SitesBLAST
Comparing 349881 FitnessBrowser__Btheta:349881 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
62% identity, 100% coverage: 1:227/227 of query aligns to 1:231/231 of P08203
- N28 (= N28) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (= K42) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (= D75) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- H95 (= H94) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H96) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
- T116 (= T115) mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
- D120 (= D119) mutation to N: Loss of the epimerase activity.
- E142 (= E141) mutation to Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- H171 (= H168) binding
- H218 (= H214) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- Y229 (= Y225) mutation to F: Loss of the epimerase activity.
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
61% identity, 96% coverage: 1:219/227 of query aligns to 1:223/223 of 1jdiA
P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
31% identity, 87% coverage: 1:198/227 of query aligns to 2:184/213 of P0DTQ0
- E76 (≠ D75) binding
- H95 (= H94) binding
- H97 (= H96) binding
- H157 (= H168) binding
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
31% identity, 87% coverage: 1:198/227 of query aligns to 2:184/207 of 6btgA
4c25A L-fuculose 1-phosphate aldolase (see paper)
30% identity, 85% coverage: 4:197/227 of query aligns to 8:189/212 of 4c25A
Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
30% identity, 80% coverage: 22:202/227 of query aligns to 19:181/181 of Q58813
- N25 (= N28) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.
P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 55% coverage: 4:127/227 of query aligns to 5:125/215 of P0AB87
- T26 (= T25) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (≠ W26) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 27:28) binding
- N29 (= N28) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- TG 43:44 (≠ SG 44:45) binding
- S71 (= S73) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (= SS 73:74) binding
- E73 (≠ D75) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
- H92 (= H94) binding
- H94 (= H96) binding
- Y113 (≠ T115) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
Sites not aligning to the query:
- 131 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; F→A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
- 155 binding
- 206 F→W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
- 207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
- 209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
- 211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
33% identity, 55% coverage: 4:127/227 of query aligns to 5:125/210 of 2fuaA
Sites not aligning to the query:
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
33% identity, 55% coverage: 4:127/227 of query aligns to 5:125/206 of 4fuaA
- active site: E73 (≠ D75), H92 (= H94), H94 (= H96), Y113 (≠ T115), A117 (≠ D119)
- binding phosphoglycolohydroxamic acid: G28 (= G27), N29 (= N28), T43 (≠ S44), S71 (= S73), S72 (= S74), E73 (≠ D75), H92 (= H94), H94 (= H96)
- binding zinc ion: H92 (= H94), H94 (= H96)
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
32% identity, 55% coverage: 4:127/227 of query aligns to 5:125/209 of 1dzuP
Sites not aligning to the query:
7x78A L-fuculose 1-phosphate aldolase (see paper)
31% identity, 55% coverage: 4:127/227 of query aligns to 5:122/203 of 7x78A
Sites not aligning to the query:
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
26% identity, 84% coverage: 3:193/227 of query aligns to 5:186/207 of 6voqA
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
22% identity, 74% coverage: 41:207/227 of query aligns to 59:211/249 of 4xxfA
P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
22% identity, 97% coverage: 7:227/227 of query aligns to 142:362/737 of P35611
Sites not aligning to the query:
- 59 modified: Phosphoserine; by PKA
- 408 modified: Phosphoserine; by PKA
- 436 modified: Phosphoserine; by PKA
- 445 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-480.
- 460 G → W: in dbSNP:rs4961
- 480 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-445.
- 481 modified: Phosphoserine; by PKA
- 586 S → C: in dbSNP:rs4963
- 716 modified: Phosphoserine; by PKC
- 726 modified: Phosphoserine; by PKA and PKC
P35612 Beta-adducin; Erythrocyte adducin subunit beta from Homo sapiens (Human) (see 2 papers)
22% identity, 94% coverage: 7:219/227 of query aligns to 130:340/726 of P35612
Sites not aligning to the query:
- 55 modified: Phosphothreonine; by PKA
- 439 T → A: in dbSNP:rs17855969
- 703 modified: Phosphoserine; by PKC
- 713 modified: Phosphoserine; by PKA and PKC
Q9QYB5 Gamma-adducin; Adducin-like protein 70 from Mus musculus (Mouse) (see paper)
20% identity, 70% coverage: 23:182/227 of query aligns to 150:308/706 of Q9QYB5
Sites not aligning to the query:
- 357 Cleavage by asparagine endopeptidase (AEP); N→A: Loss of cleavage by asparagine endopeptidase (AEP).
- 450 N→A: No effect on cleavage by asparagine endopeptidase (AEP).
- 457 N→A: No effect on cleavage by asparagine endopeptidase (AEP).
Q96GX9 Methylthioribulose-1-phosphate dehydratase; MTRu-1-P dehydratase; APAF1-interacting protein; hAPIP; EC 4.2.1.109 from Homo sapiens (Human) (see 5 papers)
31% identity, 44% coverage: 1:100/227 of query aligns to 27:121/242 of Q96GX9
- C76 (≠ V59) to Y: in dbSNP:rs1977420
- S84 (≠ E67) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.
- S87 (vs. gap) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.
- S89 (vs. gap) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.
- Q96 (≠ S74) mutation to A: Mildly reduced enzyme activity.
- C97 (≠ D75) mutation to A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
- H115 (= H94) mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.; mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.
- H117 (= H96) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.
Sites not aligning to the query:
- 7 R → W: in dbSNP:rs2956114
- 23 H → R: in dbSNP:rs17850326
- 139 active site, Proton donor/acceptor; E→A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
- 181 M → V: in dbSNP:rs17850327
- 195 H→A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.
4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
31% identity, 44% coverage: 1:100/227 of query aligns to 9:103/224 of 4m6rA
Sites not aligning to the query:
Query Sequence
>349881 FitnessBrowser__Btheta:349881
MLEELKEKVFHANLELVKHGLVIFTWGNVSAIDRETELVVIKPSGVSYDDMKAEDMVVVD
LDGKVVEGRLKPSSDTPTHVVLYKAFPEIGGVVHTHSTYATAWAQAGCDIPNIGTTHADY
FHDAIPCTADMTEAEVKGAYELETGNVIVKRFEGLNPVHTPGVLVKNHGPFSWGKDAHDA
VHNAVVMEQVAKMASIAYAVNPNLTMNPLLVEKHFSRKHGPNAYYGQ
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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