SitesBLAST
Comparing GFF4047 FitnessBrowser__Marino:GFF4047 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)
4jhxA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoylphosphate and arginine
66% identity, 100% coverage: 1:332/333 of query aligns to 3:335/336 of 4jhxA
- active site: R61 (= R59), T62 (= T60), D89 (≠ H87), R110 (= R108), H137 (= H135), Q140 (= Q138), D235 (= D232), C277 (= C274), R322 (= R319)
- binding arginine: L132 (= L130), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237), P279 (= P276)
- binding phosphoric acid mono(formamide)ester: S59 (= S57), T60 (= T58), R61 (= R59), T62 (= T60), R110 (= R108), H137 (= H135), C277 (= C274), L278 (= L275), R322 (= R319)
4jqoA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with citrulline and inorganic phosphate
66% identity, 100% coverage: 1:332/333 of query aligns to 5:337/338 of 4jqoA
- active site: R63 (= R59), T64 (= T60), D91 (≠ H87), R112 (= R108), H139 (= H135), Q142 (= Q138), D237 (= D232), C279 (= C274), R324 (= R319)
- binding citrulline: H139 (= H135), Q142 (= Q138), N173 (= N168), D237 (= D232), S241 (= S236), M242 (= M237), C279 (= C274), L280 (= L275), R324 (= R319)
4h31A Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate and l-norvaline
66% identity, 100% coverage: 1:332/333 of query aligns to 3:335/335 of 4h31A
- active site: R61 (= R59), T62 (= T60), D89 (≠ H87), R110 (= R108), H137 (= H135), Q140 (= Q138), D235 (= D232), C277 (= C274), R322 (= R319)
- binding phosphoric acid mono(formamide)ester: S59 (= S57), T60 (= T58), R61 (= R59), T62 (= T60), R110 (= R108), H137 (= H135), Q140 (= Q138), C277 (= C274), L278 (= L275), R322 (= R319)
- binding norvaline: L132 (= L130), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237)
4jfrB Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate
66% identity, 100% coverage: 1:332/333 of query aligns to 7:339/340 of 4jfrB
- active site: R65 (= R59), T66 (= T60), D93 (≠ H87), R114 (= R108), H141 (= H135), Q144 (= Q138), D239 (= D232), C281 (= C274), R326 (= R319)
- binding phosphoric acid mono(formamide)ester: S63 (= S57), T64 (= T58), R65 (= R59), T66 (= T60), R114 (= R108), H141 (= H135), Q144 (= Q138), C281 (= C274), R326 (= R319)
Q8DCF5 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Vibrio vulnificus (strain CMCP6)
66% identity, 100% coverage: 1:332/333 of query aligns to 1:333/334 of Q8DCF5
P08308 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
66% identity, 100% coverage: 1:332/333 of query aligns to 1:334/336 of P08308
- M1 (= M1) modified: Initiator methionine, Removed
- E106 (= E106) mutation E->A,G: Loss of homotropic cooperativity; gain of anabolic activity. Conformational change which modifies the catalytic site. This mutant is blocked in the active R (relaxed) state.
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
65% identity, 98% coverage: 7:331/333 of query aligns to 6:332/334 of P04391
- S56 (= S57) mutation to H: Much less active than the wild-type.
- STRT 56:59 (= STRT 57:60) binding
- R58 (= R59) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (≠ H84) binding
- K87 (= K88) mutation to Q: Much less active than the wild-type.
- R107 (= R108) binding
- HPTQ 134:137 (= HPTQ 135:138) binding
- N168 (= N168) binding
- D232 (= D232) binding
- SM 236:237 (= SM 236:237) binding
- C274 (= C274) binding ; mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 274:275) binding
- R320 (= R319) binding ; mutation to A: Much less active than the wild-type.
- A326 (= A325) mutation to G: Activity greater than the wild-type and Km for ornithwinas increases about twofold.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
65% identity, 98% coverage: 7:331/333 of query aligns to 5:331/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), R106 (= R108), L128 (= L130), H133 (= H135), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), C273 (= C274), L274 (= L275), R319 (= R319)
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
65% identity, 98% coverage: 7:331/333 of query aligns to 5:331/333 of 2otcA
- active site: R57 (= R59), T58 (= T60), H85 (= H87), R106 (= R108), H133 (= H135), Q136 (= Q138), D231 (= D232), C273 (= C274), R319 (= R319)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), R106 (= R108), H133 (= H135), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), L274 (= L275), R319 (= R319)
Q8G998 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Lentilactobacillus hilgardii (Lactobacillus hilgardii) (see paper)
52% identity, 98% coverage: 5:332/333 of query aligns to 10:336/343 of Q8G998
Sites not aligning to the query:
- 337:343 mutation Missing: It generates a metastable mutant that behaves as a mixture of monomeric and trimeric species with only the latter exhibiting OTC activity.
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
41% identity, 100% coverage: 1:333/333 of query aligns to 1:312/315 of Q51742
- M1 (= M1) modified: Initiator methionine, Removed
- W22 (≠ A22) mutation to A: Decreased heat stability.
- E26 (≠ K26) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ D30) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ A34) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y230) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ K243) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E299) mutation to G: Becomes active at low temperatures; when associated with C-228 or D-241.
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
40% identity, 98% coverage: 5:331/333 of query aligns to 37:342/354 of P00480
- G39 (≠ N7) to C: in OTCD; late onset; dbSNP:rs72554306
- R40 (= R8) to H: in OTCD; late onset; dbSNP:rs72554308
- L43 (= L11) to F: in dbSNP:rs72554309
- K46 (≠ R14) to R: in dbSNP:rs1800321
- Y55 (≠ F23) to D: in OTCD; late onset; dbSNP:rs72554319
- L63 (= L31) to P: in OTCD; late onset; dbSNP:rs72554324
- K88 (= K55) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (= STRT 57:60) binding
- G100 (≠ A67) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ A68) to L: in dbSNP:rs1133135
- L111 (= L78) to P: in dbSNP:rs1800324
- T125 (≠ K92) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D93) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (= R96) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (≠ Y107) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R108) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H135) binding
- Q171 (= Q138) binding
- I172 (= I139) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ F143) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ TM 145:146) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ V150) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (≠ D156) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G163) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D164) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (≠ G170) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ G176) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (= A178) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (= M182) to K: in OTCD; late onset
- H214 (≠ D183) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P189) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (= P194) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (≠ I213) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (= T231) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (≠ V233) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W234) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G238) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (≠ E239) to R: in dbSNP:rs1800328
- E272 (≠ K241) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (= R247) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H273) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C274) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 274:275) binding
- E309 (≠ M298) natural variant: Missing (in OTCD; late onset)
- R330 (= R319) binding
- T333 (= T322) natural variant: T -> A
- S340 (≠ A329) to P: in OTCD; late onset; dbSNP:rs72558489
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 15 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-23 and G-26.
- 23 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-26.
- 26 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-23.
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
40% identity, 98% coverage: 4:331/333 of query aligns to 3:309/321 of 1othA
- active site: R59 (= R59), T60 (= T60), V87 (≠ H87), R108 (= R108), H135 (= H135), Q138 (= Q138), D230 (= D232), C270 (= C274), R297 (= R319)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S57), T58 (= T58), R59 (= R59), T60 (= T60), R108 (= R108), L130 (= L130), H135 (= H135), N166 (= N168), D230 (= D232), S234 (= S236), M235 (= M237), C270 (= C274), L271 (= L275), R297 (= R319)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
40% identity, 98% coverage: 4:331/333 of query aligns to 3:309/321 of 1c9yA
- active site: R59 (= R59), T60 (= T60), V87 (≠ H87), R108 (= R108), H135 (= H135), Q138 (= Q138), D230 (= D232), C270 (= C274), R297 (= R319)
- binding phosphoric acid mono(formamide)ester: S57 (= S57), T58 (= T58), R59 (= R59), T60 (= T60), R108 (= R108), C270 (= C274), L271 (= L275), R297 (= R319)
- binding norvaline: L130 (= L130), N166 (= N168), D230 (= D232), S234 (= S236), M235 (= M237)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
40% identity, 98% coverage: 4:331/333 of query aligns to 36:342/354 of P00481
- R92 (= R59) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C274) mutation to S: Increases KM for ornithine 5-fold and decreases kcat 20-fold.
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
39% identity, 98% coverage: 5:329/333 of query aligns to 9:307/316 of Q81M99
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
41% identity, 97% coverage: 8:331/333 of query aligns to 3:304/307 of 2i6uA
- active site: R52 (= R59), T53 (= T60), R80 (≠ H87), R101 (= R108), H128 (= H135), Q131 (= Q138), D224 (= D232), C264 (= C274), R292 (= R319)
- binding phosphoric acid mono(formamide)ester: S50 (= S57), T51 (= T58), R52 (= R59), T53 (= T60), R101 (= R108), C264 (= C274), L265 (= L275), R292 (= R319)
- binding norvaline: L123 (= L130), N160 (= N168), D224 (= D232), S228 (= S236), M229 (= M237)
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
41% identity, 97% coverage: 8:331/333 of query aligns to 4:305/308 of 7nouA
- active site: R102 (= R108), H129 (= H135), Q132 (= Q138), D225 (= D232), C265 (= C274), R293 (= R319)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I52), T52 (= T58), R53 (= R59), R53 (= R59), F56 (≠ V62), F56 (≠ V62), L79 (≠ I85), D82 (≠ K88), E83 (= E89), V91 (= V97), Y95 (≠ V101), L266 (= L275), R293 (= R319)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
41% identity, 97% coverage: 8:331/333 of query aligns to 4:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
41% identity, 97% coverage: 8:331/333 of query aligns to 4:305/308 of 7norA
Query Sequence
>GFF4047 FitnessBrowser__Marino:GFF4047
MAFNLKNRHFLTLRDFSPREIAFLLKLSADLKTAKYAGTEVPKLEGKDIALIFEKNSTRT
RVGFEVAAFDQGARVTYLGPTGTHIGHKESVKDTARVLGRVYDAIEYRGFGQSVVDELAQ
YAGVPVYNGLTNEFHPTQILADFLTMQEHVEKPLRDVAYVFIGDAANNMGDSLLIGGAKM
GMDVRLCAPKACWPGQAVQEEAQALAAETGARITITEDVDAAVAGVDFVYTDVWVSMGEP
KEKWAERIKLLMPYQVNAALMAKTGNPRARFMHCLPAFHNTETVVGKEIQETYGIDAMEV
TEEVFESPASIVFDQAENRMHTIKAVLVATLGG
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