SitesBLAST
Comparing WP_162470667.1 NCBI__GCF_000013085.1:WP_162470667.1 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)
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
53% identity, 98% coverage: 5:304/305 of query aligns to 8:312/315 of Q51742
- W22 (≠ R19) mutation to A: Decreased heat stability.
- E26 (≠ D23) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ A27) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ E31) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (≠ V221) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (= A233) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E270) mutation to G: Becomes active at low temperatures; when associated with C-228 or D-241.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
45% identity, 97% coverage: 5:299/305 of query aligns to 12:306/316 of Q81M99
- STRT 57:60 (= STRT 54:57) binding carbamoyl phosphate
- Q84 (= Q81) binding carbamoyl phosphate
- R108 (= R105) binding carbamoyl phosphate
- HPCQ 135:138 (= HPCQ 132:135) binding carbamoyl phosphate
- N166 (= N163) binding L-ornithine
- D230 (= D223) binding L-ornithine
- SM 234:235 (= SM 227:228) binding L-ornithine
- CL 269:270 (= CL 262:263) binding carbamoyl phosphate
- R297 (= R290) binding carbamoyl phosphate
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
45% identity, 97% coverage: 5:299/305 of query aligns to 8:302/307 of 4nf2A
- active site: R55 (= R56), T56 (= T57), R83 (= R84), R104 (= R105), H131 (= H132), Q134 (= Q135), D226 (= D223), C265 (= C262), R293 (= R290)
- binding phosphoric acid mono(formamide)ester: S53 (= S54), T54 (= T55), R55 (= R56), T56 (= T57), R104 (= R105), H131 (= H132), Q134 (= Q135), C265 (= C262), L266 (= L263), R293 (= R290)
- binding norvaline: L126 (= L127), N162 (= N163), D226 (= D223), S230 (= S227), M231 (= M228)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
46% identity, 96% coverage: 5:298/305 of query aligns to 2:298/304 of 8qeuA
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
45% identity, 96% coverage: 5:298/305 of query aligns to 2:291/297 of 8qevA
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7nouA
- active site: R102 (= R105), H129 (= H132), Q132 (= Q135), D225 (= D223), C265 (= C262), R293 (= R290)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I49), T52 (= T55), R53 (= R56), R53 (= R56), F56 (≠ V59), F56 (≠ V59), L79 (= L82), D82 (≠ G85), E83 (= E86), V91 (= V94), Y95 (= Y98), L266 (= L263), R293 (= R290)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7nnyA
- active site: R102 (= R105), H129 (= H132), Q132 (= Q135), D225 (= D223), C265 (= C262), R293 (= R290)
- binding 1-naphthol: T52 (= T55), R53 (= R56), F56 (≠ V59), E83 (= E86), V91 (= V94), Y95 (= Y98)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7nnwA
- active site: R102 (= R105), H129 (= H132), Q132 (= Q135), D225 (= D223), C265 (= C262), R293 (= R290)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (= I49), T52 (= T55), R53 (= R56), F56 (≠ V59), L79 (= L82), L92 (= L95), Y95 (= Y98)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:308/308 of 7nnvA
- active site: R102 (= R105), H129 (= H132), Q132 (= Q135), D225 (= D223), C265 (= C262), R293 (= R290)
- binding phosphoric acid mono(formamide)ester: S51 (= S54), T52 (= T55), R53 (= R56), T54 (= T57), R102 (= R105), H129 (= H132), C265 (= C262), L266 (= L263), R293 (= R290)
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
46% identity, 99% coverage: 5:305/305 of query aligns to 3:307/307 of P9WIT9
- STRT 50:53 (= STRT 54:57) binding carbamoyl phosphate
- Q77 (= Q81) binding carbamoyl phosphate
- R101 (= R105) binding carbamoyl phosphate
- HPCQ 128:131 (= HPCQ 132:135) binding carbamoyl phosphate
- N160 (= N163) binding L-ornithine
- D224 (= D223) binding L-ornithine
- SM 228:229 (= SM 227:228) binding L-ornithine
- CL 264:265 (= CL 262:263) binding carbamoyl phosphate
- R292 (= R290) binding carbamoyl phosphate
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
46% identity, 99% coverage: 5:305/305 of query aligns to 3:307/307 of 2i6uA
- active site: R52 (= R56), T53 (= T57), R80 (= R84), R101 (= R105), H128 (= H132), Q131 (= Q135), D224 (= D223), C264 (= C262), R292 (= R290)
- binding phosphoric acid mono(formamide)ester: S50 (= S54), T51 (= T55), R52 (= R56), T53 (= T57), R101 (= R105), C264 (= C262), L265 (= L263), R292 (= R290)
- binding norvaline: L123 (= L127), N160 (= N163), D224 (= D223), S228 (= S227), M229 (= M228)
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
45% identity, 99% coverage: 5:305/305 of query aligns to 3:297/297 of 7nnzB
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
46% identity, 99% coverage: 5:305/305 of query aligns to 4:305/305 of 7np0A
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
45% identity, 99% coverage: 5:305/305 of query aligns to 4:302/302 of 7novA
- active site: R96 (= R105), H123 (= H132), Q126 (= Q135), D219 (= D223), C259 (= C262), R287 (= R290)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R56), F56 (≠ V59), E77 (= E86), V85 (= V94), Y89 (= Y98), L260 (= L263), A284 (= A287), R287 (= R290)
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
40% identity, 96% coverage: 5:298/305 of query aligns to 7:328/334 of P04391
- S56 (= S54) mutation to H: Much less active than the wild-type.
- STRT 56:59 (= STRT 54:57) binding carbamoyl phosphate
- R58 (= R56) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (= Q81) binding carbamoyl phosphate
- K87 (≠ G85) mutation to Q: Much less active than the wild-type.
- R107 (= R105) binding carbamoyl phosphate
- HPTQ 134:137 (≠ HPCQ 132:135) binding carbamoyl phosphate
- N168 (= N163) binding L-ornithine
- D232 (= D223) binding L-ornithine
- SM 236:237 (= SM 227:228) binding L-ornithine
- C274 (= C262) binding Zn(2+); mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 262:263) binding carbamoyl phosphate
- R320 (= R290) binding carbamoyl phosphate; mutation to A: Much less active than the wild-type.
- A326 (≠ G296) 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)
40% identity, 96% coverage: 5:298/305 of query aligns to 6:327/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S54), T56 (= T55), R57 (= R56), T58 (= T57), R106 (= R105), L128 (= L127), H133 (= H132), N167 (= N163), D231 (= D223), S235 (= S227), M236 (= M228), C273 (= C262), L274 (= L263), R319 (= R290)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
40% identity, 94% coverage: 5:290/305 of query aligns to 40:330/354 of P00481
- R92 (= R56) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C262) 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
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
39% identity, 96% coverage: 5:298/305 of query aligns to 6:327/333 of 2otcA
- active site: R57 (= R56), T58 (= T57), H85 (≠ R84), R106 (= R105), H133 (= H132), Q136 (= Q135), D231 (= D223), C273 (= C262), R319 (= R290)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S54), T56 (= T55), R57 (= R56), T58 (= T57), R106 (= R105), H133 (= H132), N167 (= N163), D231 (= D223), S235 (= S227), M236 (= M228), L274 (= L263), R319 (= R290)
Query Sequence
>WP_162470667.1 NCBI__GCF_000013085.1:WP_162470667.1
MKTPRHFLELSDFDAPALRAMLDRGLAFKAERRAGVVSAPLAGKTLALIFEKPSTRTRVS
FEVGMRQLGGSSITLSPTETQLGRGETIADTARVLSRYVDGIMLRTNDPAKLRDLSQNAS
VPVINGLTDAAHPCQIMADLMTFEEHRGSITGKVVTWVGDGNNVACSWIKASALFGFTMR
LACPAELEPPQGVLDWARANGGAVEVLRDPQEAVAGADCVVTDTWVSMGCDGAAARHALL
RPYQVTAPLMAAAAADALFMHCLPAHRGEEVTEDVIDGPQSVVWDEAENRLHAQKGILAW
CMAGS
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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