SitesBLAST
Comparing AO353_07470 FitnessBrowser__pseudo3_N2E3:AO353_07470 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)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
40% identity, 86% coverage: 34:399/425 of query aligns to 11:380/393 of 2ordA
- active site: F134 (≠ C157), E186 (= E207), D219 (= D240), Q222 (= Q243), K248 (= K269), T276 (= T297), R367 (= R386)
- binding pyridoxal-5'-phosphate: G102 (= G125), T103 (≠ S126), F134 (≠ C157), H135 (= H158), E186 (= E207), D219 (= D240), V221 (= V242), Q222 (= Q243), K248 (= K269)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
40% identity, 86% coverage: 34:399/425 of query aligns to 3:372/385 of Q9X2A5
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
38% identity, 86% coverage: 34:399/425 of query aligns to 3:365/375 of 2eh6A
- active site: F127 (≠ C157), E179 (= E207), D212 (= D240), Q215 (= Q243), K241 (= K269), T270 (= T297), R352 (= R386)
- binding pyridoxal-5'-phosphate: G95 (= G125), T96 (≠ S126), F127 (≠ C157), H128 (= H158), E179 (= E207), D212 (= D240), V214 (= V242), K241 (= K269)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
38% identity, 86% coverage: 34:399/425 of query aligns to 4:366/376 of O66442
- GT 96:97 (≠ GS 125:126) binding
- K242 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T297) binding
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 91% coverage: 22:408/425 of query aligns to 1:394/400 of 4addA
- active site: F136 (≠ C157), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T297), R372 (= R386)
- binding pyridoxal-5'-phosphate: G103 (= G125), A104 (≠ S126), F136 (≠ C157), H137 (= H158), D221 (= D240), V223 (= V242), K250 (= K269)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ V38), F136 (≠ C157), R139 (≠ H160)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 91% coverage: 22:408/425 of query aligns to 1:394/401 of 4adbB
- active site: F136 (≠ C157), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T297), R372 (= R386)
- binding pyridoxal-5'-phosphate: S102 (= S124), G103 (= G125), A104 (≠ S126), F136 (≠ C157), H137 (= H158), D221 (= D240), V223 (= V242), Q224 (= Q243), K250 (= K269)
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)
34% identity, 90% coverage: 32:412/425 of query aligns to 15:403/405 of P40732
- GT 108:109 (≠ GS 125:126) binding
- K255 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T297) binding
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
34% identity, 90% coverage: 32:412/425 of query aligns to 10:398/402 of 4jevB
- active site: F136 (≠ C157), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T297), R372 (= R386)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ G68), S102 (= S124), G103 (= G125), T104 (≠ S126), F136 (≠ C157), H137 (= H158), E188 (= E207), E193 (≠ A212), D221 (= D240), V223 (= V242), Q224 (= Q243), K250 (= K269), R372 (= R386)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
37% identity, 88% coverage: 33:405/425 of query aligns to 10:379/390 of A0QYS9
- K304 (≠ Q329) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
34% identity, 90% coverage: 32:412/425 of query aligns to 10:393/397 of 4jewA
- active site: F136 (≠ C157), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T274 (= T297), R367 (= R386)
- 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 (≠ H160), E188 (= E207), E193 (≠ A212), D221 (= D240), V223 (= V242), K250 (= K269)
- 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)
34% identity, 90% coverage: 32:412/425 of query aligns to 4:387/389 of 2pb0A
- active site: F130 (≠ C157), E182 (= E207), D215 (= D240), Q218 (= Q243), K244 (= K269), T268 (= T297), R361 (= R386)
- binding pyridoxal-5'-phosphate: S96 (= S124), G97 (= G125), T98 (≠ S126), F130 (≠ C157), H131 (= H158), E182 (= E207), D215 (= D240), V217 (= V242), Q218 (= Q243), K244 (= K269)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
35% identity, 89% coverage: 32:410/425 of query aligns to 8:390/390 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)
34% identity, 87% coverage: 31:399/425 of query aligns to 66:443/457 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)
32% identity, 86% coverage: 44:409/425 of query aligns to 31:410/414 of Q6LFH8
- C154 (≠ A164) 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 (= C170) 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 (≠ L321) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ W354) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ T392) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
36% identity, 89% coverage: 33:411/425 of query aligns to 12:389/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
36% identity, 89% coverage: 33:411/425 of query aligns to 12:389/391 of 7nn4A
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
36% identity, 89% coverage: 33:411/425 of query aligns to 18:395/400 of P9WPZ7
- K314 (≠ Q329) 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
7ta0A Human ornithine aminotransferase (hoat) soaked with 5-aminovaleric acid (see paper)
35% identity, 84% coverage: 47:402/425 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 (≠ G68), G106 (= G125), V107 (≠ S126), F141 (≠ C157), W142 (≠ H158), D227 (= D240), I229 (≠ V242), Q230 (= Q243), K256 (= K269), S285 (≠ G296), T286 (= T297)
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)
35% identity, 84% coverage: 47:402/425 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 (≠ H160) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (= A164) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (= P177) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (= A203) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (≠ A218) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y222) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (≠ E227) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (= T244) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G247) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R248) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K269) modified: N6-(pyridoxal phosphate)lysine
- E318 (= E293) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (≠ A307) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activityx; dbSNP:rs121965047
- G353 (≠ A328) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G351) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (≠ V367) 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 (= L375) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (≠ A390) 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
8ez1B Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
35% identity, 84% coverage: 47:402/425 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 (≠ G68), T104 (≠ S124), G105 (= G125), V106 (≠ S126), F140 (≠ C157), W141 (≠ H158), E198 (≠ A212), D226 (= D240), I228 (≠ V242), Q229 (= Q243), K255 (= K269), R376 (= R386)
Query Sequence
>AO353_07470 FitnessBrowser__pseudo3_N2E3:AO353_07470
MNLFSLRRQQPSLDDLVVEHFRPSRHDNLSSECLMPSVERPQQVFVRGQGSWLWDSDDRA
YLDFTQGGAANSLGHSPSVLIKAISAQAQTLINPGSGLLNRGQLNLAERLCASTGSDKVY
LLNSGSEACEAAIKLARKWGQLHRGGASRIITASGSCHGHGFAAMSASDCQNNRFEPQLP
GFSHVPFNDLPALHAAVDAQTVAILLEPIQCAAGVVPATGHYLKGVERLCRELGILLILD
EVQTGIGRCGSLLAEQFYGVRADIVVLGKGLGGGVPVAALLARGKACCLEPGELDGTHHG
NALMASAALAVLDSVLDHGFLEQVRDSAQHLREGLGRLANRYGHGELRGQGLLWGLTLSD
DSADAVVNAALYEGLLLSAPKPDCLRFTPALTVSKTNIDEMLLRLARAFSRVRTAQLQCR
KGIAV
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