SitesBLAST
Comparing Synpcc7942_0645 Synpcc7942_0645 glutamate-1-semialdehyde aminotransferase 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)
2gsaB Crystal structure of glutamate-1-semialdehyde aminomutase (aminotransferase, wild-type form) (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 2gsaB
- active site: V21 (= V47), Y144 (= Y170), E206 (= E232), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding pyridoxal-5'-phosphate: G117 (= G143), T118 (= T144), Y144 (= Y170), E206 (= E232), N211 (= N237), D239 (= D265), V241 (= V267), M242 (= M268), K267 (= K293)
2gsaA Crystal structure of glutamate-1-semialdehyde aminomutase (aminotransferase, wild-type form) (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 2gsaA
- active site: V21 (= V47), Y144 (= Y170), E206 (= E232), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G143), T118 (= T144), Y144 (= Y170), H145 (= H171), G146 (= G172), N211 (= N237), D239 (= D265), V241 (= V267), K267 (= K293)
3usfA Crystal structure of dava-4
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 3usfA
- active site: V21 (= V47), Y144 (= Y170), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding (4s)-4,5-diaminopentanoic acid: S23 (= S49), V25 (= V51), S157 (= S183), K267 (= K293), E400 (= E426)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G117 (= G143), T118 (= T144), Y144 (= Y170), N211 (= N237), D239 (= D265), V241 (= V267), K267 (= K293)
3fq7A Gabaculine complex of gsam (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 3fq7A
- active site: V21 (= V47), Y144 (= Y170), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: S23 (= S49), V25 (= V51), W61 (= W87), G117 (= G143), T118 (= T144), Y144 (= Y170), H145 (= H171), E206 (= E232), N211 (= N237), D239 (= D265), V241 (= V267), M242 (= M268), K267 (= K293), G298 (= G324), T299 (= T325), E400 (= E426)
2hp2A Inter-subunit signaling in gsam (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 2hp2A
- active site: V21 (= V47), Y144 (= Y170), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding (4s)-4,5-diaminopentanoic acid: G298 (= G324), T299 (= T325)
- binding (4r)-5-amino-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: S23 (= S49), G117 (= G143), T118 (= T144), Y144 (= Y170), H145 (= H171), E206 (= E232), N211 (= N237), D239 (= D265), V241 (= V267), M242 (= M268), K267 (= K293)
- binding pyridoxal-5'-phosphate: G298 (= G324), T299 (= T325)
2hp1A Inter-subunit signaling in gsam (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 2hp1A
- active site: V21 (= V47), Y144 (= Y170), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding (4s)-4-amino-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: S23 (= S49), V25 (= V51), W61 (= W87), S116 (= S142), G117 (= G143), T118 (= T144), Y144 (= Y170), H145 (= H171), G146 (= G172), E206 (= E232), N211 (= N237), D239 (= D265), V241 (= V267), M242 (= M268), K267 (= K293), E400 (= E426)
2hozA Inter-subunit signaling in gsam (see paper)
99% identity, 94% coverage: 27:453/453 of query aligns to 1:427/427 of 2hozA
- active site: V21 (= V47), Y144 (= Y170), D239 (= D265), M242 (= M268), K267 (= K293), A401 (= A427)
- binding (4s)-4,5-diaminopentanoic acid: E141 (= E167), G156 (= G182), S157 (= S183), P182 (= P208), N368 (= N394), E370 (= E396), K373 (= K399)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G143), T118 (= T144), Y144 (= Y170), H145 (= H171), G146 (= G172), E206 (= E232), N211 (= N237), D239 (= D265), G298 (= G324), T299 (= T325)
3fqaA Gabaculien complex of gabaculine resistant gsam version (see paper)
99% identity, 94% coverage: 28:453/453 of query aligns to 1:426/426 of 3fqaA
- active site: V20 (= V47), Y143 (= Y170), D238 (= D265), I241 (≠ M268), K266 (= K293), A400 (= A427)
- binding 3-aminobenzoic acid: S22 (= S49), R25 (= R52), W60 (= W87)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G116 (= G143), T117 (= T144), Y143 (= Y170), E205 (= E232), N210 (= N237), D238 (= D265), V240 (= V267), I241 (≠ M268)
3usfB Crystal structure of dava-4
93% identity, 94% coverage: 27:453/453 of query aligns to 1:402/402 of 3usfB
- active site: V21 (= V47), Y144 (= Y170), E181 (= E232), D214 (= D265), M217 (= M268), K242 (= K293), A376 (= A427)
- binding (4s)-4,5-diaminopentanoic acid: G273 (= G324), T274 (= T325)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G117 (= G143), T118 (= T144), Y144 (= Y170), E181 (= E232), N186 (= N237), D214 (= D265), V216 (= V267), M217 (= M268), K242 (= K293)
2hp1B Inter-subunit signaling in gsam (see paper)
93% identity, 94% coverage: 27:453/453 of query aligns to 1:398/398 of 2hp1B
- active site: V21 (= V47), Y144 (= Y170), E177 (= E232), D210 (= D265), M213 (= M268), K238 (= K293), A372 (= A427)
- binding (4s)-4-amino-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: G269 (= G324), T270 (= T325)
- binding (4s)-4,5-diaminopentanoic acid: S23 (= S49), V25 (= V51), R26 (= R52), W61 (= W87), Y144 (= Y170)
- binding pyridoxal-5'-phosphate: S116 (= S142), G117 (= G143), T118 (= T144), Y144 (= Y170), E177 (= E232), N182 (= N237), D210 (= D265), V212 (= V267), M213 (= M268), K238 (= K293)
Q42522 Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic; GSA 2; Glutamate-1-semialdehyde aminotransferase 2; GSA-AT 2; EC 5.4.3.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
74% identity, 95% coverage: 24:453/453 of query aligns to 43:472/472 of Q42522
- R92 (≠ W73) mutation to K: In gsa2-1; suppression of enf1 mutant pleiotropic developmental phenotypes; when associated with S-162.
- G162 (= G143) mutation to S: In gsa2-1; suppression of enf1 mutant pleiotropic developmental phenotypes; when associated with K-92.
P42799 Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic; AtGSA1; GSA 1; Glutamate-1-semialdehyde aminotransferase 1; GSA-AT 1; EC 5.4.3.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
70% identity, 100% coverage: 2:453/453 of query aligns to 22:474/474 of P42799
- K314 (= K293) modified: N6-(pyridoxal phosphate)lysine
5hdmB Crystal structure of arabidopsis thaliana glutamate-1-semialdehyde-2, 1-aminomutase (see paper)
73% identity, 94% coverage: 27:453/453 of query aligns to 2:428/428 of 5hdmB
- active site: V22 (= V47), Y145 (= Y170), E207 (= E232), D240 (= D265), M243 (= M268), K268 (= K293), A402 (= A427)
- binding pyridoxal-5'-phosphate: G118 (= G143), T119 (= T144), Y145 (= Y170), E207 (= E232), N212 (= N237), D240 (= D265), V242 (= V267), M243 (= M268), K268 (= K293)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G118 (= G143), T119 (= T144), Y145 (= Y170), E207 (= E232), N212 (= N237), D240 (= D265), V242 (= V267), M243 (= M268), K268 (= K293)
5hdmA Crystal structure of arabidopsis thaliana glutamate-1-semialdehyde-2, 1-aminomutase (see paper)
73% identity, 94% coverage: 27:453/453 of query aligns to 2:428/428 of 5hdmA
- active site: V22 (= V47), Y145 (= Y170), E207 (= E232), D240 (= D265), M243 (= M268), K268 (= K293), A402 (= A427)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G118 (= G143), T119 (= T144), Y145 (= Y170), G147 (= G172), E207 (= E232), N212 (= N237), D240 (= D265), V242 (= V267), K268 (= K293)
2cfbA Glutamate-1-semialdehyde 2,1-aminomutase from thermosynechococcus elongatus (see paper)
73% identity, 87% coverage: 61:453/453 of query aligns to 1:360/360 of 2cfbA
- active site: Y110 (= Y170), E144 (= E232), D177 (= D265), M180 (= M268), K205 (= K293), A334 (= A427)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G83 (= G143), T84 (= T144), Y110 (= Y170), E144 (= E232), D177 (= D265), V179 (= V267), M180 (= M268), K205 (= K293)
3bs8A Crystal structure of glutamate 1-semialdehyde aminotransferase complexed with pyridoxamine-5'-phosphate from bacillus subtilis (see paper)
59% identity, 93% coverage: 31:453/453 of query aligns to 6:427/430 of 3bs8A
- active site: V22 (= V47), Y145 (= Y170), E207 (= E232), D240 (= D265), M243 (= M268), K268 (= K293), G401 (≠ A427)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G118 (= G143), T119 (= T144), Y145 (= Y170), H146 (= H171), E207 (= E232), N212 (= N237), D240 (= D265), V242 (= V267), K268 (= K293)
6w80A Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from stenotrophomonas maltophilia k279a in complex with plp
59% identity, 91% coverage: 31:443/453 of query aligns to 10:419/430 of 6w80A
- active site: V26 (= V47), Y149 (= Y170), D241 (= D265), K269 (= K293)
- binding pyridoxal-5'-phosphate: S121 (= S142), G122 (= G143), T123 (= T144), Y149 (= Y170), H150 (= H171), E208 (= E232), N213 (= N237), D241 (= D265), V243 (= V267), K269 (= K293)
P23893 Glutamate-1-semialdehyde 2,1-aminomutase; GSA; Glutamate-1-semialdehyde aminotransferase; GSA-AT; EC 5.4.3.8 from Escherichia coli (strain K12) (see paper)
56% identity, 93% coverage: 31:453/453 of query aligns to 3:426/426 of P23893
- K265 (= K293) mutation to R: 2% of wild-type activity.
5i92F Crystal structure of glutamate-1-semialdehyde 2,1- aminomutase (gsa) from pseudomonas aeruginosa
55% identity, 93% coverage: 31:452/453 of query aligns to 3:420/420 of 5i92F
3k28A Crystal structure of a glutamate-1-semialdehyde aminotransferase from bacillus anthracis with bound pyridoxal 5'phosphate
58% identity, 94% coverage: 28:453/453 of query aligns to 3:422/423 of 3k28A
- active site: V22 (= V47), Y145 (= Y170), E202 (= E232), D235 (= D265), M238 (= M268), K263 (= K293), G396 (≠ A427)
- binding calcium ion: I103 (= I128), V106 (= V131), P107 (= P132), I109 (= I134)
- binding pyridoxal-5'-phosphate: G118 (= G143), T119 (= T144), Y145 (= Y170), H146 (= H171), G147 (= G172), E202 (= E232), D235 (= D265), V237 (= V267), M238 (= M268), K263 (= K293)
Query Sequence
>Synpcc7942_0645 Synpcc7942_0645 glutamate-1-semialdehyde aminotransferase
MRRLSASLAGDARLVCEEIALVTSSPFKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQ
PIVFDRVKDAYAWDVDGNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALE
NVLAEMVIDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVK
AGSGVATLGLPDSPGVPKSTTANTLTAPYNDLEAVKALFAENPGEIAGVILEPIVGNSGF
IVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLP
VGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLS
DGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYL
APSQFEAGFTSLAHTEEDIDATLAAARTVMSAL
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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