SitesBLAST
Comparing PfGW456L13_1158 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1158 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)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
39% identity, 86% coverage: 33:401/427 of query aligns to 10:380/393 of 2ordA
- active site: F134 (≠ C157), E186 (= E209), D219 (= D242), Q222 (= Q245), K248 (= K271), T276 (= T299), R367 (= R388)
- binding pyridoxal-5'-phosphate: G102 (= G125), T103 (≠ S126), F134 (≠ C157), H135 (= H158), E186 (= E209), D219 (= D242), V221 (= V244), Q222 (= Q245), K248 (= K271)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
39% identity, 86% coverage: 33:401/427 of query aligns to 2:372/385 of Q9X2A5
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
39% identity, 86% coverage: 33:401/427 of query aligns to 3:366/376 of O66442
- GT 96:97 (≠ GS 125:126) binding
- K242 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T299) binding
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
39% identity, 86% coverage: 33:401/427 of query aligns to 2:365/375 of 2eh6A
- active site: F127 (≠ C157), E179 (= E209), D212 (= D242), Q215 (= Q245), K241 (= K271), T270 (= T299), R352 (= R388)
- binding pyridoxal-5'-phosphate: G95 (= G125), T96 (≠ S126), F127 (≠ C157), H128 (= H158), E179 (= E209), D212 (= D242), V214 (= V244), K241 (= K271)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 89% coverage: 32:410/427 of query aligns to 10:394/401 of 4adbB
- active site: F136 (≠ C157), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R388)
- binding pyridoxal-5'-phosphate: S102 (≠ T124), G103 (= G125), A104 (≠ S126), F136 (≠ C157), H137 (= H158), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 89% coverage: 32:410/427 of query aligns to 10:394/400 of 4addA
- active site: F136 (≠ C157), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R388)
- binding pyridoxal-5'-phosphate: G103 (= G125), A104 (≠ S126), F136 (≠ C157), H137 (= H158), D221 (= D242), V223 (= V244), K250 (= K271)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ V38), F136 (≠ C157), R139 (= R160)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
36% identity, 90% coverage: 32:414/427 of query aligns to 10:398/402 of 4jevB
- active site: F136 (≠ C157), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R388)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ G68), S102 (≠ T124), G103 (= G125), T104 (≠ S126), F136 (≠ C157), H137 (= H158), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271), R372 (= R388)
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)
36% identity, 90% coverage: 32:414/427 of query aligns to 15:403/405 of P40732
- GT 108:109 (≠ GS 125:126) binding
- K255 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T299) binding
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
35% identity, 90% coverage: 32:414/427 of query aligns to 10:393/397 of 4jewA
- active site: F136 (≠ C157), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T274 (= T299), R367 (= R388)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G125), T104 (≠ S126), F136 (≠ C157), H137 (= H158), R139 (= R160), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), K250 (= K271)
- binding picric acid: K25 (≠ R47), K27 (≠ Q49), W32 (= W54)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
35% identity, 90% coverage: 32:414/427 of query aligns to 4:387/389 of 2pb0A
- active site: F130 (≠ C157), E182 (= E209), D215 (= D242), Q218 (= Q245), K244 (= K271), T268 (= T299), R361 (= R388)
- binding pyridoxal-5'-phosphate: S96 (≠ T124), G97 (= G125), T98 (≠ S126), F130 (≠ C157), H131 (= H158), E182 (= E209), D215 (= D242), V217 (= V244), Q218 (= Q245), K244 (= K271)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
35% identity, 90% coverage: 29:412/427 of query aligns to 10:390/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
36% identity, 88% coverage: 34:407/427 of query aligns to 11:379/390 of A0QYS9
- K304 (≠ Q331) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
32% identity, 86% coverage: 44:412/427 of query aligns to 31:411/414 of Q6LFH8
- C154 (≠ T164) 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 (≠ L173) 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 (≠ L323) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ W356) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ N394) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
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)
32% identity, 90% coverage: 18:401/427 of query aligns to 53:443/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
35% identity, 84% coverage: 47:404/427 of query aligns to 64:429/439 of P04181
- N89 (≠ S72) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L73) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ S76) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (= Q87) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R137) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (= R160) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (≠ T164) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (= P179) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (= A205) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (≠ A220) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y224) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (≠ E229) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (= T246) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G249) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R250) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K271) modified: N6-(pyridoxal phosphate)lysine
- E318 (= E295) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (≠ A309) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activityx; dbSNP:rs121965047
- G353 (= G330) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G353) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (≠ A372) to R: in HOGA; no effect on protein abundance; dbSNP:rs121965054; to Y: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833597
- L402 (= L377) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (≠ A392) to L: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965044
Sites not aligning to the query:
- 1:35 modified: transit peptide, Mitochondrion; in renal form
- 51 G → D: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs11553554
- 55 Y → H: in HOGA; decreased protein abundance; dbSNP:rs121965037
- 436 I → N: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833598
- 437 L → F: in HOGA; no effect on protein stability; increased ornithine aminotransferase activity; dbSNP:rs1800456
7tedA Human ornithine aminotransferase cocrystallized with its inhibitor, (s,e)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate (see paper)
35% identity, 84% coverage: 47:404/427 of query aligns to 29:394/404 of 7tedA
- binding (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid: Y50 (≠ G68), G107 (= G125), V108 (≠ S126), F142 (≠ C157), W143 (≠ H158), G144 (= G159), E200 (= E214), D228 (= D242), I230 (≠ V244), Q231 (= Q245), K257 (= K271), S286 (≠ G298), T287 (= T299)
Sites not aligning to the query:
7ta1A Human ornithine aminotransferase (hoat) soaked with gamma-aminobutyric acid (see paper)
35% identity, 84% coverage: 47:404/427 of query aligns to 29:394/404 of 7ta1A
Sites not aligning to the query:
7lnmB Ornithine aminotransferase (oat) cocrystallized with its inactivator - (1s,3s)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid (see paper)
35% identity, 84% coverage: 47:404/427 of query aligns to 29:394/404 of 7lnmB
- binding (1~{R},3~{S},4~{R})-3-methyl-4-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclopentane-1-carboxylic acid: Y50 (≠ G68), G107 (= G125), V108 (≠ S126), F142 (≠ C157), W143 (≠ H158), D228 (= D242), I230 (≠ V244), Q231 (= Q245), K257 (= K271)
7lk1A Ornithine aminotransferase (oat) with its potent inhibitor - (s)-3- amino-4,4-difluorocyclopent-1-enecarboxylic acid (ss-1-148) - 1 hour soaking (see paper)
35% identity, 84% coverage: 47:404/427 of query aligns to 29:394/404 of 7lk1A
- binding (1R,4R)-4-fluoro-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid: Y50 (≠ G68), G107 (= G125), V108 (≠ S126), F142 (≠ C157), W143 (≠ H158), E200 (= E214), D228 (= D242), I230 (≠ V244), Q231 (= Q245), K257 (= K271), R378 (= R388)
6v8cA Design, synthesis, and mechanism of fluorine-substituted cyclohexene analogues of gama-aminobutyric acid (gaba) as selective ornithine aminotransferase inactivators
35% identity, 84% coverage: 47:404/427 of query aligns to 29:394/404 of 6v8cA
- active site: F142 (≠ C157), E195 (= E209), D228 (= D242), Q231 (= Q245), K257 (= K271), T287 (= T299), R378 (= R388)
- binding pyridoxal-5'-phosphate: G107 (= G125), V108 (≠ S126), F142 (≠ C157), W143 (≠ H158), D228 (= D242), I230 (≠ V244), K257 (= K271)
- binding 3-aminocyclohexa-1,3-diene-1-carboxylic acid: Y50 (≠ G68), F142 (≠ C157), K257 (= K271)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_1158 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1158
MNLFSLRRSPPSLDDLVMDASLPSQGVNLSSEYLMPSVERPKQVFVRGQGSWLWDSDDRA
YLDFSQGGGANSLGHSPSVLVNAITAQAQSLINPGFGLHNRGMLSLAEHLCASTGSDQAY
LLNTGSEACEAAIKLARKWGQRHRGGASRIIVANNGCHGRSLATISASDSSTLANRFEPQ
LPGFSRVPFNDLPALHAAVDERTVAIMLEPIQSEAGVVPATVHYLKGVERLCRELGILLI
FDEVQTGIGRCGSLLAEQSCGVTADIVVLGKGLGGGVPLAALLARGKACCFDIGELAGTH
HGNALMTAAGLSVLDTVQDKAFLKHVAEAGQHLREGLGRLAHRYGHGELRGQGLLWGLTL
SDDSADAVVKAALYEGLLLNAPQADCLRFTPALNVSNANIDEMLLRLARAFSRVRTAQLQ
CRKGIAV
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