SitesBLAST
Comparing WP_048036790.1 NCBI__GCF_000007065.1:WP_048036790.1 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)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
54% identity, 85% coverage: 33:212/213 of query aligns to 34:214/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D102), I105 (≠ V103), H106 (= H104), I108 (= I106), G109 (= G107), V113 (= V111), S150 (≠ L148), S151 (= S149), L153 (= L151), M154 (= M152), T155 (= T153), M180 (= M178), G182 (= G180), G183 (= G181), G200 (≠ A198), S202 (≠ N200), A203 (= A201)
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
40% identity, 83% coverage: 29:205/213 of query aligns to 28:198/206 of 4jgiB
- active site: D95 (= D102), H97 (= H104), A148 (≠ T155)
- binding co-methylcobalamin: L63 (≠ V64), D95 (= D102), L96 (≠ V103), H97 (= H104), D98 (= D105), I99 (= I106), G100 (= G107), F104 (≠ V111), G140 (= G147), S142 (= S149), L145 (≠ M152), G173 (= G180), G174 (= G181), V175 (≠ A182), S191 (≠ A198), T192 (≠ E199), N193 (= N200), A194 (= A201)
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
39% identity, 90% coverage: 2:193/213 of query aligns to 1:193/212 of 3ezxA
- active site: D100 (= D102), H102 (= H104), S155 (≠ T155)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M47), F54 (= F54), D100 (= D102), I101 (≠ V103), H102 (= H104), D103 (= D105), I104 (= I106), V109 (= V111), V147 (vs. gap), S149 (= S149), L151 (= L151), M152 (= M152), T153 (= T153), M178 (= M178), G180 (= G180), G181 (= G181)
Sites not aligning to the query:
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
48% identity, 57% coverage: 91:212/213 of query aligns to 4:125/125 of 1y80A
- active site: D15 (= D102), H17 (= H104), T68 (= T155)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D102), L16 (≠ V103), H17 (= H104), D18 (= D105), I19 (= I106), G20 (= G107), V24 (= V111), G60 (= G147), M61 (≠ L148), S62 (= S149), L64 (= L151), L65 (≠ M152), T66 (= T153), I91 (≠ M178), G93 (= G180), G94 (= G181), A95 (= A182), P112 (≠ E199), D113 (≠ N200), A114 (= A201)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
35% identity, 99% coverage: 3:213/213 of query aligns to 36:243/258 of 2i2xB
- active site: D134 (= D102), H136 (= H104), T187 (= T155)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G101), D134 (= D102), V135 (= V103), H136 (= H104), D137 (= D105), I138 (= I106), G139 (= G107), V143 (= V111), T179 (≠ G147), T181 (≠ S149), L183 (= L151), M184 (= M152), T185 (= T153), A208 (≠ M178), G210 (= G180), G211 (= G181), G212 (≠ A182), G228 (≠ A198), E229 (= E199), E230 (≠ N200), A231 (= A201)
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)
35% identity, 99% coverage: 3:213/213 of query aligns to 36:243/258 of Q46EH4
- H129 (≠ G97) mutation to K: Does not affect cobalamin-binding.
- H136 (= H104) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
40% identity, 84% coverage: 35:213/213 of query aligns to 39:222/246 of 1bmtA
- active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
- binding co-methylcobalamin: E44 (= E40), M48 (≠ A44), M51 (= M47), G55 (= G51), L65 (= L61), V68 (= V64), D107 (= D102), V108 (= V103), H109 (= H104), D110 (= D105), I111 (= I106), I115 (= I110), G152 (= G147), L153 (= L148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), A185 (= A182), V207 (≠ A198), N209 (= N200), A210 (= A201)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
40% identity, 84% coverage: 35:213/213 of query aligns to 39:222/577 of 3bulA
- active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
- binding cobalamin: H109 (= H104), V116 (= V111), G152 (= G147), L153 (= L148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), Q208 (≠ E199), N209 (= N200), A210 (= A201), T213 (≠ A204)
Sites not aligning to the query:
- binding cobalamin: 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)
40% identity, 84% coverage: 35:213/213 of query aligns to 39:222/576 of 3ivaA
- active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
- binding cobalamin: H109 (= H104), G112 (= G107), V116 (= V111), G152 (= G147), L153 (= L148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), Q208 (≠ E199), N209 (= N200)
Sites not aligning to the query:
- binding cobalamin: 303, 443, 486, 488, 489, 495, 520, 521, 524, 527, 528
- binding s-adenosyl-l-homocysteine: 447, 484, 485, 489, 491, 539
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)
39% identity, 84% coverage: 35:213/213 of query aligns to 689:872/1227 of P13009
- E694 (= E40) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 101:105) binding methylcob(III)alamin
- D757 (= D102) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H104) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S149) binding methylcob(III)alamin
- T808 (= T153) binding methylcob(III)alamin
- S810 (≠ T155) mutation to A: Decreases activity by about 40%.
- A860 (= A201) binding methylcob(III)alamin
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.
- 946 binding S-adenosyl-L-methionine
- 1134 binding S-adenosyl-L-methionine
- 1189:1190 binding S-adenosyl-L-methionine
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
33% identity, 96% coverage: 8:211/213 of query aligns to 629:832/841 of 8g3hA
- binding cobalamin: F675 (= F54), V685 (= V64), K693 (≠ T72), G720 (= G101), V722 (= V103), H723 (= H104), D724 (= D105), I725 (= I106), G726 (= G107), V730 (= V111), M767 (≠ L148), S768 (= S149), L770 (= L151), V772 (≠ T153), I795 (≠ M178), L796 (≠ I179), G797 (= G180), G798 (= G181), A799 (= A182), Y818 (= Y197), A819 (= A198), E820 (= E199), D821 (≠ N200)
Sites not aligning to the query:
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
33% identity, 97% coverage: 6:211/213 of query aligns to 2:206/507 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)
37% identity, 72% coverage: 35:187/213 of query aligns to 704:866/1265 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.
8j2yA Acidimicrobiaceae bacterium photocobilins protein, dark state (see paper)
26% identity, 81% coverage: 10:181/213 of query aligns to 11:175/327 of 8j2yA
- binding cobalamin: A45 (= A44), Q48 (≠ M47), R49 (≠ N48), E65 (≠ V64), D100 (= D102), W101 (≠ V103), H102 (= H104), L104 (≠ I106), S105 (≠ G107), M108 (≠ I110), F109 (≠ V111), S147 (= S149), F153 (≠ T155), V173 (≠ I179), G174 (= G180), G175 (= G181)
Sites not aligning to the query:
8t0qA Open state of lysine 5,6-aminomutase from thermoanaerobacter tengcongensis
32% identity, 49% coverage: 93:196/213 of query aligns to 111:226/257 of 8t0qA
- binding cobalamin: H122 (= H104), V124 (≠ I106), G125 (= G107), I129 (≠ V111), Y135 (≠ S117), L174 (≠ G147), S176 (= S149), C209 (≠ I179), G210 (= G180), G211 (= G181), P212 (≠ A182)
Sites not aligning to the query:
1xrsB Crystal structure of lysine 5,6-aminomutase in complex with plp, cobalamin, and 5'-deoxyadenosine (see paper)
28% identity, 49% coverage: 93:196/213 of query aligns to 73:188/212 of 1xrsB
- active site: K95 (≠ L115)
- binding cobalamin: D82 (= D102), A83 (≠ V103), H84 (= H104), T85 (≠ D105), V86 (≠ I106), I91 (≠ V111), Y97 (≠ S117), L136 (≠ G147), V137 (≠ L148), S138 (= S149), T142 (= T153), L170 (≠ M178), C171 (≠ I179), G172 (= G180), G173 (= G181), P174 (≠ A182)
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)
28% identity, 49% coverage: 93:196/213 of query aligns to 122:237/262 of E3PRJ4
- 130:136 (vs. 101:107, 43% identical) binding adenosylcob(III)alamin
- K144 (≠ L115) modified: N6-(pyridoxal phosphate)lysine
- 185:192 (vs. 147:153, 25% identical) binding adenosylcob(III)alamin
- LCGGP 219:223 (≠ MIGGA 178:182) 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)
32% identity, 48% coverage: 94:196/213 of query aligns to 596:705/728 of 3koyA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ V103), H606 (= H104), S607 (≠ D105), V608 (≠ I106), V613 (= V111), S655 (= S149), I658 (≠ M152), S659 (≠ T153), G689 (= G180), G690 (= G181), T691 (≠ A182)
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)
32% identity, 48% coverage: 94:196/213 of query aligns to 596:705/728 of 3koxA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ V103), H606 (= H104), S607 (≠ D105), V608 (≠ I106), G609 (= G107), A654 (≠ L148), S655 (= S149), I657 (≠ L151), S659 (≠ T153), G689 (= G180), G690 (= G181), T691 (≠ A182)
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)
32% identity, 48% coverage: 94:196/213 of query aligns to 596:705/728 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_048036790.1 NCBI__GCF_000007065.1:WP_048036790.1
MSKEELLQELADAVITCKKDAVLAAVEKAKGELDPSEIIENGLAAGMNEVGVRFERGKLF
LPHVMMAADAMTAGVNALKDLMPEGSASSKMGVIVNGTVEGDVHDIGKSIVSTMLQSAGF
EVHDIGRDVPIRNFIEKAKEVNADMIGLSALMTTTLPGQRDVIELLKEEGLRDKVKVMIG
GAPATQAWADKIGADCYAENASEAVTKAKELLA
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