SitesBLAST
Comparing PP_0372 FitnessBrowser__Putida:PP_0372 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)
41% identity, 86% coverage: 35:401/426 of query aligns to 3:372/385 of Q9X2A5
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
41% identity, 86% coverage: 35:401/426 of query aligns to 11:380/393 of 2ordA
- active site: F134 (≠ C158), E186 (= E209), D219 (= D242), Q222 (= Q245), K248 (= K271), T276 (≠ S299), R367 (= R388)
- binding pyridoxal-5'-phosphate: G102 (= G126), T103 (≠ A127), F134 (≠ C158), H135 (= H159), E186 (= E209), D219 (= D242), V221 (= V244), Q222 (= Q245), K248 (= K271)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
39% identity, 86% coverage: 35:401/426 of query aligns to 3:365/375 of 2eh6A
- active site: F127 (≠ C158), E179 (= E209), D212 (= D242), Q215 (= Q245), K241 (= K271), T270 (≠ S299), R352 (= R388)
- binding pyridoxal-5'-phosphate: G95 (= G126), T96 (≠ A127), F127 (≠ C158), H128 (= H159), E179 (= E209), D212 (= D242), V214 (= V244), K241 (= K271)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
39% identity, 86% coverage: 35:401/426 of query aligns to 4:366/376 of O66442
- GT 96:97 (≠ GA 126:127) binding
- K242 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T271 (≠ S299) binding
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 91% coverage: 25:410/426 of query aligns to 2:394/401 of 4adbB
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding pyridoxal-5'-phosphate: S102 (= S125), G103 (= G126), A104 (= A127), F136 (≠ C158), H137 (= H159), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 91% coverage: 25:410/426 of query aligns to 2:394/400 of 4addA
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding pyridoxal-5'-phosphate: G103 (= G126), A104 (= A127), F136 (≠ C158), H137 (= H159), D221 (= D242), V223 (= V244), K250 (= K271)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ T39), F136 (≠ C158), R139 (= R161)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
37% identity, 90% coverage: 33:414/426 of query aligns to 10:398/402 of 4jevB
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ G69), S102 (= S125), G103 (= G126), T104 (≠ A127), F136 (≠ C158), H137 (= H159), 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)
37% identity, 90% coverage: 33:414/426 of query aligns to 15:403/405 of P40732
- GT 108:109 (≠ GA 126:127) binding
- K255 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T284 (≠ S299) binding
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 90% coverage: 33:416/426 of query aligns to 10:395/397 of 4jewA
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T274 (≠ S299), R367 (= R388)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G126), T104 (≠ A127), F136 (≠ C158), H137 (= H159), R139 (= R161), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), K250 (= K271)
- binding picric acid: K25 (≠ R48), K27 (≠ Q50), W32 (= W55)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 90% coverage: 33:416/426 of query aligns to 4:389/389 of 2pb0A
- active site: F130 (≠ C158), E182 (= E209), D215 (= D242), Q218 (= Q245), K244 (= K271), T268 (≠ S299), R361 (= R388)
- binding pyridoxal-5'-phosphate: S96 (= S125), G97 (= G126), T98 (≠ A127), F130 (≠ C158), H131 (= H159), E182 (= E209), D215 (= D242), V217 (= V244), Q218 (= Q245), K244 (= K271)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
36% identity, 86% coverage: 46:412/426 of query aligns to 21:390/390 of 8ht4B
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)
37% identity, 86% coverage: 34:401/426 of query aligns to 67:443/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
35% identity, 86% coverage: 45:411/426 of query aligns to 31:410/414 of Q6LFH8
- C154 (≠ A165) 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 (= C174) 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 (≠ T394) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
7lomC Ornithine aminotransferase (oat) soaked with its inactivator - (1s, 3s)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid (see paper)
38% identity, 84% coverage: 48:404/426 of query aligns to 28:392/402 of 7lomC
- binding (4~{R})-4-(fluoranylmethyl)-3-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclohexene-1-carboxylic acid: Y49 (≠ G69), G106 (= G126), V107 (≠ A127), F141 (≠ C158), W142 (≠ H159), E199 (= E214), D227 (= D242), I229 (≠ V244), Q230 (= Q245), K256 (= K271), R376 (= R388)
7lomA Ornithine aminotransferase (oat) soaked with its inactivator - (1s, 3s)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid (see paper)
38% identity, 84% coverage: 48:404/426 of query aligns to 28:392/402 of 7lomA
- binding (3~{S},4~{S})-4-methyl-3-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclohexene-1-carboxylic acid: Y49 (≠ G69), G106 (= G126), V107 (≠ A127), F141 (≠ C158), W142 (≠ H159), E194 (= E209), E199 (= E214), D227 (= D242), I229 (≠ V244), Q230 (= Q245), K256 (= K271), R376 (= R388)
7lonA Ornithine aminotransferase (oat) cocrystallized with its inactivator - (1s,3s)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid (see paper)
38% identity, 84% coverage: 48:404/426 of query aligns to 27:391/401 of 7lonA
- binding (1R,3S,4R)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-methylcyclohexane-1-carboxylic acid: Y48 (≠ G69), G105 (= G126), V106 (≠ A127), F140 (≠ C158), W141 (≠ H159), E193 (= E209), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271)
Sites not aligning to the query:
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
37% identity, 84% coverage: 48:404/426 of query aligns to 64:429/439 of P04181
- N89 (≠ S73) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L74) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ S77) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (= Q88) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R138) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (= R161) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (= A165) 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
7ta0A Human ornithine aminotransferase (hoat) soaked with 5-aminovaleric acid (see paper)
37% identity, 84% coverage: 48:404/426 of query aligns to 28:393/403 of 7ta0A
- binding 5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: Y49 (≠ G69), G106 (= G126), V107 (≠ A127), F141 (≠ C158), W142 (≠ H159), D227 (= D242), I229 (≠ V244), Q230 (= Q245), K256 (= K271), S285 (≠ G298), T286 (≠ S299)
Sites not aligning to the query:
8ez1B Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
37% identity, 84% coverage: 48:404/426 of query aligns to 27:392/402 of 8ez1B
- binding (1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid: Y48 (≠ G69), T104 (≠ S125), G105 (= G126), V106 (≠ A127), F140 (≠ C158), W141 (≠ H159), E198 (= E214), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271), R376 (= R388)
8ez1A Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
37% identity, 84% coverage: 48:404/426 of query aligns to 27:392/402 of 8ez1A
- binding (3E,4E)-4-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-iminocyclopent-1-ene-1-carboxylic acid: Y48 (≠ G69), G105 (= G126), V106 (≠ A127), F140 (≠ C158), W141 (≠ H159), E198 (= E214), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271), R376 (= R388)
Query Sequence
>PP_0372 FitnessBrowser__Putida:PP_0372
MNLFNLRRSAPAAAAEPKRAPVIVPHASEQSPERLMPGTERAAQVFVRGQGSWLWDNEGH
AYLDFTQGGAVNSLGHSPSVLVKALGNQAQALINPGSGFHNRGLLGLVNRLCQSTGSDQA
YLLNSGAEACEGAIKLARKWGQLHRNGAYHIITASQACHGRSLGALSASDPLPCNRCEPG
LPGFSKVPFNDLAALHAEVDSRTVAIMLEPIQGEAGVIPATQEYLKGVETLCRELGILLI
LDEVQTGIGRCGALLAEELYGVRADIITLGKGLGGGVPLAALLARGKACCAEPGELEGSH
HGNALMCAAGLAVLDSVLEPGFLAQVQDNGRHLREGLSRLTGRYGQGEVRGHGLLWALQL
KENLARELVAAALHEGLLLNAPQVDVVRFSPALTVSKGNIDEMLLRLARAFARLHAQQQA
RREMPA
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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