SitesBLAST
Comparing WP_075860193.1 NCBI__GCF_001950255.1:WP_075860193.1 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)
4ppmA Crystal structure of pige: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (map) from serratia sp. Fs14 (see paper)
40% identity, 91% coverage: 27:453/470 of query aligns to 20:461/464 of 4ppmA
- active site: M35 (≠ L42), Y159 (≠ F163), E212 (= E216), D245 (= D249), Q248 (= Q252), K274 (= K278), T309 (= T313), R431 (= R423)
- binding magnesium ion: A351 (≠ Q355), Y354 (= Y358), V357 (≠ I361)
- binding pyridoxal-5'-phosphate: G132 (= G136), T133 (≠ A137), Y159 (≠ F163), H160 (= H164), D245 (= D249), V247 (≠ I251), K274 (= K278)
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
39% identity, 91% coverage: 27:453/470 of query aligns to 391:852/853 of A0A0J9X1Q5
- GT 503:504 (≠ GA 136:137) binding pyridoxal 5'-phosphate
- K645 (= K278) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T313) binding pyridoxal 5'-phosphate
4uoyA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate (see paper)
39% identity, 90% coverage: 21:444/470 of query aligns to 26:441/454 of 4uoyA
- active site: F44 (≠ L48), F174 (= F163), E232 (= E216), D265 (= D249), Q268 (= Q252), K294 (= K278), T326 (= T313), R420 (= R423)
- binding pyridoxal-5'-phosphate: G144 (= G136), T145 (≠ A137), F174 (= F163), H175 (= H164), G176 (= G165), E232 (= E216), D265 (= D249), V267 (≠ I251), Q268 (= Q252), K294 (= K278)
8cplC Yzw2 a scaffold for cryo-em of small proteins of interest
39% identity, 92% coverage: 21:452/470 of query aligns to 24:454/499 of 8cplC
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
39% identity, 90% coverage: 21:444/470 of query aligns to 26:441/453 of 4uoxA
- active site: F44 (≠ L48), F174 (= F163), E232 (= E216), D265 (= D249), Q268 (= Q252), K294 (= K278), T326 (= T313), R420 (= R423)
- binding pyridoxal-5'-phosphate: S143 (= S135), G144 (= G136), T145 (≠ A137), F174 (= F163), H175 (= H164), G176 (= G165), D265 (= D249), V267 (≠ I251), Q268 (= Q252), T325 (≠ S312), T326 (= T313)
- binding 1,4-diaminobutane: E237 (= E221), K294 (= K278)
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)
39% identity, 90% coverage: 21:444/470 of query aligns to 32:447/459 of P42588
- GT 150:151 (≠ GA 136:137) binding in other chain
- Q274 (= Q252) binding in other chain
- K300 (= K278) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T313) binding pyridoxal 5'-phosphate
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
41% identity, 84% coverage: 52:446/470 of query aligns to 28:394/395 of Q5SHH5
- GT 113:114 (≠ GA 136:137) binding pyridoxal 5'-phosphate
- K254 (= K278) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T313) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 84% coverage: 52:446/470 of query aligns to 20:386/387 of 1wkhA
- active site: F132 (= F163), E184 (= E216), D217 (= D249), Q220 (= Q252), K246 (= K278), T275 (= T313), R363 (= R423)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (= Y78), S104 (= S135), G105 (= G136), T106 (≠ A137), F132 (= F163), S133 (≠ H164), E184 (= E216), E189 (= E221), D217 (= D249), I219 (= I251), K246 (= K278), R363 (= R423)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 84% coverage: 52:446/470 of query aligns to 20:386/387 of 1wkgA
- active site: F132 (= F163), E184 (= E216), D217 (= D249), Q220 (= Q252), K246 (= K278), T275 (= T313), R363 (= R423)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (= Y78), G105 (= G136), T106 (≠ A137), F132 (= F163), S133 (≠ H164), R135 (≠ K166), E184 (= E216), D217 (= D249), I219 (= I251), Q220 (= Q252), K246 (= K278), G273 (≠ T311), T274 (≠ S312), T275 (= T313)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 84% coverage: 52:446/470 of query aligns to 20:386/387 of 1vefA
- active site: F132 (= F163), D217 (= D249), K246 (= K278), T275 (= T313), R363 (= R423)
- binding pyridoxal-5'-phosphate: G105 (= G136), T106 (≠ A137), F132 (= F163), S133 (≠ H164), E184 (= E216), D217 (= D249), I219 (= I251), K246 (= K278)
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)
38% identity, 84% coverage: 54:448/470 of query aligns to 21:385/390 of A0QYS9
- K304 (≠ N345) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
38% identity, 83% coverage: 59:447/470 of query aligns to 34:394/400 of P9WPZ7
- K314 (≠ N345) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine; partial
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
38% identity, 83% coverage: 59:447/470 of query aligns to 28:388/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
38% identity, 83% coverage: 59:447/470 of query aligns to 28:388/391 of 7nn4A
Sites not aligning to the query:
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
36% identity, 84% coverage: 51:447/470 of query aligns to 18:391/393 of 2ordA
- active site: F134 (= F163), E186 (= E216), D219 (= D249), Q222 (= Q252), K248 (= K278), T276 (= T313), R367 (= R423)
- binding pyridoxal-5'-phosphate: G102 (= G136), T103 (≠ A137), F134 (= F163), H135 (= H164), E186 (= E216), D219 (= D249), V221 (≠ I251), Q222 (= Q252), K248 (= K278)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
36% identity, 84% coverage: 51:447/470 of query aligns to 10:383/385 of Q9X2A5
- GT 94:95 (≠ GA 136:137) binding pyridoxal 5'-phosphate
- T268 (= T313) binding pyridoxal 5'-phosphate
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
35% identity, 81% coverage: 57:436/470 of query aligns to 34:397/414 of Q6LFH8
- C154 (≠ A170) modified: Disulfide link with 163, Reversible; mutation to S: Severe reduction in catalytic activity. Does not affect TRX1-mediated activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-163.
- C163 (≠ Y179) modified: Disulfide link with 154, Reversible; mutation to S: No effect on catalytic activity. Requires higher concentrations of TRX1 for activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-154.
- C316 (≠ A337) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ I371) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ I429) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
5e5iA Structure of the ornithine aminotransferase from toxoplasma gondii in complex with inactivator
35% identity, 87% coverage: 26:434/470 of query aligns to 15:402/421 of 5e5iA
- active site: Y153 (≠ F163), E206 (= E216), D239 (= D249), Q242 (= Q252), K268 (= K278), T298 (= T313), R391 (= R423)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: S297 (= S312), T298 (= T313)
- binding 6-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]-4-oxidanylidene-hexanoic acid: Y31 (≠ L42), V61 (≠ Y78), G118 (= G136), A119 (= A137), W154 (≠ H164), E211 (= E221), D239 (= D249), I241 (= I251), Q242 (= Q252), K268 (= K278)
5e3kB Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with (s)-4-amino-5-fluoropentanoic acid
35% identity, 87% coverage: 26:434/470 of query aligns to 17:404/424 of 5e3kB
- active site: Y155 (≠ F163), E208 (= E216), D241 (= D249), Q244 (= Q252), K270 (= K278), T300 (= T313), R393 (= R423)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: Y33 (≠ L42), V63 (≠ Y78), G120 (= G136), A121 (= A137), Y155 (≠ F163), W156 (≠ H164), E213 (= E221), D241 (= D249), I243 (= I251), Q244 (= Q252), K270 (= K278), S299 (= S312), T300 (= T313)
- binding carbonate ion: P180 (= P188), G181 (≠ E189)
5dj9A Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with gabaculine
35% identity, 87% coverage: 26:434/470 of query aligns to 15:402/421 of 5dj9A
- active site: Y153 (≠ F163), E206 (= E216), D239 (= D249), Q242 (= Q252), K268 (= K278), T298 (= T313), R391 (= R423)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: Y31 (≠ L42), V61 (≠ Y78), G118 (= G136), A119 (= A137), Y153 (≠ F163), W154 (≠ H164), E211 (= E221), D239 (= D249), I241 (= I251), Q242 (= Q252), K268 (= K278), S297 (= S312), T298 (= T313)
Query Sequence
>WP_075860193.1 NCBI__GCF_001950255.1:WP_075860193.1
MLKLSRKKKEVKNMELITLEKALNLTRQDIRDLYREYVNESLATLLGLLEFDKQFVRAKG
TKVWDNEGNEYLDFLGGYGSLNFGHNPEEIWQAVDEVKDLPNLLQASIGQLIGAAAFNLA
AITPGNLKRVFFGNSGAEAVEGALKLARIYTGRPGIVYAHNSFHGKSFGALSVTGRQKYQ
TPFSPLLPECYPVVYGDLDELESILKSKPIAAFIVEPIQGEGGVIVPPKGYLKGALELCH
KYGALLIADEIQTGFGRTGRVFAVEHEGIVPDIMCVAKSLGGGVIPVGAYITSDAIWKKA
YGSTDKATLHTSTFGGNTKAMAAVIKAMELLIKWDLAKKADELGNYFLDQLKSLQNSYPL
IKDIRGKGLLIGIEFNEPKGILNKIPGLTNLAREYTGSFVAGLLMNKYRIITAYTLNNPN
VIRLEPPLIVEKEELNFMVSALKEIFESHNSFLGVASANLKTVFGSLFKK
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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