SitesBLAST
Comparing WP_011320615.1 NCBI__GCF_000204075.1:WP_011320615.1 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)
Q9GJX5 Taurochenodeoxycholic 6 alpha-hydroxylase; CYPIVA21; Cytochrome P450 4A21; EC 1.14.14.57 from Sus scrofa (Pig) (see 2 papers)
26% identity, 90% coverage: 30:441/459 of query aligns to 71:498/504 of Q9GJX5
- AAGHDS 314:319 (≠ FAGHET 260:265) mutation to FEGHDT: Complete loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6ooaA Human cyp3a4 bound to a drug substrate (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 11:445/452 of 6ooaA
- active site: T265 (= T265), F391 (= F386), C398 (= C393)
- binding protoporphyrin ix containing fe: R78 (≠ N74), I91 (≠ L86), S92 (≠ M87), W99 (≠ H94), R103 (= R98), F110 (= F105), F258 (≠ I258), A261 (= A261), T265 (= T265), L329 (= L326), R331 (= R329), P390 (= P385), F391 (= F386), G392 (= G387), R396 (= R391), N397 (≠ R392), C398 (= C393), I399 (≠ L394), A404 (= A399), M408 (≠ I403)
- binding (3aS,4R,5S,6R,8R,9R,9aR,10R)-6-ethyl-5-hydroxy-4,6,9,10-tetramethyl-1-oxodecahydro-3a,9-propanocyclopenta[8]annulen-8-yl [(5-amino-1H-1,2,4-triazol-3-yl)sulfanyl]acetate: S92 (≠ M87), L183 (vs. gap), F260 (= F260), A261 (= A261)
P33274 Cytochrome P450 4F1; CYPIVF1; Cytochrome P450-A3; Leukotriene-B4 20-monooxygenase; EC 1.14.14.94 from Rattus norvegicus (Rat) (see paper)
26% identity, 79% coverage: 76:439/459 of query aligns to 127:512/524 of P33274
- E328 (≠ A261) binding covalent
- C468 (= C393) binding axial binding residue
P51869 Cytochrome P450 4F4; CYPIVF4; Leukotriene-B4 20-monooxygenase; EC 1.14.14.94 from Rattus norvegicus (Rat) (see paper)
25% identity, 95% coverage: 2:439/459 of query aligns to 48:512/522 of P51869
- E328 (≠ A261) binding covalent
- C468 (= C393) binding axial binding residue
6uneA Human cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 10:445/452 of 6uneA
- active site: T265 (= T265), F391 (= F386), C398 (= C393)
- binding protoporphyrin ix containing fe: R77 (≠ N74), I90 (≠ L86), S91 (≠ M87), W98 (≠ H94), R102 (= R98), F109 (= F105), F258 (≠ I258), A261 (= A261), T265 (= T265), I325 (≠ V322), L329 (= L326), R331 (= R329), P390 (= P385), F391 (= F386), G392 (= G387), R396 (= R391), N397 (≠ R392), C398 (= C393), A404 (= A399), M408 (≠ I403)
- binding tert-butyl [(2R)-1-(1H-indol-3-yl)-3-{[(2S)-3-oxo-2-(phenylamino)-3-{[(pyridin-3-yl)methyl]amino}propyl]sulfanyl}propan-2-yl]carbamate: R77 (≠ N74), R78 (≠ K75), F80 (≠ A77), S91 (≠ M87), I92 (≠ L88), F182 (≠ Y161), F184 (≠ Q163), F210 (≠ Q205), I257 (≠ T257), F260 (= F260), A261 (= A261)
7ufaA Cyp3a4 bound to an inhibitor (see paper)
25% identity, 95% coverage: 5:439/459 of query aligns to 11:440/448 of 7ufaA
- binding protoporphyrin ix containing fe: R78 (≠ N74), I91 (≠ L86), S92 (≠ M87), W99 (≠ H94), R103 (= R98), F110 (= F105), F253 (≠ I258), A256 (= A261), R326 (= R329), P385 (= P385), F386 (= F386), G387 (= G387), R391 (= R391), N392 (≠ R392), C393 (= C393), A399 (= A399), M403 (≠ I403)
- binding tert-butyl [(2S)-1-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-4-yl)propyl]amino}propan-2-yl]sulfanyl}-3-phenylpropan-2-yl]carbamate: R78 (≠ N74), S92 (≠ M87), F205 (≠ Q205), I251 (≠ L256), F255 (= F260), A256 (= A261), T260 (= T265)
Q9HBI6 Cytochrome P450 4F11; CYPIVF11; 3-hydroxy fatty acids omega-hydroxylase CYP4F11; Docosahexaenoic acid omega-hydroxylase; Long-chain fatty acid omega-monooxygenase; Phylloquinone omega-hydroxylase CYP4F11; EC 1.14.14.1; EC 1.14.14.79; EC 1.14.14.80; EC 1.14.14.78 from Homo sapiens (Human) (see 5 papers)
27% identity, 75% coverage: 96:439/459 of query aligns to 146:512/524 of Q9HBI6
- C260 (= C208) modified: 4-hydroxynonenal-conjugated cysteine
- H261 (vs. gap) modified: 4-hydroxynonenal-conjugated histidine
- C276 (≠ T222) to R: in dbSNP:rs8104361
- H347 (≠ N280) modified: 4-hydroxynonenal-conjugated histidine
- C354 (≠ L287) modified: 4-hydroxynonenal-conjugated cysteine
- D446 (≠ I374) to N: does not affect enzyme activity; dbSNP:rs1060463
- K451 (≠ R376) modified: 4-hydroxynonenal-conjugated lysine
Sites not aligning to the query:
- 45 modified: 4-hydroxynonenal-conjugated cysteine
2ve3A Retinoic acid bound cyanobacterial cyp120a1 (see paper)
28% identity, 90% coverage: 6:418/459 of query aligns to 7:408/435 of 2ve3A
- active site: A246 (= A261), E249 (= E264), T250 (= T265), L251 (≠ T266), F376 (= F386), C383 (= C393), E392 (= E402)
- binding protoporphyrin ix containing fe: L85 (= L86), H93 (= H94), R97 (= R98), F151 (≠ V152), L242 (≠ T257), L243 (≠ I258), A246 (= A261), G247 (= G262), T250 (= T265), P309 (≠ V322), V310 (≠ L323), R315 (≠ P328), Y336 (≠ A350), P375 (= P385), F376 (= F386), R381 (= R391), C383 (= C393), A389 (= A399)
- binding retinoic acid: F21 (≠ W20), W72 (≠ G73), F174 (≠ D176), F245 (= F260), G311 (≠ P324), G312 (≠ T325), Q337 (≠ S351)
6unlA Cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 12:429/436 of 6unlA
- active site: T249 (= T265), F375 (= F386), C382 (= C393)
- binding protoporphyrin ix containing fe: R79 (≠ N74), I92 (≠ L86), S93 (≠ M87), W100 (≠ H94), R104 (= R98), F111 (= F105), F242 (≠ I258), A245 (= A261), T249 (= T265), I309 (≠ V322), L313 (= L326), R315 (= R329), P374 (= P385), F375 (= F386), G376 (= G387), R380 (= R391), N381 (≠ R392), C382 (= C393)
- binding tert-butyl [(2R)-1-(naphthalen-1-yl)-3-{[(2S)-3-(naphthalen-1-yl)-1-oxo-1-{[(pyridin-3-yl)methyl]amino}propan-2-yl]sulfanyl}propan-2-yl]carbamate: R79 (≠ N74), F82 (≠ A77), S93 (≠ M87), I94 (≠ L88), F174 (= F168), F195 (≠ Y210), I241 (≠ T257), F244 (= F260), A245 (= A261), T249 (= T265)
7uffB Human cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 10:437/444 of 7uffB
- binding protoporphyrin ix containing fe: R77 (≠ N74), W98 (≠ H94), R102 (= R98), F250 (≠ I258), A253 (= A261), I317 (≠ V322), L321 (= L326), R323 (= R329), P382 (= P385), F383 (= F386), G384 (= G387), R388 (= R391), N389 (≠ R392), C390 (= C393), F395 (≠ L398), A396 (= A399), M400 (≠ I403)
- binding N-(2-oxo-2-{[(2S)-1-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}-3-phenylpropan-2-yl]amino}ethyl)pyridine-3-carboxamide: D48 (≠ A44), R78 (≠ K75), S91 (≠ M87), I249 (≠ T257), F252 (= F260), A253 (= A261), T257 (= T265)
6ungA Human cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 11:446/453 of 6ungA
- active site: T266 (= T265), F392 (= F386), C399 (= C393)
- binding protoporphyrin ix containing fe: R78 (≠ N74), S92 (≠ M87), R103 (= R98), F110 (= F105), F259 (≠ I258), A262 (= A261), G263 (= G262), T266 (= T265), I326 (≠ V322), L330 (= L326), R332 (= R329), P391 (= P385), F392 (= F386), G393 (= G387), R397 (= R391), N398 (≠ R392), C399 (= C393), G401 (= G395), M409 (≠ I403)
- binding tert-butyl [(2S)-1-(naphthalen-1-yl)-3-{[(2R)-3-oxo-2-(phenylamino)-3-{[(pyridin-3-yl)methyl]amino}propyl]sulfanyl}propan-2-yl]carbamate: R78 (≠ N74), S92 (≠ M87), F183 (≠ Y161), F211 (≠ Q205), I258 (≠ T257), F261 (= F260), A262 (= A261), T266 (= T265), L439 (≠ F431)
8gk3A Cytochrome p450 3a7 in complex with dehydroepiandrosterone sulfate (see paper)
24% identity, 94% coverage: 5:434/459 of query aligns to 14:461/473 of 8gk3A
- binding protoporphyrin ix containing fe: R81 (≠ N74), I94 (≠ L86), S95 (≠ M87), R106 (= R98), A281 (= A261), G282 (= G262), T285 (= T265), L349 (= L326), R351 (= R329), F411 (= F386), R416 (= R391), N417 (≠ R392), C418 (= C393), I419 (≠ L394), A424 (= A399), M428 (≠ I403)
- binding 17-oxoandrost-5-en-3beta-yl hydrogen sulfate: F202 (≠ L189), F204 (≠ Q191), L212 (≠ W199), R219 (≠ Q206)
Sites not aligning to the query:
7p6lB Heme domain of cyp505a30, a fungal hydroxylase from myceliophthora thermophila, bound to dodecanoic acid
27% identity, 86% coverage: 24:420/459 of query aligns to 25:432/458 of 7p6lB
- binding protoporphyrin ix containing fe: K69 (≠ I70), L86 (≠ D92), F87 (≠ R93), F107 (= F105), F261 (≠ I258), A264 (= A261), G265 (= G262), T268 (= T265), T269 (= T266), I328 (≠ L323), I331 (≠ F327), P397 (= P385), F398 (= F386), G399 (= G387), R403 (= R391), C405 (= C393), I406 (≠ L394), G407 (= G395), A411 (= A399)
P20817 Cytochrome P450 4A14; CYPIVA14; Cytochrome P450-LA-omega 3; Lauric acid omega-hydroxylase; Long-chain fatty acid omega-monooxygenase; EC 1.14.14.80 from Rattus norvegicus (Rat) (see 4 papers)
24% identity, 87% coverage: 43:441/459 of query aligns to 87:501/507 of P20817
- K91 (≠ G47) mutation to T: Impairs substrate binding.
- A113 (≠ D69) mutation to P: 70-fold increase of the binding constant for lauric acid associated with higher catalytic activity.
- SGI 114:116 (≠ IGR 70:72) mutation Missing: Higher kcat for hydroxylation of lauric acid. 2-fold increase of omega/(omega-1) hydroxylation ratio for lauric and myristic acids; when associated with S-119.
- F119 (≠ K75) mutation to S: 7-fold increase of the binding constant for lauric acid associated with higher catalytic activity. 2-fold increase of omega/omega-1 hydroxylation ratio for lauric and myristic acids; when associated with S114_I116del.
- E318 (≠ A261) binding covalent; mutation to A: Loss of covalent heme binding.; mutation to D: Significant reduction in covalent heme binding.; mutation to Q: Significant reduction in covalent heme binding.
- C454 (= C393) binding axial binding residue
Sites not aligning to the query:
- 1:4 modified: propeptide, Removed in mature form
- 63 D→N: Has no significant effect on the catalytic activity toward lauric and myristic acids.
P24462 Cytochrome P450 3A7; CYPIIIA7; Cytochrome P450-HFLA; P450HLp2; EC 1.14.14.1 from Homo sapiens (Human) (see paper)
25% identity, 88% coverage: 29:434/459 of query aligns to 66:485/503 of P24462
- N116 (≠ T84) mutation to S: Has no effect on catalytic activity.
- H174 (≠ S138) mutation to D: Increases catalytic activity.
- N214 (≠ S177) mutation to D: Increases catalytic activity.
- K224 (= K187) mutation to T: Reduces affinity for substrate and catalytic efficiency.
- K244 (≠ R207) mutation to E: Reduces affinity for substrate and catalytic efficiency.
- K262 (= K223) mutation to E: Has no effect on catalytic activity.
6uniA Human cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 12:428/435 of 6uniA
- active site: T248 (= T265), F374 (= F386), C381 (= C393)
- binding protoporphyrin ix containing fe: R79 (≠ N74), I92 (≠ L86), S93 (≠ M87), R104 (= R98), F241 (≠ I258), A244 (= A261), T248 (= T265), I308 (≠ V322), L312 (= L326), R314 (= R329), P373 (= P385), F374 (= F386), G375 (= G387), R379 (= R391), N380 (≠ R392), C381 (= C393), I382 (≠ L394), A387 (= A399)
- binding tert-butyl [(2S)-1-(1H-indol-3-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[2-(pyridin-3-yl)ethyl]amino}propan-2-yl]sulfanyl}propan-2-yl]carbamate: R79 (≠ N74), R80 (≠ K75), P81 (≠ L76), F82 (≠ A77), S93 (≠ M87), I94 (≠ L88), F195 (≠ Y210), F243 (= F260), A244 (= A261), T248 (= T265)
P24464 Cytochrome P450 4A12; CYPIVA12; CYPIVA8; Cytochrome P450-KP1; Cytochrome P450-PP1; EC 1.14.14.1 from Rattus norvegicus (Rat) (see paper)
27% identity, 75% coverage: 75:416/459 of query aligns to 119:478/508 of P24464
- E319 (≠ A261) binding covalent
- C455 (= C393) binding axial binding residue
Q02928 Cytochrome P450 4A11; 20-hydroxyeicosatetraenoic acid synthase; 20-HETE synthase; CYP4AII; CYPIVA11; Cytochrome P-450HK-omega; Cytochrome P450HL-omega; Fatty acid omega-hydroxylase; Lauric acid omega-hydroxylase; Long-chain fatty acid omega-monooxygenase; EC 1.14.14.1; EC 1.14.14.80 from Homo sapiens (Human) (see 8 papers)
25% identity, 90% coverage: 29:441/459 of query aligns to 76:504/519 of Q02928
- G130 (≠ S85) mutation to S: Loss of activity.
- E321 (≠ A261) binding covalent; mutation to A: Loss of covalent heme binding.
- S353 (= S293) to G: in dbSNP:rs3899049
- F434 (≠ E371) to S: risk factor for hypertension; significantly reduced arachidonic acid and lauric acid metabolizing activity; dbSNP:rs1126742
- C457 (= C393) binding axial binding residue
Sites not aligning to the query:
8ewlA Crystal structure of cyp3a4 bound to an inhibitor (see paper)
24% identity, 95% coverage: 5:439/459 of query aligns to 12:442/449 of 8ewlA
- binding protoporphyrin ix containing fe: R79 (≠ N74), I92 (≠ L86), S93 (≠ M87), W100 (≠ H94), R104 (= R98), A258 (= A261), T262 (= T265), I322 (≠ V322), L326 (= L326), R328 (= R329), P387 (= P385), F388 (= F386), G389 (= G387), R393 (= R391), N394 (≠ R392), C395 (= C393), I396 (≠ L394), G397 (= G395), A401 (= A399)
- binding {N-[([2,2'-bipyridin]-5-yl-kappa~2~N~1~,N~1'~)methyl]-3-(pyridin-4-yl)propanamide}bis[2-(quinolin-2-yl-kappaN)phenyl-kappaC~1~]iridium(1+): F82 (≠ A77), I94 (≠ L88), F187 (≠ L167), V208 (≠ I209), F209 (≠ Y210), A258 (= A261), T262 (= T265), L435 (≠ F431)
7sv2A Human cytochrome p450 (cyp) 3a5 ternary complex with azamulin (see paper)
24% identity, 94% coverage: 5:436/459 of query aligns to 16:455/465 of 7sv2A
- binding protoporphyrin ix containing fe: R83 (≠ G73), S97 (≠ M87), W104 (≠ H94), R108 (= R98), F115 (= F105), A275 (= A261), G276 (= G262), T279 (= T265), R345 (= R329), P403 (= P385), F404 (= F386), R409 (= R391), N410 (≠ R392), C411 (= C393), I412 (≠ L394), A417 (= A399)
- binding (3aS,4R,5S,6R,8R,9R,9aR,10R)-6-ethyl-5-hydroxy-4,6,9,10-tetramethyl-1-oxodecahydro-3a,9-propanocyclopenta[8]annulen-8-yl [(5-amino-1H-1,2,4-triazol-3-yl)sulfanyl]acetate: R83 (≠ G73), R84 (≠ N74), S97 (≠ M87), S97 (≠ M87), T185 (≠ W171), K186 (≠ L172), F188 (≠ M174), F198 (≠ R180), I271 (≠ T257), F274 (= F260), A275 (= A261), E344 (≠ P328), G450 (= G430), L451 (≠ F431)
Query Sequence
>WP_011320615.1 NCBI__GCF_000204075.1:WP_011320615.1
MLTQLPNPISVPSWWQLINWIADPIGFQKKYSQKYGDIFSMQLAGIGSFVILGEPQAIQE
IFTQDSRFDIGRGNKLAEPLIGRTSLMLMDGDRHRRERKLLMPPFHGEKLQAYAQQICLI
THQIASQWQIGQPFVARSAMQKLSLEVIIQIVFGLANGERYQQIKPLFTDWLNMTDSPLR
SSMLFLKSLQQDWGNRSPWGQMKYQQRCIYDLLQAEIEEKRTKENERRGDVLSLMMAARD
ENGQAMTDEELKDELLTILFAGHETTATTIAWAFYQIFRNVNVREKLQQELDSLGENPNP
MEIAQLPYLTAVCQETLRMYPVLPTLFPRITKSSINIAGYQLEPNTTLMASIYLIHYRED
LYPHPQQFRPERFIERQYSPSEYIPFGGGSRRCLGYALALLEIKLVIATVLSNYQLALAE
DKPIKVQRRGFTLAPEGGVRMIMTGKKSLRFEQSNKIFN
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