SitesBLAST
Comparing WP_109969686.1 NCBI__GCF_003173355.1:WP_109969686.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see paper)
42% identity, 85% coverage: 15:254/281 of query aligns to 11:259/304 of Q96XT4
- C12 (= C16) binding [4Fe-4S] cluster
- C15 (= C19) binding [4Fe-4S] cluster
- IGCS 44:47 (≠ IGCH 51:54) binding thiamine diphosphate
- C46 (= C53) binding [4Fe-4S] cluster
- D90 (= D95) binding Mg(2+)
- GD 91:92 (= GD 96:97) binding thiamine diphosphate
- N118 (= N123) binding Mg(2+)
- V120 (= V125) binding Mg(2+)
- GL 122:123 (= GL 127:128) binding thiamine diphosphate
- C197 (= C202) binding [4Fe-4S] cluster
5b46B 2-oxoacid:ferredoxin oxidoreductase 2 from sulfolobus tokodai - ligand free form (see paper)
42% identity, 85% coverage: 15:254/281 of query aligns to 8:256/301 of 5b46B
- binding magnesium ion: D87 (= D95), N115 (= N123), V117 (= V125)
- binding iron/sulfur cluster: W8 (= W15), C9 (= C16), C12 (= C19), C43 (= C53), C194 (= C202), T196 (≠ S204), Y197 (≠ F205)
- binding thiamine diphosphate: I41 (= I51), G42 (= G52), C43 (= C53), S44 (≠ H54), H62 (= H70), G86 (= G94), G88 (= G96), D89 (= D97), N115 (= N123), V117 (= V125), Y118 (= Y126), G119 (= G127), L120 (= L128), T121 (= T129)
P72579 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 from Sulfolobus sp. (see paper)
41% identity, 91% coverage: 9:264/281 of query aligns to 5:269/305 of P72579
- K49 (= K56) mutation to I: Strong decrease of the oxidoreductase activity with pyruvate, 2-oxobutyrate and 2-oxoglutarate.; mutation to R: Increase the oxidoreductase activity with pyruvate.; mutation to V: Slight decrease of the oxidoreductase activity with pyruvate, 2-oxobutyrate and 2-oxoglutarate.
- L123 (= L128) mutation L->A,I: Strong decrease of the oxidoreductase activity with pyruvate, 2-oxobutyrate and 2-oxoglutarate.; mutation to N: Strong decrease of the oxidoreductase activity with pyruvate and 2-oxobutyrate. However, this mutant shows almost the same activity with 2-oxoglutarate as the wild-type.
Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 2 papers)
41% identity, 90% coverage: 13:264/281 of query aligns to 9:269/305 of Q96Y68
- C12 (= C16) binding [4Fe-4S] cluster
- C15 (= C19) binding [4Fe-4S] cluster
- C46 (= C53) binding [4Fe-4S] cluster
- K49 (= K56) mutation to I: Loss of oxidoreductase activity toward 2-oxoglutarate but retains its activity toward pyruvate.
- D90 (= D95) binding Mg(2+)
- GD 91:92 (= GD 96:97) binding thiamine diphosphate
- N118 (= N123) binding Mg(2+)
- V120 (= V125) binding Mg(2+)
- GL 122:123 (= GL 127:128) binding thiamine diphosphate
- K125 (≠ T130) Plays an important role in the binding of CoA; mutation to A: Shows a strong decrease of affinity for CoA and a poor inactivation by 4-fluoro-7-nitrobenzofurazan (NBD-F).
- K173 (≠ P178) mutation to A: Same oxidoreductase activity as the wild-type.
- C197 (= C202) binding [4Fe-4S] cluster
5b47B 2-oxoacid:ferredoxin oxidoreductase 2 from sulfolobus tokodai - pyruvate complex (see paper)
39% identity, 85% coverage: 15:254/281 of query aligns to 4:230/275 of 5b47B
- binding magnesium ion: D83 (= D95), N111 (= N123)
- binding iron/sulfur cluster: C5 (= C16), C8 (= C19), C39 (= C53), C179 (= C202)
- binding thiamine diphosphate: I37 (= I51), G38 (= G52), C39 (= C53), S40 (≠ H54), H58 (= H70), G84 (= G96), D85 (= D97), N111 (= N123), V113 (= V125), Y114 (= Y126), L116 (= L128)
5b48B 2-oxoacid:ferredoxin oxidoreductase 1 from sulfolobus tokodai (see paper)
39% identity, 91% coverage: 9:264/281 of query aligns to 1:251/286 of 5b48B
- binding magnesium ion: D84 (= D95), N112 (= N123), V114 (= V125)
- binding iron/sulfur cluster: C8 (= C16), C11 (= C19), C42 (= C53), C183 (= C202), T185 (≠ S204)
- binding 2-[(2E)-3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-2-(1-oxidanylpropylidene)-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: I40 (= I51), G41 (= G52), C42 (= C53), S43 (≠ H54), H59 (= H70), G85 (= G96), D86 (= D97), N112 (= N123), V114 (= V125), Y115 (= Y126), G116 (= G127), L117 (= L128)
6n2oD 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus with 2-oxoglutarate, coenzyme a and succinyl-coa bound (see paper)
34% identity, 91% coverage: 9:264/281 of query aligns to 18:269/291 of 6n2oD
- binding magnesium ion: D101 (= D95), N129 (= N123), I131 (≠ V125)
- binding succinyl-coenzyme a: I57 (= I51), R62 (≠ K56), L134 (= L128), K136 (≠ T130)
- binding iron/sulfur cluster: W24 (= W15), C25 (= C16), C28 (= C19), C59 (= C53), C208 (= C202), T210 (≠ S204), F211 (= F205)
- binding thiamine diphosphate: I57 (= I51), G58 (= G52), C59 (= C53), S60 (≠ H54), H76 (= H70), G102 (= G96), D103 (= D97), N129 (= N123), I131 (≠ V125), G133 (= G127), L134 (= L128), T135 (= T129)
6n2oB 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus with 2-oxoglutarate, coenzyme a and succinyl-coa bound (see paper)
34% identity, 91% coverage: 9:264/281 of query aligns to 18:269/291 of 6n2oB
- binding 2-oxoglutaric acid: R62 (≠ K56), L134 (= L128)
- binding coenzyme a: K136 (≠ T130), Y150 (≠ K144)
- binding magnesium ion: D101 (= D95), N129 (= N123), I131 (≠ V125)
- binding iron/sulfur cluster: W24 (= W15), C25 (= C16), C28 (= C19), C59 (= C53), C208 (= C202), T210 (≠ S204), F211 (= F205)
- binding thiamine diphosphate: I57 (= I51), G58 (= G52), C59 (= C53), S60 (≠ H54), H76 (= H70), G102 (= G96), D103 (= D97), N129 (= N123), I131 (≠ V125), Y132 (= Y126), G133 (= G127), L134 (= L128), T135 (= T129)
6n2nB Crystal structure of 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus (see paper)
34% identity, 91% coverage: 9:264/281 of query aligns to 18:269/291 of 6n2nB
- binding magnesium ion: D101 (= D95), N129 (= N123), I131 (≠ V125)
- binding iron/sulfur cluster: W24 (= W15), C25 (= C16), C28 (= C19), H30 (≠ N21), C59 (= C53), C208 (= C202), T210 (≠ S204), F211 (= F205)
- binding thiamine diphosphate: I57 (= I51), G58 (= G52), C59 (= C53), S60 (≠ H54), H76 (= H70), G100 (= G94), D101 (= D95), G102 (= G96), D103 (= D97), N129 (= N123), I131 (≠ V125), Y132 (= Y126), G133 (= G127), L134 (= L128), T135 (= T129)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
38% identity, 23% coverage: 71:134/281 of query aligns to 404:466/539 of 6lpiB
- active site: D428 (= D95), N455 (= N123), A457 (≠ V125), L458 (≠ Y126), L460 (= L128), V461 (≠ T129), Q464 (= Q132)
- binding magnesium ion: D428 (= D95), N455 (= N123)
- binding thiamine diphosphate: G427 (= G94), D428 (= D95), G429 (= G96), S430 (≠ D97), M433 (≠ A100), N455 (= N123), A457 (≠ V125), L458 (≠ Y126), G459 (= G127), L460 (= L128), V461 (≠ T129)
Sites not aligning to the query:
- active site: 27, 29, 30, 31, 32, 53, 76, 115, 116, 117, 165, 256, 283, 375, 401, 403
- binding flavin-adenine dinucleotide: 155, 212, 213, 214, 236, 237, 238, 254, 256, 257, 276, 277, 278, 280, 282, 283, 300, 301, 319, 320, 380, 398
- binding thiamine diphosphate: 53, 76, 79, 376, 377, 378, 401, 403
5exeC Crystal structure of oxalate oxidoreductase from moorella thermoacetica bound with carboxy-tpp adduct (see paper)
39% identity, 22% coverage: 89:149/281 of query aligns to 104:164/314 of 5exeC
- active site: N143 (≠ L128)
- binding [2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-carboxy-4-methyl-1,3-thiazol-3-ium-5-yl]ethoxy-oxidanyl-phosphoryl] hydrogen phosphate: G109 (= G94), D110 (= D95), G111 (= G96), Y136 (≠ H121), N138 (= N123), S140 (≠ V125), Y141 (= Y126), A142 (≠ G127), N143 (≠ L128), T144 (= T129)
- binding magnesium ion: D110 (= D95), D130 (= D115), N138 (= N123), S140 (≠ V125)
Sites not aligning to the query:
- binding [2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-carboxy-4-methyl-1,3-thiazol-3-ium-5-yl]ethoxy-oxidanyl-phosphoryl] hydrogen phosphate: 50, 51, 52, 74
- binding magnesium ion: 211, 213
- binding iron/sulfur cluster: 24, 27, 29, 52, 225, 226, 227
5c4iC Structure of an oxalate oxidoreductase (see paper)
39% identity, 22% coverage: 89:149/281 of query aligns to 104:164/312 of 5c4iC
- active site: N143 (≠ L128)
- binding magnesium ion: D110 (= D95), N138 (= N123), S140 (≠ V125)
- binding iron/sulfur cluster: A142 (≠ G127)
- binding thiamine diphosphate: G109 (= G94), D110 (= D95), G111 (= G96), Y136 (≠ H121), N138 (= N123), S140 (≠ V125), Y141 (= Y126), A142 (≠ G127), N143 (≠ L128), T144 (= T129)
Sites not aligning to the query:
5exdF Crystal structure of oxalate oxidoreductase from moorella thermoacetica bound with carboxy-di-oxido-methyl-tpp (coom-tpp) intermediate (see paper)
39% identity, 22% coverage: 89:149/281 of query aligns to 104:164/310 of 5exdF
- active site: N143 (≠ L128)
- binding magnesium ion: D110 (= D95), N138 (= N123), S140 (≠ V125)
- binding [2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-2-[1,1,2-tris(oxidanyl)-2-oxidanylidene-ethyl]-1,3-thiazol-3-ium-5-yl]ethoxy-oxidanyl-phosphoryl] hydrogen phosphate: D110 (= D95), G111 (= G96), Y136 (≠ H121), N138 (= N123), S140 (≠ V125), Y141 (= Y126), A142 (≠ G127), N143 (≠ L128), T144 (= T129)
- binding iron/sulfur cluster: A142 (≠ G127)
Sites not aligning to the query:
- binding [2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-2-[1,1,2-tris(oxidanyl)-2-oxidanylidene-ethyl]-1,3-thiazol-3-ium-5-yl]ethoxy-oxidanyl-phosphoryl] hydrogen phosphate: 50, 51, 52, 74
- binding iron/sulfur cluster: 24, 27, 29, 52, 225, 227
Query Sequence
>WP_109969686.1 NCBI__GCF_003173355.1:WP_109969686.1
MTSEESLVTQAQNTWCPGCGNFAIQHAMKFVIQELEAEGISRDQFVLVSGIGCHAKIADY
FQLNSFYSLHGRTIPVATGIKMANPDLKVICFAGDGDLYAEGLDHLIHAAKRNIDITVIC
HNNRVYGLTTGQYTPTSPYGYKGKSTPQGLHEYPLNVIELLLGSGATFVSRAYTRRLPHL
RRIFREAIMHPGFAHVDVLQICASFFNMTTWYDERIYETSESNAGLFEFACRTAQQWNYN
DDAKIPIGIFFKTKKPVLPEKKIKKEVNRSNLVKTILDRAT
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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