SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 7025321 FitnessBrowser__ANA3:7025321 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 8 hits to proteins with known functional sites (download)

Q88E47 Homogentisate 1,2-dioxygenase; HGDO; Homogentisate oxygenase; Homogentisic acid oxidase; Homogentisicase; EC 1.13.11.5 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
24% identity, 74% coverage: 100:383/386 of query aligns to 129:421/433 of Q88E47

query
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Q88E47

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H288 (= H263) active site, Proton acceptor; mutation to F: Reduces the catalytic efficiency 75-fold.
Y346 (≠ F316) binding ; mutation to F: Decreases the affinity for homogentisate more than 60-fold and reduces the catalytic efficiency 20-fold.
H367 (= H336) binding

3zdsA Structure of homogentisate 1,2-dioxygenase in complex with reaction intermediates of homogentisate with oxygen. (see paper)
24% identity, 74% coverage: 100:383/386 of query aligns to 121:413/425 of 3zdsA

query
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3zdsA

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active site: H280 (= H263), H323 (= H300), E329 (= E307), H353 (= H330), H359 (= H336)
binding fe (iii) ion: H323 (= H300), E329 (= E307), H359 (= H336)
binding 4-Maleylacetoacetic acid: H280 (= H263), P283 (= P266), P320 (= P297), W321 (≠ Y298), H323 (= H300), M331 (≠ L309), Y338 (≠ F316), H359 (= H336), M386 (= M358)

3zdsF Structure of homogentisate 1,2-dioxygenase in complex with reaction intermediates of homogentisate with oxygen. (see paper)
23% identity, 74% coverage: 100:383/386 of query aligns to 122:414/426 of 3zdsF

query
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3zdsF

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active site: H281 (≠ P266), H324 (= H300), E330 (= E307), H354 (= H330), H360 (= H336)
binding fe (iii) ion: H324 (= H300), E330 (= E307), H360 (= H336)
binding 2-[(6R)-6-(dioxidanyl)-6-oxidanyl-3-oxidanylidene-cyclohexa-1,4-dien-1-yl]ethanoic acid: H281 (≠ P266), P284 (≠ H269), P321 (= P297), W322 (≠ Y298), H324 (= H300), E330 (= E307), M332 (≠ L309), Y339 (≠ F316), H360 (= H336), M387 (= M358)

3zdsC Structure of homogentisate 1,2-dioxygenase in complex with reaction intermediates of homogentisate with oxygen. (see paper)
23% identity, 74% coverage: 100:383/386 of query aligns to 122:414/426 of 3zdsC

query
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3zdsC

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W

active site: H281 (≠ P266), H324 (= H300), E330 (= E307), H354 (= H330), H360 (= H336)
binding fe (iii) ion: H324 (= H300), E330 (= E307), H360 (= H336)
binding 2-(6-oxidanyl-3-oxidanylidene-cyclohexa-1,4-dien-1-yl)ethanoic acid: H281 (≠ P266), P284 (≠ H269), F307 (vs. gap), P321 (= P297), E330 (= E307), M332 (≠ L309), Y339 (≠ F316), H360 (= H336)
binding oxygen molecule: P284 (≠ H269), H324 (= H300), E330 (= E307)

4aq6D Substrate bound homogentisate 1,2-dioxygenase (see paper)
24% identity, 74% coverage: 100:383/386 of query aligns to 123:415/427 of 4aq6D

query
sites
4aq6D

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active site: H282 (= H263), H325 (= H300), E331 (= E307), H355 (= H330), H361 (= H336)
binding fe (iii) ion: H325 (= H300), E331 (= E307), H361 (= H336)
binding 2-(3,6-dihydroxyphenyl)acetic acid: H282 (= H263), P285 (= P266), P322 (= P297), W323 (≠ Y298), E331 (= E307), M333 (≠ L309), Y340 (≠ F316), H361 (= H336)

Q93099 Homogentisate 1,2-dioxygenase; Homogentisate oxygenase; Homogentisic acid oxidase; Homogentisicase; EC 1.13.11.5 from Homo sapiens (Human) (see 13 papers)
22% identity, 75% coverage: 94:383/386 of query aligns to 125:427/445 of Q93099

query
sites
Q93099

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G161 (= G129) to R: in AKU; loss of activity; most prevalent mutation in Slovak and Czech patients; dbSNP:rs28941783
E168 (= E136) to K: in AKU; loss of activity; dbSNP:rs375283568
M172 (≠ L140) natural variant: M -> T
P230 (= P204) to S: in AKU; complete loss of activity; dbSNP:rs28942100
H335 (= H300) binding
E341 (= E307) binding
M368 (≠ G333) to V: in AKU; loss of activity; dbSNP:rs120074173
H371 (= H336) binding

Sites not aligning to the query:

80 Q → H: in dbSNP:rs2255543

Q9Y041 Homogentisate 1,2-dioxygenase; Homogentisate oxygenase; Homogentisic acid oxidase; Homogentisicase; EC 1.13.11.5 from Caenorhabditis elegans (see paper)
24% identity, 58% coverage: 117:338/386 of query aligns to 152:374/437 of Q9Y041

query
sites
Q9Y041

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G173 (= G138) mutation to R: Suppresses fah-1 RNAi-mediated toxicity.

1ey2A Human homogentisate dioxygenase with fe(ii) (see paper)
24% identity, 63% coverage: 94:338/386 of query aligns to 124:364/419 of 1ey2A

query
sites
1ey2A

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active site: H291 (= H263), H334 (= H300), E340 (= E307), H356 (= H330), H362 (= H336)
binding fe (ii) ion: H334 (= H300), E340 (= E307), H362 (= H336)

Query Sequence

>7025321 FitnessBrowser__ANA3:7025321
MPFYVKQGQVPHKRHIAFEKENGELYREELFSTHGFSNIYSNKYHHNMPTKALEVAPYRL
GHGAQWEDSLVQNYKLDSRTADREGNFFSARNKIFYNNDVAIYTAKVTQDTPEFYRNAYA
DEVVFVHEGEGTLYSEYGTLEIKKWDYLVIPRGTTHQLKFNDYSNVRLFVIEAFSMVEVP
KHFRNEYGQLLESAPYCERDLRTPVLQDAVVERGAFPLVCKFGDKYQLTTLEWHPFDLAG
WDGCVYPWAFNITEYAPKVGKIHLPPSDHLVFTAHNFVVCNFVPRPYDFHERAIPAPYYH
NNIDSDEVLYYVDGDFMSRTEIEAGYITLHQKGVAHGPQPGRTEASIGKKETYEYAVMVD
TFAPLKLTEHVQNCMSKDYNRSWLEN

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