SitesBLAST
Comparing WP_014450271.1 NCBI__GCF_000284315.1:WP_014450271.1 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)
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
46% identity, 97% coverage: 2:302/309 of query aligns to 4:302/307 of 4nf2A
- active site: R55 (= R55), T56 (= T56), R83 (= R82), R104 (= R103), H131 (= H130), Q134 (= Q133), D226 (= D225), C265 (= C265), R293 (= R293)
- binding phosphoric acid mono(formamide)ester: S53 (= S53), T54 (= T54), R55 (= R55), T56 (= T56), R104 (= R103), H131 (= H130), Q134 (= Q133), C265 (= C265), L266 (= L266), R293 (= R293)
- binding norvaline: L126 (= L125), N162 (= N161), D226 (= D225), S230 (= S229), M231 (= M230)
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
46% identity, 97% coverage: 2:302/309 of query aligns to 8:306/316 of Q81M99
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
42% identity, 97% coverage: 6:306/309 of query aligns to 8:311/315 of Q51742
- W22 (≠ A20) mutation to A: Decreased heat stability.
- E26 (≠ D24) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ R28) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ N32) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y223) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ K236) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E273) 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
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
42% identity, 97% coverage: 6:305/309 of query aligns to 3:304/307 of 2i6uA
- active site: R52 (= R55), T53 (= T56), R80 (= R82), R101 (= R103), H128 (= H130), Q131 (= Q133), D224 (= D225), C264 (= C265), R292 (= R293)
- binding phosphoric acid mono(formamide)ester: S50 (= S53), T51 (= T54), R52 (= R55), T53 (= T56), R101 (= R103), C264 (= C265), L265 (= L266), R292 (= R293)
- binding norvaline: L123 (= L125), N160 (= N161), D224 (= D225), S228 (= S229), M229 (= M230)
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
42% identity, 97% coverage: 6:305/309 of query aligns to 3:304/307 of P9WIT9
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7nouA
- active site: R102 (= R103), H129 (= H130), Q132 (= Q133), D225 (= D225), C265 (= C265), R293 (= R293)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I48), T52 (= T54), R53 (= R55), R53 (= R55), F56 (≠ L58), F56 (≠ L58), L79 (= L80), D82 (≠ G83), E83 (= E84), V91 (= V92), Y95 (= Y96), L266 (= L266), R293 (= R293)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7nnyA
- active site: R102 (= R103), H129 (= H130), Q132 (= Q133), D225 (= D225), C265 (= C265), R293 (= R293)
- binding 1-naphthol: T52 (= T54), R53 (= R55), F56 (≠ L58), E83 (= E84), V91 (= V92), Y95 (= Y96)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7nnwA
- active site: R102 (= R103), H129 (= H130), Q132 (= Q133), D225 (= D225), C265 (= C265), R293 (= R293)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (= I48), T52 (= T54), R53 (= R55), F56 (≠ L58), L79 (= L80), L92 (≠ V93), Y95 (= Y96)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:305/308 of 7nnvA
- active site: R102 (= R103), H129 (= H130), Q132 (= Q133), D225 (= D225), C265 (= C265), R293 (= R293)
- binding phosphoric acid mono(formamide)ester: S51 (= S53), T52 (= T54), R53 (= R55), T54 (= T56), R102 (= R103), H129 (= H130), C265 (= C265), L266 (= L266), R293 (= R293)
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
42% identity, 97% coverage: 6:305/309 of query aligns to 4:302/305 of 7np0A
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
41% identity, 97% coverage: 6:305/309 of query aligns to 4:299/302 of 7novA
- active site: R96 (= R103), H123 (= H130), Q126 (= Q133), D219 (= D225), C259 (= C265), R287 (= R293)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R55), F56 (≠ L58), E77 (= E84), V85 (= V92), Y89 (= Y96), L260 (= L266), A284 (= A290), R287 (= R293)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
39% identity, 97% coverage: 6:306/309 of query aligns to 2:303/304 of 8qeuA
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
40% identity, 97% coverage: 6:305/309 of query aligns to 3:294/297 of 7nnzB
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
39% identity, 97% coverage: 6:305/309 of query aligns to 40:342/354 of P00480
- R40 (= R6) to H: in OTCD; late onset; dbSNP:rs72554308
- L43 (= L9) to F: in dbSNP:rs72554309
- K46 (≠ A12) to R: in dbSNP:rs1800321
- Y55 (= Y21) to D: in OTCD; late onset; dbSNP:rs72554319
- L63 (≠ F25) to P: in OTCD; late onset; dbSNP:rs72554324
- K88 (= K51) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (= STRT 53:56) binding
- G100 (= G63) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ V64) to L: in dbSNP:rs1133135
- L111 (= L74) to P: in dbSNP:rs1800324
- T125 (≠ E87) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D88) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (= R91) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (≠ M102) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R103) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H130) binding
- Q171 (= Q133) binding
- I172 (≠ A134) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ F138) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ YA 140:141) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ F145) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (= G150) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G157) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D158) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (≠ A163) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ A169) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (= A171) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (≠ A175) to K: in OTCD; late onset
- H214 (≠ K176) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P182) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (= P187) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (≠ V206) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (= T224) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (≠ V226) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W227) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G231) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (= Q232) to R: in dbSNP:rs1800328
- E272 (≠ G234) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (= R239) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H264) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C265) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 265:266) binding
- E309 (≠ L272) natural variant: Missing (in OTCD; late onset)
- R330 (= R293) binding
- T333 (≠ L296) natural variant: T -> A
- S340 (≠ F303) 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.
- 39 G → C: in OTCD; late onset; dbSNP:rs72554306
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
39% identity, 97% coverage: 6:305/309 of query aligns to 7:309/321 of 1othA
- active site: R59 (= R55), T60 (= T56), V87 (≠ R82), R108 (= R103), H135 (= H130), Q138 (= Q133), D230 (= D225), C270 (= C265), R297 (= R293)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S53), T58 (= T54), R59 (= R55), T60 (= T56), R108 (= R103), L130 (= L125), H135 (= H130), N166 (= N161), D230 (= D225), S234 (= S229), M235 (= M230), C270 (= C265), L271 (= L266), R297 (= R293)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
39% identity, 97% coverage: 6:305/309 of query aligns to 7:309/321 of 1c9yA
- active site: R59 (= R55), T60 (= T56), V87 (≠ R82), R108 (= R103), H135 (= H130), Q138 (= Q133), D230 (= D225), C270 (= C265), R297 (= R293)
- binding phosphoric acid mono(formamide)ester: S57 (= S53), T58 (= T54), R59 (= R55), T60 (= T56), R108 (= R103), C270 (= C265), L271 (= L266), R297 (= R293)
- binding norvaline: L130 (= L125), N166 (= N161), D230 (= D225), S234 (= S229), M235 (= M230)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
39% identity, 97% coverage: 6:305/309 of query aligns to 40:342/354 of P00481
- R92 (= R55) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C265) 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
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
37% identity, 97% coverage: 6:306/309 of query aligns to 2:296/297 of 8qevA
Query Sequence
>WP_014450271.1 NCBI__GCF_000284315.1:WP_014450271.1
MKKGTRSFLQLADLSEESAAYLLDFSVRIKKNPELFENMLRRQTVGLIFEKASTRTRLSF
EAGVHQMGGDTLFLGTDSQLSRGESVEDTARVVGGYLDLVIMRTFGHDRIERFAEYCPVP
VINGLTDLHHPCQALSDFAYARELFSELRGLPVTYIGDGNNMAHSLMEAAALFGAKMTVS
TPREYRPDTEILRMSDERARKNGGFVRWLEDPLLASEQAMLLYTDVWTSMGQEGEKSIRE
LEFAGYQINEGILQVADPKAVIFHCLPAYRGLEITASAIDGPQSRVFLQAQYRLYLQKAV
MLFCLGKDS
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