SitesBLAST
Comparing BPHYT_RS15580 FitnessBrowser__BFirm:BPHYT_RS15580 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)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 97% coverage: 11:391/394 of query aligns to 3:382/385 of Q9X2A5
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
43% identity, 97% coverage: 11:391/394 of query aligns to 11:390/393 of 2ordA
- active site: F134 (= F134), E186 (= E186), D219 (= D219), Q222 (= Q222), K248 (= K248), T276 (= T276), R367 (= R368)
- binding pyridoxal-5'-phosphate: G102 (= G102), T103 (≠ A103), F134 (= F134), H135 (= H135), E186 (= E186), D219 (= D219), V221 (= V221), Q222 (= Q222), K248 (= K248)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
41% identity, 97% coverage: 11:391/394 of query aligns to 1:376/376 of O66442
- GT 96:97 (≠ GA 102:103) binding
- K242 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T276) binding
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
41% identity, 97% coverage: 11:391/394 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F134), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T270 (= T276), R352 (= R368)
- binding pyridoxal-5'-phosphate: G95 (= G102), T96 (≠ A103), F127 (= F134), H128 (= H135), E179 (= E186), D212 (= D219), V214 (= V221), K241 (= K248)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 96% coverage: 2:380/394 of query aligns to 7:384/400 of 4addA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T276), R372 (= R368)
- binding pyridoxal-5'-phosphate: G103 (= G102), A104 (= A103), F136 (= F134), H137 (= H135), D221 (= D219), V223 (= V221), K250 (= K248)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ T15), F136 (= F134), R139 (= R137)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 96% coverage: 2:380/394 of query aligns to 7:384/401 of 4adbB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T276), R372 (= R368)
- binding pyridoxal-5'-phosphate: S102 (= S101), G103 (= G102), A104 (= A103), F136 (= F134), H137 (= H135), D221 (= D219), V223 (= V221), Q224 (= Q222), K250 (= K248)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
40% identity, 96% coverage: 17:394/394 of query aligns to 10:388/388 of 3nx3A
- active site: F127 (= F134), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T271 (= T276), R362 (= R368)
- binding magnesium ion: N191 (≠ T198), F194 (= F201), I313 (≠ S318), F316 (≠ R321), D317 (≠ G322), C319 (≠ E324), Q370 (≠ T376), K371 (≠ N377)
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)
38% identity, 96% coverage: 17:394/394 of query aligns to 75:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
38% identity, 95% coverage: 9:384/394 of query aligns to 10:388/402 of 4jevB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T276), R372 (= R368)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ W45), S102 (= S101), G103 (= G102), T104 (≠ A103), F136 (= F134), H137 (= H135), E188 (= E186), E193 (= E191), D221 (= D219), V223 (= V221), Q224 (= Q222), K250 (= K248), R372 (= R368)
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)
38% identity, 95% coverage: 9:384/394 of query aligns to 15:393/405 of P40732
- GT 108:109 (≠ GA 102:103) binding
- K255 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T276) binding
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 95% coverage: 9:384/394 of query aligns to 10:383/397 of 4jewA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T274 (= T276), R367 (= R368)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G102), T104 (≠ A103), F136 (= F134), H137 (= H135), R139 (= R137), E188 (= E186), E193 (= E191), D221 (= D219), V223 (= V221), K250 (= K248)
- binding picric acid: K25 (≠ H24), K27 (= K26), W32 (≠ Y31)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 95% coverage: 9:384/394 of query aligns to 4:377/389 of 2pb0A
- active site: F130 (= F134), E182 (= E186), D215 (= D219), Q218 (= Q222), K244 (= K248), T268 (= T276), R361 (= R368)
- binding pyridoxal-5'-phosphate: S96 (= S101), G97 (= G102), T98 (≠ A103), F130 (= F134), H131 (= H135), E182 (= E186), D215 (= D219), V217 (= V221), 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)
37% identity, 95% coverage: 18:393/394 of query aligns to 18:385/390 of A0QYS9
- K304 (≠ A312) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
35% identity, 92% coverage: 18:380/394 of query aligns to 17:378/390 of 8ht4B
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
33% identity, 93% coverage: 20:387/394 of query aligns to 30:403/414 of Q6LFH8
- C154 (≠ T141) 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 (≠ W150) 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 (≠ L300) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ R333) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ N374) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
34% identity, 96% coverage: 14:391/394 of query aligns to 23:394/395 of Q5SHH5
- GT 113:114 (≠ GA 102:103) binding
- K254 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T276) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 96% coverage: 14:391/394 of query aligns to 15:386/387 of 1wkhA
- active site: F132 (= F134), E184 (= E186), D217 (= D219), Q220 (= Q222), K246 (= K248), T275 (= T276), R363 (= R368)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ W45), S104 (= S101), G105 (= G102), T106 (≠ A103), F132 (= F134), S133 (≠ H135), E184 (= E186), E189 (= E191), D217 (= D219), I219 (≠ V221), K246 (= K248), R363 (= R368)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 96% coverage: 14:391/394 of query aligns to 15:386/387 of 1wkgA
- active site: F132 (= F134), E184 (= E186), D217 (= D219), Q220 (= Q222), K246 (= K248), T275 (= T276), R363 (= R368)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (≠ T15), Y46 (≠ W45), G105 (= G102), T106 (≠ A103), F132 (= F134), S133 (≠ H135), R135 (= R137), E184 (= E186), D217 (= D219), I219 (≠ V221), Q220 (= Q222), K246 (= K248), G273 (= G274), T274 (≠ G275), T275 (= T276)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 96% coverage: 14:391/394 of query aligns to 15:386/387 of 1vefA
- active site: F132 (= F134), D217 (= D219), K246 (= K248), T275 (= T276), R363 (= R368)
- binding pyridoxal-5'-phosphate: G105 (= G102), T106 (≠ A103), F132 (= F134), S133 (≠ H135), E184 (= E186), D217 (= D219), I219 (≠ V221), K246 (= K248)
Sites not aligning to the query:
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 95% coverage: 18:392/394 of query aligns to 26:394/400 of P9WPZ7
- K314 (≠ E308) 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
>BPHYT_RS15580 FitnessBrowser__BFirm:BPHYT_RS15580
MNFNEYPIESLMYITNRPEIVFTHGKGSWLYDNNGKRYLDFIQGWAVNSLGHCNDGMIEA
LNKQSQLLINPSPAFYNQPMAQLAGLLTQHSCFDKVFFANSGAEANEGAIKLARKWGKKF
KDGAFEIITFDHSFHGRTLATMSASGKPGWDTIYAPQVPGFPKADLNDIASVEKLINAKT
VAVMLEPIQGEGGVIPATREFMQQLRELTKKHNLLLIVDEVQSGCGRAGTLFAYELSDIE
PDIMTLGKGIGGGVPLAALLAKAEIAVFEAGDQGGTYNGNPLMTAVGYSVISQLTAPGFL
EGLRARGEYLRAKLLELSEERGFEGERGEGLLRALLLGKDIGNQIVEKARDMQPDGLLLN
AARPNLLRFMPALNVTNEEIDQMMTMLRSILDTL
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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