns to 42:237/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
41% identity, 66% coverage: 30:216/283 of query aligns to 42:237/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S49), G62 (= G50), G64 (= G52), K65 (= K53), S66 (= S54), T67 (= T55), Q111 (= Q90), K161 (≠ N140), Q162 (= Q141), S164 (= S143), G166 (= G145), M167 (= M146), Q188 (≠ E167), H221 (= H200)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
39% identity, 66% coverage: 29:216/283 of query aligns to 21:217/375 of 2d62A
1g291 Malk (see paper)
40% identity, 66% coverage: 29:216/283 of query aligns to 18:214/372 of 1g291
- binding magnesium ion: D69 (≠ S82), E71 (≠ Q84), K72 (≠ R85), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S49), G39 (= G50), C40 (= C51), G41 (= G52), K42 (= K53), T43 (≠ S54), T44 (= T55)
Sites not aligning to the query:
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 70% coverage: 18:215/283 of query aligns to 4:208/393 of P9WQI3
- H193 (= H200) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 66% coverage: 29:215/283 of query aligns to 16:205/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
37% identity, 66% coverage: 29:215/283 of query aligns to 18:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S49), G39 (= G50), G41 (= G52), K42 (= K53), S43 (= S54), Q82 (= Q90), Q133 (= Q141), G136 (= G144), G137 (= G145), Q138 (≠ M146), H192 (= H200)
- binding magnesium ion: S43 (= S54), Q82 (= Q90)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
37% identity, 66% coverage: 29:215/283 of query aligns to 18:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S49), C40 (= C51), G41 (= G52), K42 (= K53), S43 (= S54), T44 (= T55), Q82 (= Q90), R129 (= R137), Q133 (= Q141), S135 (= S143), G136 (= G144), G137 (= G145), Q159 (≠ E167), H192 (= H200)
- binding magnesium ion: S43 (= S54), Q82 (= Q90)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 90% coverage: 17:272/283 of query aligns to 3:267/369 of P19566
- L86 (= L94) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 70% coverage: 17:215/283 of query aligns to 3:207/371 of P68187
- A85 (≠ T93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ H119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
40% identity, 70% coverage: 17:215/283 of query aligns to 2:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F27), S37 (= S49), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), Q81 (= Q90), R128 (= R137), A132 (≠ Q141), S134 (= S143), G136 (= G145), Q137 (≠ M146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 70% coverage: 17:215/283 of query aligns to 2:206/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F27), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (= R137), S134 (= S143), Q137 (≠ M146)
- binding beryllium trifluoride ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q90), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 70% coverage: 17:215/283 of query aligns to 2:206/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F27), V17 (vs. gap), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (= R137), A132 (≠ Q141), S134 (= S143), Q137 (≠ M146)
- binding tetrafluoroaluminate ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
Query Sequence
>PP_0209 FitnessBrowser__Putida:PP_0209
MNRYQQAPGRIDGRGLSIRLGHGSEAFEAVQRLDFAVEPGEFVCILGPSGCGKSTLLGAL
AGHLVPSSGQLNVDGQPVDGPSPQRGMVFQHHTLLPWRSVLDNVAFGLKMQGLERTERHR
QAREMLQLVGLADFAGRWPNQLSGGMQQRAEIARVLINRPRLLLMDEPFGALDAQTRARM
QELLLDIWASIRTTVLFVTHDIDEALFLADRILVMSPRPGRFIEDLRLDFARPRRASLLT
SPEFTHLKRHCLALLRHEEGRELPRLTPLGLPDTDHPPLRIAL
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