SitesBLAST
Comparing 6939514 FitnessBrowser__SB2B:6939514 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)
7vo1A Structure of aminotransferase-substrate complex (see paper)
31% identity, 94% coverage: 6:451/472 of query aligns to 1:443/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ W77), S121 (= S133), G122 (= G134), T123 (= T135), F149 (= F161), H150 (= H162), R152 (≠ E164), E234 (= E241), D262 (= D269), V264 (= V271), Q265 (≠ L272), K291 (= K298), N318 (≠ S327), T319 (= T328), R417 (= R425)
7vntA Structure of aminotransferase-substrate complex (see paper)
31% identity, 94% coverage: 6:451/472 of query aligns to 1:443/452 of 7vntA
- binding L-ornithine: F149 (= F161), R152 (≠ E164), E234 (= E241), K291 (= K298)
- binding pyridoxal-5'-phosphate: G122 (= G134), T123 (= T135), F149 (= F161), H150 (= H162), E229 (= E236), D262 (= D269), V264 (= V271), Q265 (≠ L272), K291 (= K298)
7vnoA Structure of aminotransferase (see paper)
31% identity, 94% coverage: 6:451/472 of query aligns to 1:443/452 of 7vnoA
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
31% identity, 94% coverage: 6:451/472 of query aligns to 3:445/454 of O50131
- T92 (≠ F102) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ H103) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G134) binding
- T125 (= T135) binding
- Q267 (≠ L272) binding
- K293 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T328) binding
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 86% coverage: 40:446/472 of query aligns to 13:419/426 of P22256
- I50 (≠ W77) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 134:135) binding
- E211 (= E241) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V271) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (≠ L272) binding
- K268 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T328) binding
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
31% identity, 89% coverage: 35:453/472 of query aligns to 19:443/448 of 4ysnC
- active site: A29 (≠ G45), Y149 (≠ F161), E224 (= E236), D257 (= D269), N260 (≠ L272), K287 (= K298), T316 (= T328), R415 (= R425)
- binding pyridoxal-5'-phosphate: S121 (= S133), G122 (= G134), S123 (≠ T135), Y149 (≠ F161), H150 (= H162), E224 (= E236), D257 (= D269), V259 (= V271), K287 (= K298), F315 (≠ S327), T316 (= T328)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 86% coverage: 40:446/472 of query aligns to 12:418/425 of 1sffA
- active site: V18 (≠ Y46), Y137 (≠ F161), E205 (= E236), D238 (= D269), Q241 (≠ L272), K267 (= K298), T296 (= T328), R397 (= R425)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ G101), G110 (= G134), S111 (≠ T135), Y137 (≠ F161), H138 (= H162), R140 (≠ E164), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (≠ L272), K267 (= K298), T296 (= T328)
- binding sulfate ion: N152 (= N176), Y393 (≠ Q421)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 86% coverage: 40:446/472 of query aligns to 12:418/425 of 1sf2A
- active site: V18 (≠ Y46), Y137 (≠ F161), E205 (= E236), D238 (= D269), Q241 (≠ L272), K267 (= K298), T296 (= T328), R397 (= R425)
- binding pyridoxal-5'-phosphate: G110 (= G134), S111 (≠ T135), Y137 (≠ F161), H138 (= H162), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (≠ L272), K267 (= K298)
- binding sulfate ion: N152 (= N176), Y393 (≠ Q421)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
31% identity, 89% coverage: 35:453/472 of query aligns to 10:434/439 of 5wyaA
- active site: A20 (≠ G45), Y140 (≠ F161), E215 (= E236), D248 (= D269), N251 (≠ L272), K278 (= K298), T307 (= T328), R406 (= R425)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ W77), Y82 (≠ R109), S112 (= S133), G113 (= G134), S114 (≠ T135), Y140 (≠ F161), H141 (= H162), E215 (= E236), D248 (= D269), V250 (= V271), N251 (≠ L272), K278 (= K298), F306 (≠ S327), T307 (= T328), R406 (= R425)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
31% identity, 89% coverage: 35:453/472 of query aligns to 12:436/446 of 5wyfA
- active site: A22 (≠ G45), Y142 (≠ F161), E217 (= E236), D250 (= D269), N253 (≠ L272), K280 (= K298), T309 (= T328), R408 (= R425)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ W77), Y84 (≠ R109), G115 (= G134), S116 (≠ T135), Y142 (≠ F161), H143 (= H162), D222 (≠ E241), D250 (= D269), V252 (= V271), N253 (≠ L272), K280 (= K298), F308 (≠ S327), T309 (= T328), R408 (= R425)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
29% identity, 94% coverage: 7:448/472 of query aligns to 22:458/474 of O58478
- D251 (≠ E241) mutation to A: Loss of activity.
- K308 (= K298) mutation to A: Loss of activity.
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
30% identity, 86% coverage: 40:446/472 of query aligns to 12:418/425 of 1szkA
- active site: V18 (≠ Y46), Y137 (≠ F161), E205 (= E236), D238 (= D269), Q241 (≠ L272), K267 (= K298), T296 (= T328), R397 (= R425)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G134), S111 (≠ T135), Y137 (≠ F161), H138 (= H162), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (≠ L272), K267 (= K298)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
29% identity, 85% coverage: 52:451/472 of query aligns to 26:412/412 of 2eo5A
- active site: F139 (= F161), E219 (= E236), D252 (= D269), Q255 (≠ L272), K281 (= K298), T303 (= T328), R386 (= R425)
- binding pyridoxal-5'-phosphate: G113 (= G134), T114 (= T135), F139 (= F161), H140 (= H162), E219 (= E236), D252 (= D269), V254 (= V271), Q255 (≠ L272), K281 (= K298)
Sites not aligning to the query:
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
29% identity, 94% coverage: 7:451/472 of query aligns to 7:438/439 of 3q8nC
- active site: V32 (≠ Y46), Y151 (≠ F161), E221 (= E236), D254 (= D269), Q257 (≠ L272), K283 (= K298), T312 (= T328), R412 (= R425)
- binding 4-oxobutanoic acid: G124 (= G134), A125 (≠ T135), V256 (= V271), K283 (= K298)
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
30% identity, 83% coverage: 57:449/472 of query aligns to 29:420/421 of P50457
- K267 (= K298) mutation to A: No GABA-AT activity.
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
32% identity, 84% coverage: 56:453/472 of query aligns to 25:400/401 of 4adbB
- active site: F136 (= F161), E188 (= E236), D221 (= D269), Q224 (≠ L272), K250 (= K298), T279 (= T328), R372 (= R425)
- binding pyridoxal-5'-phosphate: S102 (= S133), G103 (= G134), A104 (≠ T135), F136 (= F161), H137 (= H162), D221 (= D269), V223 (= V271), Q224 (≠ L272), K250 (= K298)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
32% identity, 84% coverage: 56:453/472 of query aligns to 25:400/400 of 4addA
- active site: F136 (= F161), E188 (= E236), D221 (= D269), Q224 (≠ L272), K250 (= K298), T279 (= T328), R372 (= R425)
- binding pyridoxal-5'-phosphate: G103 (= G134), A104 (≠ T135), F136 (= F161), H137 (= H162), D221 (= D269), V223 (= V271), K250 (= K298)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F161), R139 (≠ E164)
Sites not aligning to the query:
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
30% identity, 80% coverage: 58:434/472 of query aligns to 26:369/390 of A0QYS9
- K304 (≠ E360) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P42588 Putrescine aminotransferase; PAT; PATase; Cadaverine transaminase; Diamine transaminase; Putrescine transaminase; Putrescine--2-oxoglutaric acid transaminase; Putrescine:2-OG aminotransferase; EC 2.6.1.82; EC 2.6.1.29 from Escherichia coli (strain K12) (see paper)
30% identity, 79% coverage: 62:432/472 of query aligns to 76:433/459 of P42588
- GT 150:151 (= GT 134:135) binding in other chain
- Q274 (≠ L272) binding in other chain
- K300 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T328) binding
4uoxC Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
30% identity, 79% coverage: 62:432/472 of query aligns to 74:431/456 of 4uoxC
- active site: F178 (= F161), E236 (= E236), D269 (= D269), Q272 (≠ L272), K298 (= K298), T330 (= T328), R424 (= R425)
- binding pyridoxal-5'-phosphate: S147 (= S133), G148 (= G134), T149 (= T135), F178 (= F161), H179 (= H162), G180 (= G163), D269 (= D269), V271 (= V271), Q272 (≠ L272), K298 (= K298), T329 (≠ S327), T330 (= T328)
Sites not aligning to the query:
Query Sequence
>6939514 FitnessBrowser__SB2B:6939514
MMNSIMKMNYKLPGPKSKAMLERGIPLFRNGLRYEEECKKAARRGYRGASQVVVGRAQGS
FVWDLDDNQYIDFQNGWASNPFGNAHPEIVEAVHWAHTRYGFHYDTPHRYELAEKLVQIM
PNRALTRINFEISGTEAAEAAVNLALTHTKRRYIISFSSSFHGEALGSKMLSGTSNNNHY
MEAWSGGVITAPYPYSGEIPAGMTQEQYVEYCLWYIDNHITSSIVPANNIAGLIIEPGLA
EGGNWIPPKRFMQGLRELCNKHDWVMIVDEVLTGLGRTGKMWAIEHYDVIPDVLVFGKNI
SGGIEPCAGIAARDEIMGDNEHYHTGSTYAGSPAACCAGLKTLELYERENIVEYVAYLGE
IAKGIMQKWTRYSIVNEVRCNGLLLGVNFVSPDEHQKDWWFAREVRSRMMENGVWAINDR
QTNVRLYPALNMEESVLREGLAIMEEAIAHVDSIRQSSFGDSPAWPTGDAGF
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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