SitesBLAST
Comparing 349868 FitnessBrowser__Btheta:349868 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)
46% identity, 32% coverage: 406:598/602 of query aligns to 20:214/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D488), I105 (≠ L489), H106 (= H490), I108 (= I492), G109 (= G493), V113 (= V497), S150 (≠ M534), S151 (= S535), L153 (= L537), M154 (≠ L538), T155 (= T539), M180 (= M564), G182 (= G566), G183 (= G567), G200 (≠ S584), S202 (≠ N586), A203 (= A587)
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
63% identity, 20% coverage: 476:598/602 of query aligns to 3:125/125 of 1y80A
- active site: D15 (= D488), H17 (= H490), T68 (= T541)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D488), L16 (= L489), H17 (= H490), D18 (= D491), I19 (= I492), G20 (= G493), V24 (= V497), G60 (≠ C533), M61 (= M534), S62 (= S535), L64 (= L537), L65 (= L538), T66 (= T539), I91 (≠ M564), G93 (= G566), G94 (= G567), A95 (= A568), P112 (≠ D585), D113 (≠ N586), A114 (= A587)
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
40% identity, 31% coverage: 396:579/602 of query aligns to 9:193/212 of 3ezxA
- active site: D100 (= D488), H102 (= H490), S155 (≠ T541)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M434), F54 (= F441), D100 (= D488), I101 (≠ L489), H102 (= H490), D103 (= D491), I104 (= I492), V109 (= V497), V147 (≠ C533), S149 (= S535), L151 (= L537), M152 (≠ L538), T153 (= T539), M178 (= M564), G180 (= G566), G181 (= G567)
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)
40% identity, 29% coverage: 423:595/602 of query aligns to 36:202/206 of 4jgiB
- active site: D95 (= D488), H97 (= H490), A148 (≠ T541)
- binding co-methylcobalamin: L63 (= L451), D95 (= D488), L96 (= L489), H97 (= H490), D98 (= D491), I99 (= I492), G100 (= G493), F104 (≠ V497), G140 (≠ C533), S142 (= S535), L145 (= L538), G173 (= G566), G174 (= G567), V175 (≠ A568), S191 (= S584), T192 (≠ D585), N193 (= N586), A194 (= A587)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
33% identity, 34% coverage: 394:599/602 of query aligns to 11:222/577 of 3bulA
- active site: D107 (= D488), H109 (= H490), S160 (≠ T541)
- binding cobalamin: H109 (= H490), V116 (= V497), G152 (≠ C533), L153 (≠ M534), S154 (= S535), L156 (= L537), I157 (≠ L538), T158 (= T539), G183 (= G566), G184 (= G567), Q208 (≠ D585), N209 (= N586), A210 (= A587), T213 (≠ A590)
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)
33% identity, 34% coverage: 394:599/602 of query aligns to 11:222/576 of 3ivaA
- active site: D107 (= D488), H109 (= H490), S160 (≠ T541)
- binding cobalamin: H109 (= H490), G112 (= G493), V116 (= V497), G152 (≠ C533), L153 (≠ M534), S154 (= S535), L156 (= L537), I157 (≠ L538), T158 (= T539), G183 (= G566), G184 (= G567), Q208 (≠ D585), N209 (= N586)
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)
31% identity, 43% coverage: 339:598/602 of query aligns to 622:871/1227 of P13009
- E694 (≠ N427) binding
- GDVHD 756:760 (≠ GDLHD 487:491) binding
- D757 (= D488) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H490) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S535) binding
- T808 (= T539) binding
- S810 (≠ T541) mutation to A: Decreases activity by about 40%.
- A860 (= A587) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding
- 310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 946 binding
- 1134 binding
- 1189:1190 binding
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, 34% coverage: 394:598/602 of query aligns to 11:221/246 of 1bmtA
- active site: D107 (= D488), H109 (= H490), S160 (≠ T541)
- binding co-methylcobalamin: E44 (≠ N427), M48 (≠ I431), M51 (= M434), G55 (= G438), L65 (≠ V448), V68 (≠ L451), D107 (= D488), V108 (≠ L489), H109 (= H490), D110 (= D491), I111 (= I492), I115 (≠ L496), G152 (≠ C533), L153 (≠ M534), S154 (= S535), L156 (= L537), I157 (≠ L538), T158 (= T539), G183 (= G566), G184 (= G567), A185 (= A568), V207 (≠ S584), N209 (= N586), A210 (= A587)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8
36% identity, 28% coverage: 413:580/602 of query aligns to 23:185/507 of 8sseA
Sites not aligning to the query:
- binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 30% coverage: 422:601/602 of query aligns to 656:836/841 of 8g3hA
- binding cobalamin: F675 (= F441), V685 (≠ L451), K693 (= K459), G720 (= G487), V722 (≠ L489), H723 (= H490), D724 (= D491), I725 (= I492), G726 (= G493), V730 (= V497), M767 (= M534), S768 (= S535), L770 (= L537), V772 (≠ T539), I795 (≠ M564), L796 (≠ I565), G797 (= G566), G798 (= G567), A799 (= A568), Y818 (= Y583), A819 (≠ S584), E820 (≠ D585), D821 (≠ N586)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
32% identity, 36% coverage: 384:599/602 of query aligns to 31:243/258 of 2i2xB
- active site: D134 (= D488), H136 (= H490), T187 (= T541)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G487), D134 (= D488), V135 (≠ L489), H136 (= H490), D137 (= D491), I138 (= I492), G139 (= G493), V143 (= V497), T179 (≠ C533), T181 (≠ S535), L183 (= L537), M184 (≠ L538), T185 (= T539), A208 (≠ M564), G210 (= G566), G211 (= G567), G212 (≠ A568), G228 (≠ S584), E229 (≠ D585), E230 (≠ N586), A231 (= A587)
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)
32% identity, 36% coverage: 384:599/602 of query aligns to 31:243/258 of Q46EH4
- H129 (≠ G483) mutation to K: Does not affect cobalamin-binding.
- H136 (= H490) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
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, 25% coverage: 422:572/602 of query aligns to 704:865/1265 of Q99707
Sites not aligning to the query:
- 61 natural variant: R -> K
- 255 C → Y: in dbSNP:rs1140598
- 382:384 binding
- 449 binding
- 470 binding
- 537 binding
- 579 binding
- 585 binding
- 591 binding
- 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.
E3PY95 D-ornithine 4,5-aminomutase subunit beta; D-ornithine aminomutase E component; OAM-E; EC 5.4.3.5 from Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) (see 2 papers)
32% identity, 20% coverage: 479:601/602 of query aligns to 604:733/740 of E3PY95
- EHS 614:616 (≠ LHD 489:491) binding
- H615 (= H490) binding axial binding residue; mutation to G: Loss of corrinoid-binding ability.
- K626 (vs. gap) modified: N6-(pyridoxal phosphate)lysine
- STIISH 664:669 (≠ SALLTT 535:540) binding
Sites not aligning to the query:
1id8A Nmr structure of glutamate mutase (b12-binding subunit) complexed with the vitamin b12 nucleotide (see paper)
31% identity, 15% coverage: 480:570/602 of query aligns to 6:95/137 of 1id8A
Sites not aligning to the query:
3koyA Crystal structure of ornithine 4,5 aminomutase in complex with ornithine (aerobic) (see paper)
32% identity, 20% coverage: 479:601/602 of query aligns to 595:724/728 of 3koyA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ L489), H606 (= H490), S607 (≠ D491), V608 (≠ I492), V613 (= V497), S655 (= S535), I658 (≠ L538), S659 (≠ T539), G689 (= G566), G690 (= G567), T691 (≠ A568), F707 (≠ S584), G710 (≠ A587), S711 (≠ N588)
Sites not aligning to the query:
- active site: 183, 218, 290
- binding cobalamin: 112, 483
- 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, 20% coverage: 479:601/602 of query aligns to 595:724/728 of 3koxA
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ L489), H606 (= H490), S607 (≠ D491), V608 (≠ I492), G609 (= G493), A654 (≠ M534), S655 (= S535), I657 (≠ L537), S659 (≠ T539), G689 (= G566), G690 (= G567), T691 (≠ A568), F707 (≠ S584), G708 (≠ D585), G710 (≠ A587), S711 (≠ N588)
Sites not aligning to the query:
- active site: 183, 218, 290
- binding cobalamin: 112, 483
- 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, 20% coverage: 479:601/602 of query aligns to 595:724/728 of 3kowB
- active site: K617 (vs. gap)
- binding cobalamin: E605 (≠ L489), H606 (= H490), S607 (≠ D491), V608 (≠ I492), G609 (= G493), L610 (≠ K494), I657 (≠ L537), G689 (= G566), G690 (= G567), T691 (≠ A568), F707 (≠ S584), S711 (≠ N588)
Sites not aligning to the query:
- active site: 183, 218, 290
- binding pyridoxal-5'-phosphate: 105, 110, 156, 158, 178, 183, 188, 218, 219
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, 18% coverage: 476:582/602 of query aligns to 116:237/262 of E3PRJ4
- 130:136 (vs. 488:493, 43% identical) binding
- K144 (≠ L501) modified: N6-(pyridoxal phosphate)lysine
- 185:192 (vs. 533:540, 25% identical) binding
- LCGGP 219:223 (≠ MIGGA 564:568) binding
Sites not aligning to the query:
1xrsB Crystal structure of lysine 5,6-aminomutase in complex with plp, cobalamin, and 5'-deoxyadenosine (see paper)
29% identity, 18% coverage: 476:581/602 of query aligns to 67:187/212 of 1xrsB
- active site: K95 (≠ L501)
- binding cobalamin: D82 (= D488), A83 (≠ L489), H84 (= H490), T85 (≠ D491), V86 (≠ I492), I91 (≠ V497), Y97 (≠ G503), L136 (≠ C533), V137 (≠ M534), S138 (= S535), T142 (= T539), L170 (≠ M564), C171 (≠ I565), G172 (= G566), G173 (= G567), P174 (≠ A568)
Sites not aligning to the query:
Query Sequence
>349868 FitnessBrowser__Btheta:349868
MKTWKTNLEETKQRYINWWNHKGIILSMWEHFQEGVKPHADIAPPAPARDLSQKWFDPQW
RAEYLDWYVAHSSLMADMLPVANTQLGPGSLAAILGGVFEGGEDTIWIHPDPNFNDEIVF
NPEHPNWLLHKELLKACKAKANGNYFVGMPDLMEGLDVLAALKGTDMVLLDTVMQSEVLE
QQMQQINDIYFKVFDELYDIIREGDEMAFCYFSSWAPGKMSKLQSDISTMISQDDYRRFV
QPFIREQCQKIDYTLYHLDGVGAMHHLPALLEIEELNAIQWTPGVGEPQGGSPKWYDLYK
KILAGGKSVMACWVTLEELKPLLDHIGADGVHLEMDFHNEREVEQAMRIIEEYTGSSSSV
SADVHTNQPVGEQDNAQESIRIREEKSQEEDRMKPLYDAIVAGKLEPAVEVTKDAIAAGV
LPQDIINGYMITAMGEVGQRFQDGKAFVPQLLMAGRAMKGALELLKPLLAGNASATIGKI
VIGTVKGDLHDIGKNLVASMLEGCGFEVINIGIDVTCDKFVEAVKENKADILCMSALLTT
TMTYMQDVIRALEEAGIRDQVKVMIGGAPVSQGFADEIGADGYSDNANTAVAVAKVLMGK
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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