SitesBLAST
Comparing WP_011024052.1 NCBI__GCF_000007345.1:WP_011024052.1 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)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
39% identity, 76% coverage: 53:253/264 of query aligns to 14:214/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D143), I105 (≠ V144), H106 (= H145), I108 (= I147), G109 (= G148), V113 (= V152), S150 (≠ M189), S151 (= S190), L153 (= L192), M154 (= M193), T155 (= T194), M180 (= M219), G182 (= G221), G183 (= G222), G200 (≠ P239), S202 (≠ D241), A203 (= A242)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
38% identity, 75% coverage: 49:245/264 of query aligns to 43:234/258 of 2i2xB
- active site: D134 (= D143), H136 (= H145), T187 (= T196)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G142), D134 (= D143), V135 (= V144), H136 (= H145), D137 (= D146), I138 (= I147), G139 (= G148), V143 (= V152), T179 (≠ S188), T181 (≠ S190), L183 (= L192), M184 (= M193), T185 (= T194), A208 (≠ M219), G210 (= G221), G211 (= G222), G212 (≠ A223), G228 (≠ P239), E229 (≠ H240), E230 (≠ D241), A231 (= A242)
Q46EH4 Methanol--corrinoid protein; Methanol:corrinoid methyltransferase 1 subunit of 27 kDa; MT1 subunit 27 kDa from Methanosarcina barkeri (strain Fusaro / DSM 804) (see paper)
38% identity, 75% coverage: 49:245/264 of query aligns to 43:234/258 of Q46EH4
- H129 (≠ G138) mutation to K: Does not affect cobalamin-binding.
- H136 (= H145) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
37% identity, 63% coverage: 68:234/264 of query aligns to 28:193/212 of 3ezxA
- active site: D100 (= D143), H102 (= H145), S155 (≠ T196)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M87), F54 (≠ Y94), D100 (= D143), I101 (≠ V144), H102 (= H145), D103 (= D146), I104 (= I147), V109 (= V152), V147 (vs. gap), S149 (= S190), L151 (= L192), M152 (= M193), T153 (= T194), M178 (= M219), G180 (= G221), G181 (= G222)
Sites not aligning to the query:
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
34% identity, 64% coverage: 74:243/264 of query aligns to 33:195/206 of 4jgiB
- active site: D95 (= D143), H97 (= H145), A148 (≠ T196)
- binding co-methylcobalamin: L63 (= L104), D95 (= D143), L96 (≠ V144), H97 (= H145), D98 (= D146), I99 (= I147), G100 (= G148), F104 (≠ V152), G140 (≠ S188), S142 (= S190), L145 (≠ M193), G173 (= G221), G174 (= G222), V175 (≠ A223), S191 (≠ P239), T192 (≠ H240), N193 (≠ D241), A194 (= A242)
P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 84% coverage: 2:223/264 of query aligns to 606:835/1227 of P13009
- E694 (≠ I80) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 142:146) binding methylcob(III)alamin
- D757 (= D143) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H145) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S190) binding methylcob(III)alamin
- T808 (= T194) binding methylcob(III)alamin
- S810 (≠ T196) mutation to A: Decreases activity by about 40%.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding Zn(2+)
- 310 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 860 binding methylcob(III)alamin
- 946 binding S-adenosyl-L-methionine
- 1134 binding S-adenosyl-L-methionine
- 1189:1190 binding S-adenosyl-L-methionine
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
33% identity, 82% coverage: 47:262/264 of query aligns to 11:226/246 of 1bmtA
- active site: D107 (= D143), H109 (= H145), S160 (≠ T196)
- binding co-methylcobalamin: E44 (≠ I80), M48 (≠ A84), M51 (= M87), G55 (= G91), L65 (≠ V101), V68 (≠ L104), D107 (= D143), V108 (= V144), H109 (= H145), D110 (= D146), I111 (= I147), I115 (≠ L151), G152 (≠ S188), L153 (≠ M189), S154 (= S190), L156 (= L192), I157 (≠ M193), T158 (= T194), G183 (= G221), G184 (= G222), A185 (= A223), V207 (≠ A243), N209 (≠ A245), A210 (= A246)
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
44% identity, 44% coverage: 135:250/264 of query aligns to 7:122/125 of 1y80A
- active site: D15 (= D143), H17 (= H145), T68 (= T196)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D143), L16 (≠ V144), H17 (= H145), D18 (= D146), I19 (= I147), G20 (= G148), V24 (= V152), G60 (≠ S188), M61 (= M189), S62 (= S190), L64 (= L192), L65 (≠ M193), T66 (= T194), I91 (≠ M219), G93 (= G221), G94 (= G222), A95 (= A223), P112 (≠ H240), D113 (= D241), A114 (= A242)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
34% identity, 67% coverage: 47:223/264 of query aligns to 11:185/577 of 3bulA
- active site: D107 (= D143), H109 (= H145), S160 (≠ T196)
- binding cobalamin: H109 (= H145), V116 (= V152), G152 (≠ S188), L153 (≠ M189), S154 (= S190), L156 (= L192), I157 (≠ M193), T158 (= T194), G183 (= G221), G184 (= G222)
Sites not aligning to the query:
- binding cobalamin: 208, 209, 210, 213, 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
34% identity, 67% coverage: 47:223/264 of query aligns to 11:185/576 of 3ivaA
- active site: D107 (= D143), H109 (= H145), S160 (≠ T196)
- binding cobalamin: H109 (= H145), G112 (= G148), V116 (= V152), G152 (≠ S188), L153 (≠ M189), S154 (= S190), L156 (= L192), I157 (≠ M193), T158 (= T194), G183 (= G221), G184 (= G222)
Sites not aligning to the query:
- binding cobalamin: 208, 209, 303, 443, 486, 488, 489, 495, 520, 521, 524, 527, 528
- binding s-adenosyl-l-homocysteine: 447, 484, 485, 489, 491, 539
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
33% identity, 72% coverage: 46:235/264 of query aligns to 3:185/507 of 8sseA
Sites not aligning to the query:
- binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492
Q99707 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Homo sapiens (Human) (see 6 papers)
35% identity, 55% coverage: 78:223/264 of query aligns to 706:861/1265 of Q99707
Sites not aligning to the query:
- 61 natural variant: R -> K
- 255 C → Y: in dbSNP:rs1140598
- 382:384 binding (6S)-5,6,7,8-tetrahydrofolate
- 449 binding (6S)-5,6,7,8-tetrahydrofolate
- 470 binding (6S)-5,6,7,8-tetrahydrofolate
- 537 binding (6S)-5,6,7,8-tetrahydrofolate
- 579 binding (6S)-5,6,7,8-tetrahydrofolate
- 585 binding (6S)-5,6,7,8-tetrahydrofolate
- 591 binding (6S)-5,6,7,8-tetrahydrofolate
- 919 D → G: in dbSNP:rs1805087
- 963 D→E: Decreases binding to MTRR; when associated with N-1071.
- 1071 K→N: Decreases binding to MTRR; when associated with E-963.
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
31% identity, 60% coverage: 75:233/264 of query aligns to 656:809/841 of 8g3hA
- binding cobalamin: F675 (≠ Y94), V685 (≠ L104), K693 (≠ Y112), G720 (= G142), V722 (= V144), H723 (= H145), D724 (= D146), I725 (= I147), G726 (= G148), V730 (= V152), M767 (= M189), S768 (= S190), L770 (= L192), V772 (≠ T194), I795 (≠ M219), L796 (≠ V220), G797 (= G221), G798 (= G222), A799 (= A223)
Sites not aligning to the query:
8t0qA Open state of lysine 5,6-aminomutase from thermoanaerobacter tengcongensis
33% identity, 39% coverage: 135:236/264 of query aligns to 111:225/257 of 8t0qA
- binding cobalamin: H122 (= H145), V124 (≠ I147), G125 (= G148), I129 (≠ V152), Y135 (≠ A158), L174 (≠ S188), S176 (= S190), C209 (≠ V220), G210 (= G221), G211 (= G222), P212 (≠ A223)
Sites not aligning to the query:
Q59268 2-methyleneglutarate mutase; Alpha-methyleneglutarate mutase; EC 5.4.99.4 from Eubacterium barkeri (Clostridium barkeri) (see paper)
35% identity, 37% coverage: 126:222/264 of query aligns to 466:562/614 of Q59268
- D483 (= D143) mutation to N: Activity reduced 2000-fold.
- H485 (= H145) mutation to Q: Loss of activity.
Sites not aligning to the query:
- 464 H→Q: No effect on activity.
1xrsB Crystal structure of lysine 5,6-aminomutase in complex with plp, cobalamin, and 5'-deoxyadenosine (see paper)
29% identity, 44% coverage: 121:236/264 of query aligns to 63:187/212 of 1xrsB
- active site: K95 (≠ N159)
- binding cobalamin: D82 (= D143), A83 (≠ V144), H84 (= H145), T85 (≠ D146), V86 (≠ I147), I91 (≠ L155), Y97 (≠ F161), L136 (≠ S188), V137 (≠ M189), S138 (= S190), T142 (= T194), L170 (≠ M219), C171 (≠ V220), G172 (= G221), G173 (= G222), P174 (≠ A223)
Sites not aligning to the query:
E3PRJ4 Lysine 5,6-aminomutase beta subunit; 5,6-LAM; D-lysine 5,6-aminomutase beta subunit; L-beta-lysine 5,6-aminomutase beta subunit; EC 5.4.3.3 from Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) (see paper)
29% identity, 44% coverage: 121:236/264 of query aligns to 112:236/262 of E3PRJ4
- 130:136 (vs. 143:148, 43% identical) binding adenosylcob(III)alamin
- K144 (≠ N159) modified: N6-(pyridoxal phosphate)lysine
- 185:192 (vs. 188:194, 25% identical) binding adenosylcob(III)alamin
- LCGGP 219:223 (≠ MVGGA 219:223) binding adenosylcob(III)alamin
Sites not aligning to the query:
- 239:244 binding adenosylcob(III)alamin
3koyA Crystal structure of ornithine 4,5 aminomutase in complex with ornithine (aerobic) (see paper)
28% identity, 45% coverage: 117:236/264 of query aligns to 575:704/728 of 3koyA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ V144), H606 (= H145), S607 (≠ D146), V608 (≠ I147), V613 (= V152), S655 (= S190), I658 (≠ M193), S659 (≠ T194), G689 (= G221), G690 (= G222), T691 (≠ A223)
Sites not aligning to the query:
- active site: 183, 218, 290
- binding cobalamin: 112, 483, 707, 710, 711
- binding (E)-N~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-ornithine: 77, 105, 109, 110, 156, 158, 178, 183, 188, 218, 219, 290, 292
3koxA Crystal structure of ornithine 4,5 aminomutase in complex with 2,4- diaminobutyrate (anaerobic) (see paper)
28% identity, 45% coverage: 117:236/264 of query aligns to 575:704/728 of 3koxA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ V144), H606 (= H145), S607 (≠ D146), V608 (≠ I147), G609 (= G148), A654 (≠ M189), S655 (= S190), I657 (≠ L192), S659 (≠ T194), G689 (= G221), G690 (= G222), T691 (≠ A223)
Sites not aligning to the query:
- active site: 183, 218, 290
- binding cobalamin: 112, 483, 707, 708, 710, 711
- binding (2S)-2-amino-4-{[(1Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}butanoic acid: 77, 105, 108, 110, 156, 158, 183, 188, 218, 219, 290
3kowB Crystal structure of ornithine 4,5 aminomutase backsoaked complex (see paper)
28% identity, 45% coverage: 117:236/264 of query aligns to 575:704/728 of 3kowB
Sites not aligning to the query:
- active site: 183, 218, 290
- binding cobalamin: 707, 711
- binding pyridoxal-5'-phosphate: 105, 110, 156, 158, 178, 183, 188, 218, 219
Query Sequence
>WP_011024052.1 NCBI__GCF_000007345.1:WP_011024052.1
MDDLPEEVQELIEELDEAAEDEDEDAIKDLTQKLLATGVDVEAITLKKLALLVMDGEEEM
TQGWTQVAIQIGTDPFKTLIEGLAAGMSLIGKKYEEGEAFVPQLLIASAAMYGGMDLLAP
YMKQDENSGSKAATVVIGTVEGDVHDIGKSLVKTLLSANGFNCVDLGNDVPASRFIEAAR
ENKATAVSMSTLMTTTMAEMPKVVKMLENEGIRDKLLVMVGGAPITAEYASQIGADVSPH
DAASAASWLKGAVFDFPSESVRWS
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