SitesBLAST
Comparing WP_012967145.1 NCBI__GCF_000025465.1:WP_012967145.1 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)
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)
87% identity, 100% coverage: 1:404/406 of query aligns to 1:404/405 of P40732
- GT 108:109 (= GT 108:109) binding pyridoxal 5'-phosphate
- K255 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T284) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
86% identity, 98% coverage: 7:404/406 of query aligns to 2:399/402 of 4jevB
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R377)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I51), S102 (= S107), G103 (= G108), T104 (= T109), F136 (= F141), H137 (= H142), E188 (= E193), E193 (= E198), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255), R372 (= R377)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
85% identity, 98% coverage: 7:404/406 of query aligns to 2:394/397 of 4jewA
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T274 (= T284), R367 (= R377)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G108), T104 (= T109), F136 (= F141), H137 (= H142), R139 (= R144), E188 (= E193), E193 (= E198), D221 (= D226), V223 (= V228), K250 (= K255)
- binding picric acid: K25 (= K30), K27 (= K32), W32 (= W37)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
85% identity, 97% coverage: 12:404/406 of query aligns to 1:388/389 of 2pb0A
- active site: F130 (= F141), E182 (= E193), D215 (= D226), Q218 (= Q229), K244 (= K255), T268 (= T284), R361 (= R377)
- binding pyridoxal-5'-phosphate: S96 (= S107), G97 (= G108), T98 (= T109), F130 (= F141), H131 (= H142), E182 (= E193), D215 (= D226), V217 (= V228), Q218 (= Q229), K244 (= K255)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
60% identity, 99% coverage: 5:405/406 of query aligns to 1:400/401 of 4adbB
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R377)
- binding pyridoxal-5'-phosphate: S102 (= S107), G103 (= G108), A104 (≠ T109), F136 (= F141), H137 (= H142), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
60% identity, 99% coverage: 5:405/406 of query aligns to 1:400/400 of 4addA
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R377)
- binding pyridoxal-5'-phosphate: G103 (= G108), A104 (≠ T109), F136 (= F141), H137 (= H142), D221 (= D226), V223 (= V228), K250 (= K255)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y21), F136 (= F141), R139 (= R144)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
43% identity, 95% coverage: 23:406/406 of query aligns to 19:392/393 of 2ordA
- active site: F134 (= F141), E186 (= E193), D219 (= D226), Q222 (= Q229), K248 (= K255), T276 (= T284), R367 (= R377)
- binding pyridoxal-5'-phosphate: G102 (= G108), T103 (= T109), F134 (= F141), H135 (= H142), E186 (= E193), D219 (= D226), V221 (= V228), Q222 (= Q229), K248 (= K255)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 95% coverage: 23:406/406 of query aligns to 11:384/385 of Q9X2A5
- GT 94:95 (= GT 108:109) binding pyridoxal 5'-phosphate
- T268 (= T284) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 97% coverage: 11:404/406 of query aligns to 29:429/429 of P73133
- Y39 (= Y21) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S107) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G108) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T109) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R144) 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 (= E198) 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 (= D226) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q229) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K255) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T284) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R377) 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.
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)
42% identity, 95% coverage: 15:398/406 of query aligns to 67:451/457 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)
40% identity, 92% coverage: 23:394/406 of query aligns to 12:370/376 of O66442
- GT 96:97 (= GT 108:109) binding pyridoxal 5'-phosphate
- K242 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T284) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
40% identity, 92% coverage: 23:394/406 of query aligns to 11:369/375 of 2eh6A
- active site: F127 (= F141), E179 (= E193), D212 (= D226), Q215 (= Q229), K241 (= K255), T270 (= T284), R352 (= R377)
- binding pyridoxal-5'-phosphate: G95 (= G108), T96 (= T109), F127 (= F141), H128 (= H142), E179 (= E193), D212 (= D226), V214 (= V228), K241 (= K255)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
38% identity, 95% coverage: 17:400/406 of query aligns to 4:385/388 of 3nx3A
- active site: F127 (= F141), E179 (= E193), D212 (= D226), Q215 (= Q229), K241 (= K255), T271 (= T284), R362 (= R377)
- binding magnesium ion: N191 (≠ T205), F194 (= F208), I313 (≠ D326), F316 (= F329), D317 (= D330), C319 (≠ F332), Q370 (≠ D385), K371 (≠ E386)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
39% identity, 95% coverage: 20:404/406 of query aligns to 23:394/395 of Q5SHH5
- GT 113:114 (= GT 108:109) binding pyridoxal 5'-phosphate
- K254 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T284) binding pyridoxal 5'-phosphate
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 96% coverage: 2:389/406 of query aligns to 4:382/400 of P9WPZ7
- K314 (= K320) 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
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 95% coverage: 20:404/406 of query aligns to 15:386/387 of 1wkhA
- active site: F132 (= F141), E184 (= E193), D217 (= D226), Q220 (= Q229), K246 (= K255), T275 (= T284), R363 (= R377)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I51), S104 (= S107), G105 (= G108), T106 (= T109), F132 (= F141), S133 (≠ H142), E184 (= E193), E189 (= E198), D217 (= D226), I219 (≠ V228), K246 (= K255), R363 (= R377)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 95% coverage: 20:404/406 of query aligns to 15:386/387 of 1wkgA
- active site: F132 (= F141), E184 (= E193), D217 (= D226), Q220 (= Q229), K246 (= K255), T275 (= T284), R363 (= R377)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y21), Y46 (≠ I51), G105 (= G108), T106 (= T109), F132 (= F141), S133 (≠ H142), R135 (= R144), E184 (= E193), D217 (= D226), I219 (≠ V228), Q220 (= Q229), K246 (= K255), G273 (= G282), T274 (≠ S283), T275 (= T284)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 95% coverage: 20:404/406 of query aligns to 15:386/387 of 1vefA
- active site: F132 (= F141), D217 (= D226), K246 (= K255), T275 (= T284), R363 (= R377)
- binding pyridoxal-5'-phosphate: G105 (= G108), T106 (= T109), F132 (= F141), S133 (≠ H142), E184 (= E193), D217 (= D226), I219 (≠ V228), K246 (= K255)
Sites not aligning to the query:
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
41% identity, 94% coverage: 7:389/406 of query aligns to 3:376/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
41% identity, 94% coverage: 7:389/406 of query aligns to 3:376/391 of 7nn4A
Query Sequence
>WP_012967145.1 NCBI__GCF_000025465.1:WP_012967145.1
MATEQPAITRATFDEVILPIYAPAEFIPVKGKGSRVWDQQGKEYVDFAGGIAVTALGHCH
PALVAALHEQGETLWHTSNVFTNEPALRLGCKLVEATFAERVVFMNSGTEANETAFKLAR
HYAVTRHSPYKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIVHIPFNDLQAVK
AVMDDHTCAVVVEPIQGEGGVTAATPAFLQGLRELCDQHQALLVFDEVQCGMGRTGSLFA
YMHYGVTPDILTSAKALGGGFPVSAMLTTHEIASAFHAGSHGSTYGGNPLACAVANAAFD
LINTPAVLDGVSAKRELFVKHLQQLDAEFDLFSDIRGMGLLIGAELKPQHKGRARDFLYA
AAQAGVMVLNAGPDVMRFVPSLIIDEQDIAEGMARFAQAVAKVING
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