SitesBLAST
Comparing WP_012101948.1 NCBI__GCF_000016505.1:WP_012101948.1 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)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
45% identity, 97% coverage: 10:388/390 of query aligns to 10:391/393 of 2ordA
- active site: F134 (= F135), E186 (= E186), D219 (= D219), Q222 (= Q222), K248 (= K248), T276 (= T277), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G102), T103 (≠ A103), F134 (= F135), H135 (= H136), E186 (= E186), D219 (= D219), V221 (≠ I221), Q222 (= Q222), K248 (= K248)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
45% identity, 97% coverage: 10:388/390 of query aligns to 2:383/385 of Q9X2A5
- GT 94:95 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- T268 (= T277) binding pyridoxal 5'-phosphate
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 96% coverage: 11:385/390 of query aligns to 69:451/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
47% identity, 97% coverage: 10:387/390 of query aligns to 3:376/376 of O66442
- GT 96:97 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K242 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T277) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
47% identity, 97% coverage: 10:387/390 of query aligns to 2:375/375 of 2eh6A
- active site: F127 (= F135), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T270 (= T277), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G102), T96 (≠ A103), F127 (= F135), H128 (= H136), E179 (= E186), D212 (= D219), V214 (≠ I221), K241 (= K248)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
43% identity, 97% coverage: 10:387/390 of query aligns to 34:425/429 of P73133
- Y39 (= Y15) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S101) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G102) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A103) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R138) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (= E191) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D219) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q222) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K248) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T277) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R364) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 98% coverage: 9:389/390 of query aligns to 10:397/401 of 4adbB
- active site: F136 (= F135), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S101), G103 (= G102), A104 (= A103), F136 (= F135), H137 (= H136), D221 (= D219), V223 (≠ I221), Q224 (= Q222), K250 (= K248)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 98% coverage: 9:389/390 of query aligns to 10:397/400 of 4addA
- active site: F136 (= F135), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G102), A104 (= A103), F136 (= F135), H137 (= H136), D221 (= D219), V223 (≠ I221), K250 (= K248)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y15), F136 (= F135), R139 (= R138)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
40% identity, 95% coverage: 8:377/390 of query aligns to 1:375/388 of 3nx3A
- active site: F127 (= F135), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T271 (= T277), R362 (= R364)
- binding magnesium ion: N191 (≠ S198), F194 (= F201), I313 (vs. gap), F316 (≠ K321), D317 (≠ N322), C319 (≠ L324), Q370 (≠ S372), K371 (= K373)
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 97% coverage: 9:387/390 of query aligns to 15:400/405 of P40732
- GT 108:109 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K255 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T277) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
34% identity, 97% coverage: 9:387/390 of query aligns to 10:395/402 of 4jevB
- active site: F136 (= F135), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I45), S102 (= S101), G103 (= G102), T104 (≠ A103), F136 (= F135), H137 (= H136), E188 (= E186), E193 (= E191), D221 (= D219), V223 (≠ I221), Q224 (= Q222), K250 (= K248), R372 (= R364)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
37% identity, 98% coverage: 4:387/390 of query aligns to 3:389/390 of 8ht4B
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 93% coverage: 15:377/390 of query aligns to 24:384/395 of Q5SHH5
- GT 113:114 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K254 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T277) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 93% coverage: 15:377/390 of query aligns to 16:376/387 of 1wkhA
- active site: F132 (= F135), E184 (= E186), D217 (= D219), Q220 (= Q222), K246 (= K248), T275 (= T277), R363 (= R364)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I45), S104 (= S101), G105 (= G102), T106 (≠ A103), F132 (= F135), S133 (≠ H136), E184 (= E186), E189 (= E191), D217 (= D219), I219 (= I221), K246 (= K248), R363 (= R364)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 93% coverage: 15:377/390 of query aligns to 16:376/387 of 1wkgA
- active site: F132 (= F135), E184 (= E186), D217 (= D219), Q220 (= Q222), K246 (= K248), T275 (= T277), R363 (= R364)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y15), Y46 (≠ I45), G105 (= G102), T106 (≠ A103), F132 (= F135), S133 (≠ H136), R135 (= R138), E184 (= E186), D217 (= D219), I219 (= I221), Q220 (= Q222), K246 (= K248), G273 (= G275), T274 (≠ S276), T275 (= T277)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 93% coverage: 15:377/390 of query aligns to 16:376/387 of 1vefA
- active site: F132 (= F135), D217 (= D219), K246 (= K248), T275 (= T277), R363 (= R364)
- binding pyridoxal-5'-phosphate: G105 (= G102), T106 (≠ A103), F132 (= F135), S133 (≠ H136), E184 (= E186), D217 (= D219), I219 (= I221), K246 (= K248)
Sites not aligning to the query:
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
34% identity, 97% coverage: 9:387/390 of query aligns to 10:390/397 of 4jewA
- active site: F136 (= F135), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T274 (= T277), R367 (= R364)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G102), T104 (≠ A103), F136 (= F135), H137 (= H136), R139 (= R138), E188 (= E186), E193 (= E191), D221 (= D219), V223 (≠ I221), K250 (= K248)
- binding picric acid: K25 (≠ H24), K27 (≠ E26), W32 (≠ F31)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
34% identity, 97% coverage: 9:387/390 of query aligns to 4:384/389 of 2pb0A
- active site: F130 (= F135), E182 (= E186), D215 (= D219), Q218 (= Q222), K244 (= K248), T268 (= T277), R361 (= R364)
- binding pyridoxal-5'-phosphate: S96 (= S101), G97 (= G102), T98 (≠ A103), F130 (= F135), H131 (= H136), E182 (= E186), D215 (= D219), V217 (≠ I221), Q218 (= Q222), K244 (= K248)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
36% identity, 99% coverage: 1:388/390 of query aligns to 1:384/390 of A0QYS9
- K304 (= K309) 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)
35% identity, 98% coverage: 8:389/390 of query aligns to 16:395/400 of P9WPZ7
- K314 (= K309) 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
Query Sequence
>WP_012101948.1 NCBI__GCF_000016505.1:WP_012101948.1
MDYLNYAKEYLMNTYNHLPVVFTHGEGCKLFDTDNKEYLDFTSGIGVMSLGYGNKNWIKA
VEAQLEKVVHTSNIFLNIPVLELAKKFTEISNMTKVFFCNSGAEANEGAIKLARKYSFDK
HGKARNTILTLKKSFHGRTITTLKAGGQEKLHKYFYPFTEGFKYAEANVEELEKSIDSSI
CAIMIEPIQGEGGINPLSEEFVHKVFGIAEKEDILVICDEIQCGIGRTGKIYGFNNYGVC
PDIISTAKGLGGGLPIGAVLCNEKLNNTFEYGDHGSTFGGNPVCAAGALEVLNIISENSF
LEEVSEKGKFVKEYFKSKNKKNILEVRGMGLMIGIEIEGEASRVQKKALQKGLLVLTAGP
NVVRLLPPLIISKEELEAGLNTLYEIIEEE
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