SitesBLAST
Comparing WP_012968351.1 NCBI__GCF_000025465.1:WP_012968351.1 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)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
64% identity, 97% coverage: 5:392/401 of query aligns to 3:391/401 of 4adbB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R373)
- binding pyridoxal-5'-phosphate: S102 (= S104), G103 (= G105), A104 (= A106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
64% identity, 97% coverage: 5:392/401 of query aligns to 3:391/400 of 4addA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R373)
- binding pyridoxal-5'-phosphate: G103 (= G105), A104 (= A106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), K250 (= K252)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ F18), F136 (= F138), R139 (= R141)
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)
56% identity, 99% coverage: 5:400/401 of query aligns to 8:404/405 of P40732
- GT 108:109 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K255 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T281) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
56% identity, 99% coverage: 5:400/401 of query aligns to 3:399/402 of 4jevB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R373)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I48), S102 (= S104), G103 (= G105), T104 (≠ A106), F136 (= F138), H137 (= H139), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252), R372 (= R373)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
55% identity, 99% coverage: 5:400/401 of query aligns to 3:394/397 of 4jewA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T274 (= T281), R367 (= R373)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G105), T104 (≠ A106), F136 (= F138), H137 (= H139), R139 (= R141), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), K250 (= K252)
- binding picric acid: K25 (≠ R27), K27 (≠ A29), W32 (= W34)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
55% identity, 98% coverage: 10:400/401 of query aligns to 2:388/389 of 2pb0A
- active site: F130 (= F138), E182 (= E190), D215 (= D223), Q218 (= Q226), K244 (= K252), T268 (= T281), R361 (= R373)
- binding pyridoxal-5'-phosphate: S96 (= S104), G97 (= G105), T98 (≠ A106), F130 (= F138), H131 (= H139), E182 (= E190), D215 (= D223), V217 (= V225), Q218 (= Q226), K244 (= K252)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
45% identity, 98% coverage: 9:400/401 of query aligns to 30:429/429 of P73133
- Y39 (≠ F18) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S104) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G105) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A106) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R141) 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 (= E195) 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 (= D223) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q226) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K252) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T281) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R373) 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.
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
43% identity, 96% coverage: 13:396/401 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F138), E186 (= E190), D219 (= D223), Q222 (= Q226), K248 (= K252), T276 (= T281), R367 (= R373)
- binding pyridoxal-5'-phosphate: G102 (= G105), T103 (≠ A106), F134 (= F138), H135 (= H139), E186 (= E190), D219 (= D223), V221 (= V225), Q222 (= Q226), K248 (= K252)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 96% coverage: 13:396/401 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- T268 (= T281) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 97% coverage: 12:399/401 of query aligns to 1:371/375 of 2eh6A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T270 (= T281), R352 (= R373)
- binding pyridoxal-5'-phosphate: G95 (= G105), T96 (≠ A106), F127 (= F138), H128 (= H139), E179 (= E190), D212 (= D223), V214 (= V225), K241 (= K252)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 97% coverage: 12:399/401 of query aligns to 2:372/376 of O66442
- GT 96:97 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K242 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T281) 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)
42% identity, 95% coverage: 8:388/401 of query aligns to 63:445/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
40% identity, 98% coverage: 6:397/401 of query aligns to 2:390/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
43% identity, 96% coverage: 7:390/401 of query aligns to 4:376/390 of A0QYS9
- K304 (≠ E309) 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)
43% identity, 97% coverage: 7:396/401 of query aligns to 12:397/400 of P9WPZ7
- K314 (≠ D316) 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
43% identity, 97% coverage: 7:396/401 of query aligns to 6:391/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
43% identity, 97% coverage: 7:396/401 of query aligns to 6:391/391 of 7nn4A
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
41% identity, 93% coverage: 26:396/401 of query aligns to 32:393/395 of Q5SHH5
- GT 113:114 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K254 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T281) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 93% coverage: 26:396/401 of query aligns to 24:385/387 of 1wkhA
- active site: F132 (= F138), E184 (= E190), D217 (= D223), Q220 (= Q226), K246 (= K252), T275 (= T281), R363 (= R373)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I48), S104 (= S104), G105 (= G105), T106 (≠ A106), F132 (= F138), S133 (≠ H139), E184 (= E190), E189 (= E195), D217 (= D223), I219 (≠ V225), K246 (= K252), R363 (= R373)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 93% coverage: 26:396/401 of query aligns to 24:385/387 of 1wkgA
- active site: F132 (= F138), E184 (= E190), D217 (= D223), Q220 (= Q226), K246 (= K252), T275 (= T281), R363 (= R373)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ I48), G105 (= G105), T106 (≠ A106), F132 (= F138), S133 (≠ H139), R135 (= R141), E184 (= E190), D217 (= D223), I219 (≠ V225), Q220 (= Q226), K246 (= K252), G273 (= G279), T274 (= T280), T275 (= T281)
Sites not aligning to the query:
Query Sequence
>WP_012968351.1 NCBI__GCF_000025465.1:WP_012968351.1
MSGTMTREDFDAYLVPCFAPAPFIPVRAAGSRVWDQQGKEYIDMAGGIAVNALGHAHPAL
AQALQDQLAKLWHIGNGYTNEPVLQLAKTLVQSTFADKVFFCNSGAEANEAALKLARKYA
HDKFGGEKSEIIAFNHAFHGRTLFTVSVGGQPKYSSDYAPLPQGITHLPYNDIEAVTAAI
SSRTCAVIVEPIIGEGGVIPADPAFLQALRTLCDRHHATLIFDEVQTGAGRTGHLYAYQH
YNVVPDILTSAKGLGGGFPIGAMLAKEAWAQVFQPGTHGTTFGGNPLAATVANAVLAHLD
APLLAGVGERHALIVDQLNAISARYDAFSAVRGTGLLIGAELAGPLRGKAKTLTNLAAEE
GLIALIAGPDVLRFAPALNIPLADIAEAFVRLDRAVARLTR
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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