SitesBLAST
Comparing BPHYT_RS27685 FitnessBrowser__BFirm:BPHYT_RS27685 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)
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)
65% identity, 100% coverage: 1:332/332 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.
4jqoA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with citrulline and inorganic phosphate
62% identity, 100% coverage: 1:332/332 of query aligns to 5:337/338 of 4jqoA
- active site: R63 (= R59), T64 (= T60), D91 (≠ R87), 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)
4jfrB Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate
62% identity, 100% coverage: 1:332/332 of query aligns to 7:339/340 of 4jfrB
- active site: R65 (= R59), T66 (= T60), D93 (≠ R87), 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)
4h31A Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate and l-norvaline
62% identity, 100% coverage: 1:332/332 of query aligns to 3:335/335 of 4h31A
- active site: R61 (= R59), T62 (= T60), D89 (≠ R87), 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)
4jhxA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoylphosphate and arginine
62% identity, 100% coverage: 1:332/332 of query aligns to 3:335/336 of 4jhxA
- active site: R61 (= R59), T62 (= T60), D89 (≠ R87), 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)
Q8DCF5 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Vibrio vulnificus (strain CMCP6)
62% identity, 100% coverage: 1:332/332 of query aligns to 1:333/334 of Q8DCF5
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
58% identity, 99% coverage: 5:332/332 of query aligns to 4:333/334 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 (= Q84) 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)
58% identity, 99% coverage: 5:332/332 of query aligns to 3:332/333 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)
58% identity, 99% coverage: 5:332/332 of query aligns to 3:332/333 of 2otcA
- active site: R57 (= R59), T58 (= T60), H85 (≠ R87), 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)
49% identity, 99% coverage: 5:332/332 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)
40% identity, 98% coverage: 1:327/332 of query aligns to 1:306/315 of Q51742
- M1 (= M1) modified: Initiator methionine, Removed
- W22 (≠ G22) mutation to A: Decreased heat stability.
- E26 (≠ D26) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ E30) 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 (= A243) 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.
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
39% identity, 98% coverage: 4:329/332 of query aligns to 8:307/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
38% identity, 98% coverage: 4:329/332 of query aligns to 4:303/307 of 4nf2A
- active site: R55 (= R59), T56 (= T60), R83 (= R87), R104 (= R108), H131 (= H135), Q134 (= Q138), D226 (= D232), C265 (= C274), R293 (= R319)
- binding phosphoric acid mono(formamide)ester: S53 (= S57), T54 (= T58), R55 (= R59), T56 (= T60), R104 (= R108), H131 (= H135), Q134 (= Q138), C265 (= C274), L266 (= L275), R293 (= R319)
- binding norvaline: L126 (= L130), N162 (= N168), D226 (= D232), S230 (= S236), M231 (= M237)
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 97% coverage: 8:328/332 of query aligns to 3:301/307 of P9WIT9
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: 8:328/332 of query aligns to 3:301/307 of 2i6uA
- active site: R52 (= R59), T53 (= T60), R80 (= R87), 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: 8:328/332 of query aligns to 4:302/308 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 (≠ C62), F56 (≠ C62), L79 (= L85), D82 (≠ K88), E83 (= E89), V91 (= V97), Y95 (≠ L101), 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: 8:328/332 of query aligns to 4:302/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
41% identity, 97% coverage: 8:328/332 of query aligns to 4:302/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
41% identity, 97% coverage: 8:328/332 of query aligns to 4:302/308 of 7nnyA
- active site: R102 (= R108), H129 (= H135), Q132 (= Q138), D225 (= D232), C265 (= C274), R293 (= R319)
- binding 1-naphthol: T52 (= T58), R53 (= R59), F56 (≠ C62), E83 (= E89), V91 (= V97), Y95 (≠ L101)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
41% identity, 97% coverage: 8:328/332 of query aligns to 4:302/308 of 7nnwA
- active site: R102 (= R108), H129 (= H135), Q132 (= Q138), D225 (= D232), C265 (= C274), R293 (= R319)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (= I52), T52 (= T58), R53 (= R59), F56 (≠ C62), L79 (= L85), L92 (= L98), Y95 (≠ L101)
Query Sequence
>BPHYT_RS27685 FitnessBrowser__BFirm:BPHYT_RS27685
MAFNLHNRSLLNMQDFSPRDIGFLLDLAAELKRAKYAGNEVPRLNGKNVALIFEKTSTRT
RCAFEVAVHDQGGHVTYIDSASSQLGRKESLKDTARVLGRLYDGIEYRGFHQSVVEDLAA
YSHVPVWNGLTDEFHPTQVLADLLTMREFGEKPLHELSFCYLGDARFNMGNSLLIGGVQM
GMDVRIAAPRELWPHDELVQQMRHLAERTGASVTIVEDPVAGVGGADFVYTDVWVSMGEP
MEAWGPRIDLLLPYQVNAALMKATGKSRTRFMHCLPAYHNLETDIGRQLHERFGLSELEV
SDEVFESNASIVFSQAENRMHTIKAVLVATLA
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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