SitesBLAST
Comparing GFF2604 FitnessBrowser__Phaeo:GFF2604 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)
5khaA Structure of glutamine-dependent NAD+ synthetase from acinetobacter baumannii in complex with adenosine diphosphate (adp)
39% identity, 99% coverage: 5:548/552 of query aligns to 3:522/526 of 5khaA
- active site: D291 (= D296), E397 (= E402)
- binding adenosine-5'-diphosphate: Y273 (= Y278), F279 (= F284), N368 (= N373), R372 (= R377), M379 (= M384), S382 (= S387), N383 (= N388), C403 (≠ A408), T404 (= T409), Y494 (= Y520), K495 (= K521)
2e18A Crystal structure of project ph0182 from pyrococcus horikoshii ot3
35% identity, 46% coverage: 267:522/552 of query aligns to 5:242/256 of 2e18A
Sites not aligning to the query:
P9WJJ3 Glutamine-dependent NAD(+) synthetase; NAD(+) synthase [glutamine-hydrolyzing]; EC 6.3.5.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:519/679 of P9WJJ3
- E52 (= E45) mutation to A: Lack of glutamine-dependent activity. Retains 30% of ammonia-dependent activity.
- K121 (= K113) mutation to A: Lack of glutamine-dependent and ammonia-dependent activities.
- C176 (= C149) mutation to A: Lack of glutamine-dependent activity. Retains 90% of ammonia-dependent activity.
Sites not aligning to the query:
- 656 D→A: Causes a decrease in ammonia channel efficiency to 70% compared with wild-type enzyme.
6ofcB Crystal structure of m. Tuberculosis glutamine-dependent NAD+ synthetase complexed with sulfonamide derivative 1, pyrophosphate, and glutamine (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:509/669 of 6ofcB
- binding pyrophosphate 2-: S368 (= S292), G370 (= G294), S373 (= S297)
- binding 5'-O-[(pyridine-3-carbonyl)sulfamoyl]adenosine: R354 (≠ Y278), L358 (≠ T282), G366 (= G290), V367 (≠ L291), S368 (= S292), A398 (≠ M317), L399 (= L318), R452 (= R379), G465 (≠ E392), I466 (≠ M393), T470 (= T397), W480 (≠ Y407), S481 (≠ A408), T482 (= T409), T482 (= T409), Y483 (≠ I410), D487 (= D413), H491 (≠ G417)
Sites not aligning to the query:
O25096 NH(3)-dependent NAD(+) synthetase; EC 6.3.1.5 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
33% identity, 40% coverage: 264:486/552 of query aligns to 1:208/260 of O25096
- 31:38 (vs. 290:297, 88% identical) binding
- T132 (= T397) binding
- K161 (= K426) binding
1xngB Crystal structure of nh3-dependent NAD+ synthetase from helicobacter pylori (see paper)
33% identity, 40% coverage: 266:486/552 of query aligns to 1:206/262 of 1xngB
- active site: D35 (= D296), E135 (= E402)
- binding adenosine-5'-triphosphate: G29 (= G290), L30 (= L291), S31 (= S292), G33 (= G294), L34 (≠ V295), D35 (= D296), S36 (= S297), M56 (≠ L318), R112 (= R379), T130 (= T397), E135 (= E402), K159 (= K426), S181 (= S462)
- binding nicotinic acid adenine dinucleotide: R21 (≠ T282), F23 (= F284), N106 (= N373), Y117 (≠ M384), S120 (= S387), L121 (≠ N388), L126 (≠ M393), Y140 (= Y407), G141 (≠ A408), T142 (= T409), D146 (= D413), A150 (≠ G417), A182 (= A463)
Sites not aligning to the query:
3dlaA X-ray crystal structure of glutamine-dependent NAD+ synthetase from mycobacterium tuberculosis bound to naad+ and don (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 14:506/651 of 3dlaA
- binding nicotinic acid adenine dinucleotide: R355 (≠ Y278), L359 (≠ T282), G462 (≠ E392), E472 (= E402), W477 (≠ Y407), S478 (≠ A408), T479 (= T409), Y480 (≠ I410), D484 (= D413), H488 (≠ G417)
- binding 5-oxo-l-norleucine: Y128 (≠ A119), F131 (= F122), C177 (= C149), E178 (= E150), F181 (≠ W153)
Sites not aligning to the query:
6ofcC Crystal structure of m. Tuberculosis glutamine-dependent NAD+ synthetase complexed with sulfonamide derivative 1, pyrophosphate, and glutamine (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:515/665 of 6ofcC
- binding glutamine: Y58 (= Y51), K121 (= K113), P125 (= P117), F130 (= F122), A176 (= A158), E177 (= E159), F180 (vs. gap)
- binding 5'-O-[(pyridine-3-carbonyl)sulfamoyl]adenosine: R354 (≠ Y278), L358 (≠ T282), G366 (= G290), V367 (≠ L291), S368 (= S292), S373 (= S297), F397 (≠ V316), A398 (≠ M317), L399 (= L318), R458 (= R379), N467 (= N388), G471 (≠ E392), T476 (= T397), W486 (≠ Y407), S487 (≠ A408), T488 (= T409), Y489 (≠ I410), H497 (≠ G417)
Sites not aligning to the query:
3dlaB X-ray crystal structure of glutamine-dependent NAD+ synthetase from mycobacterium tuberculosis bound to naad+ and don (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:502/649 of 3dlaB
- binding nicotinic acid adenine dinucleotide: L358 (≠ T282), G458 (≠ E392), W473 (≠ Y407), S474 (≠ A408), T475 (= T409), D480 (= D413), H484 (≠ G417)
- binding 5-oxo-l-norleucine: C176 (= C149), F180 (≠ W153), S201 (≠ N173), S203 (= S175), R209 (≠ K181), Y230 (≠ N204)
Sites not aligning to the query:
3sytA Crystal structure of glutamine-dependent NAD+ synthetase from m. Tuberculosis bound to amp/ppi, NAD+, and glutamate (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:513/660 of 3sytA
- binding adenosine monophosphate: G366 (= G290), V367 (≠ L291), S368 (= S292), S373 (= S297), L399 (= L318), R456 (= R379), T474 (= T397)
- binding glutamic acid: Y127 (≠ A119), F180 (≠ W153), S203 (= S175), R209 (≠ K181)
- binding nicotinamide-adenine-dinucleotide: R354 (≠ Y278), L358 (≠ T282), N450 (= N373), N465 (= N388), G469 (≠ E392), E479 (= E402), W484 (≠ Y407), S485 (≠ A408), T486 (= T409), Y487 (≠ I410), D491 (= D413), H495 (≠ G417)
- binding pyrophosphate 2-: S368 (= S292), G370 (= G294), L371 (≠ V295), D372 (= D296), S373 (= S297)
Sites not aligning to the query:
3sytD Crystal structure of glutamine-dependent NAD+ synthetase from m. Tuberculosis bound to amp/ppi, NAD+, and glutamate (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:503/649 of 3sytD
- binding adenosine monophosphate: G366 (= G290), V367 (≠ L291), S368 (= S292), A398 (≠ M317), L399 (= L318), R446 (= R379)
- binding glutamic acid: Y127 (≠ A119), E177 (= E150), F180 (≠ W153), S203 (= S175)
- binding nicotinamide-adenine-dinucleotide: R354 (≠ Y278), L358 (≠ T282), N455 (= N388), G459 (≠ E392), E469 (= E402), W474 (≠ Y407), T476 (= T409), Y477 (≠ I410), D481 (= D413), H485 (≠ G417)
- binding pyrophosphate 2-: S368 (= S292), G370 (= G294), L371 (≠ V295), D372 (= D296), S373 (= S297)
Sites not aligning to the query:
3sezC Crystal structure of c176a mutant of glutamine-dependent NAD+ synthetase from m. Tuberculosis in complex with atp and naad+ (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:502/648 of 3sezC
- binding adenosine-5'-triphosphate: G366 (= G290), V367 (≠ L291), S368 (= S292), S373 (= S297), A398 (≠ M317), L399 (= L318), R445 (= R379), T463 (= T397)
- binding nicotinic acid adenine dinucleotide: L358 (≠ T282), N454 (= N388), G458 (≠ E392), E468 (= E402), W473 (≠ Y407), S474 (≠ A408), T475 (= T409), Y476 (≠ I410), D480 (= D413), H484 (≠ G417)
Sites not aligning to the query:
3seqD Crystal structure of c176a mutant of glutamine-dependent NAD+ synthetase from m. Tuberculosis in complex with ampcpp and naad+ (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 14:504/650 of 3seqD
- binding diphosphomethylphosphonic acid adenosyl ester: G367 (= G290), V368 (≠ L291), S369 (= S292), G371 (= G294), L372 (≠ V295), D373 (= D296), S374 (= S297), A399 (≠ M317), L400 (= L318), R447 (= R379), T465 (= T397)
- binding nicotinic acid adenine dinucleotide: R355 (≠ Y278), L359 (≠ T282), N456 (= N388), G460 (≠ E392), W475 (≠ Y407), S476 (≠ A408), T477 (= T409), Y478 (≠ I410), D482 (= D413), H486 (≠ G417)
Sites not aligning to the query:
3sezA Crystal structure of c176a mutant of glutamine-dependent NAD+ synthetase from m. Tuberculosis in complex with atp and naad+ (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 13:513/658 of 3sezA
- binding adenosine-5'-triphosphate: G366 (= G290), V367 (≠ L291), S368 (= S292), S373 (= S297), A398 (≠ M317), L399 (= L318), R456 (= R379), T474 (= T397)
- binding nicotinic acid adenine dinucleotide: R354 (≠ Y278), L358 (≠ T282), N465 (= N388), G469 (≠ E392), E479 (= E402), W484 (≠ Y407), S485 (≠ A408), T486 (= T409), Y487 (≠ I410), D491 (= D413), H495 (≠ G417)
Sites not aligning to the query:
3seqA Crystal structure of c176a mutant of glutamine-dependent NAD+ synthetase from m. Tuberculosis in complex with ampcpp and naad+ (see paper)
25% identity, 78% coverage: 6:435/552 of query aligns to 14:514/661 of 3seqA
- binding diphosphomethylphosphonic acid adenosyl ester: G367 (= G290), V368 (≠ L291), S369 (= S292), G371 (= G294), L372 (≠ V295), D373 (= D296), S374 (= S297), L400 (= L318), R457 (= R379), T475 (= T397)
- binding nicotinic acid adenine dinucleotide: R355 (≠ Y278), L359 (≠ T282), V447 (≠ L369), N466 (= N388), G470 (≠ E392), E480 (= E402), W485 (≠ Y407), T487 (= T409), Y488 (≠ I410), D492 (= D413), H496 (≠ G417)
Sites not aligning to the query:
3fiuA Structure of nmn synthetase from francisella tularensis (see paper)
30% identity, 36% coverage: 288:486/552 of query aligns to 28:207/238 of 3fiuA
- binding adenosine monophosphate: G30 (= G290), L31 (= L291), S32 (= S292), L56 (= L318), R113 (= R379), T131 (= T397), D147 (= D413), S182 (= S462)
- binding magnesium ion: D36 (= D296), E136 (= E402)
- binding pyrophosphate 2-: S32 (= S292), G34 (= G294), I35 (≠ V295), D36 (= D296), S37 (= S297), K160 (= K426), P181 (= P461), S182 (= S462)
Q6IA69 Glutamine-dependent NAD(+) synthetase; NAD(+) synthase [glutamine-hydrolyzing]; NAD(+) synthetase; EC 6.3.5.1 from Homo sapiens (Human) (see 4 papers)
22% identity, 77% coverage: 1:427/552 of query aligns to 1:545/706 of Q6IA69
- C49 (≠ T49) to R: in VCRL3; loss of protein expression
- V74 (≠ A78) to L: in dbSNP:rs2276360
- W132 (vs. gap) to L: in VCRL3; decreased protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity; dbSNP:rs189928649
- C175 (= C149) mutation to S: Eliminates glutamine-dependent NAD synthetase activity with the ammonia-dependent activity intact.
- Q204 (≠ Y177) to H: in dbSNP:rs7950441
Sites not aligning to the query:
- 573 A → T: in VCRL3; no effect on protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity; dbSNP:rs144139747
6ofbA Crystal structure of human glutamine-dependent NAD+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+ (see paper)
23% identity, 77% coverage: 4:427/552 of query aligns to 2:543/696 of 6ofbA
- binding adenosine monophosphate: P353 (≠ G290), L354 (= L291), S355 (= S292), M416 (≠ L318), R487 (= R379), C529 (≠ D413)
- binding nicotinic acid adenine dinucleotide: Q347 (≠ F284), R485 (= R377), Q496 (vs. gap), L508 (≠ E392), L509 (≠ M393), L524 (≠ A408), D533 (≠ G417)
- binding magnesium ion: V358 (= V295), D359 (= D296)
- binding pyrophosphate 2-: S355 (= S292), G357 (= G294), D359 (= D296), S360 (= S297)
Sites not aligning to the query:
2pzaA NAD+ synthetase from bacillus anthracis with amp + ppi and mg2+ (see paper)
28% identity, 37% coverage: 275:480/552 of query aligns to 30:237/279 of 2pzaA
- active site: D51 (= D296), E163 (= E402)
- binding adenosine monophosphate: G45 (= G290), I46 (≠ L291), S47 (= S292), S52 (= S297), R79 (≠ M317), L80 (= L318), Q85 (= Q325), R140 (= R379), T158 (= T397), E163 (= E402), D174 (= D413), T209 (≠ E448), A210 (≠ G449)
- binding magnesium ion: D51 (= D296), E163 (= E402)
- binding pyrophosphate 2-: S47 (= S292), G49 (= G294), D51 (= D296), S52 (= S297), K187 (= K426), P208 (= P447), T209 (≠ E448)
2pz8A NAD+ synthetase from bacillus anthracis with amp-cpp and mg2+ (see paper)
28% identity, 37% coverage: 275:480/552 of query aligns to 30:237/280 of 2pz8A
- active site: D51 (= D296), E163 (= E402)
- binding diphosphomethylphosphonic acid adenosyl ester: G45 (= G290), I46 (≠ L291), S47 (= S292), G49 (= G294), Q50 (≠ V295), D51 (= D296), S52 (= S297), R79 (≠ M317), L80 (= L318), Q85 (= Q325), R140 (= R379), T158 (= T397), P208 (= P447), T209 (≠ E448)
Query Sequence
>GFF2604 FitnessBrowser__Phaeo:GFF2604
MADRFRVTLAQLNPTVGDLAGNANKAREAWAAGRDAGADLVALPEMFITGYNTQDLVQKP
VFHQAAIAEVERLAADCADGPALAVGSPWVADGKLFNAYLILKGGKITTQVLKHHLPNAT
VFDEVRIFDAGPLGGPYAVGNTRIGSPICEDGWYEDVAETLAETGAEFLLIPNGSPYFRN
KMDVRFNHMVARAVETDLPVIYLNMVGGQDDQVFDGGSFVLNPGGALALQMPVFDEAIQH
LDLERTAEGWRAVEGPKASLPDEWEQDYHVMTLSLRDYMRKTGFKKVLLGLSGGVDSAIV
ATIAVDALGAENVRCVMLPSEYTSQESLDDAEAVAKALGVHYDYVPIAEGRAAITNTLAP
LFAGLDEGLTEENIQSRLRGLLLMAMSNKFGEMLLTTGNKSEVAVGYATIYGDMAGGYNP
IKDLYKTRVFETCRWRNDNHRDWMMGPEGEVIRPNVIDKPPSAELRDDQKDSDSLPDYPE
LDALLEILVDRDGSIADCVAAGFSRENAKRVEHLIYISEYKRFQSAPGARLTPRAFWLDR
RYPIVNRWRDPS
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