SitesBLAST
Comparing WP_073040638.1 NCBI__GCF_900129305.1:WP_073040638.1 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)
P08237 ATP-dependent 6-phosphofructokinase, muscle type; ATP-PFK; PFK-M; 6-phosphofructokinase type A; Phosphofructo-1-kinase isozyme A; PFK-A; Phosphohexokinase; EC 2.7.1.11 from Homo sapiens (Human) (see 6 papers)
42% identity, 99% coverage: 3:731/738 of query aligns to 16:755/780 of P08237
- R39 (= R26) to P: in GSD7; Italian; dbSNP:rs121918193
- G57 (= G44) to V: in GSD7; Italian
- R100 (≠ K87) to Q: in dbSNP:rs2228500
- S180 (≠ T166) to C: in GSD7; Italian
- G209 (= G195) to D: in GSD7; loss of activity shown by complementation assays in yeast; dbSNP:rs767265360
- D309 (= D295) to G: in GSD7; Spanish; complete loss of enzyme activity; dbSNP:rs1169383137
- D543 (= D530) to A: in GSD7; Italian; dbSNP:rs121918194
- K557 (≠ R544) modified: N6-(2-hydroxyisobutyryl)lysine
- D591 (≠ E577) to A: in GSD7; Italian
- W686 (≠ E672) to C: in GSD7; Japanese; dbSNP:rs121918196
- R696 (vs. gap) to H: in dbSNP:rs41291971
P00511 ATP-dependent 6-phosphofructokinase, muscle type; ATP-PFK; PFK-M; 6-phosphofructokinase type A; Phosphofructo-1-kinase isozyme A; PFK-A; Phosphohexokinase; EC 2.7.1.11 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
42% identity, 99% coverage: 3:731/738 of query aligns to 16:755/780 of P00511
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 775 modified: Phosphoserine; by PKA
3o8lA Structure of phosphofructokinase from rabbit skeletal muscle (see paper)
42% identity, 99% coverage: 3:731/738 of query aligns to 8:747/748 of 3o8lA
- active site: G17 (= G12), R80 (= R75), D111 (= D106), S156 (= S150), D158 (= D152), D160 (= D154), R202 (= R196)
- binding adenosine-5'-diphosphate: D165 (= D159), M166 (= M160), F300 (= F294), F530 (= F525), F663 (= F657)
- binding adenosine-5'-triphosphate: G16 (= G11), Y47 (= Y42), R80 (= R75), C81 (≠ S76), R85 (= R80), G110 (= G105), G112 (= G107), S113 (= S108), T115 (≠ M110), G116 (= G111), W219 (= W213), H234 (≠ K228), R238 (≠ A232), Y377 (≠ V371), H382 (≠ R376), I383 (= I377)
- binding phosphate ion: R416 (= R410), G449 (≠ T443), G450 (≠ S444), R463 (= R457), S522 (≠ D517), N524 (= N519), R727 (≠ G711)
4xyjF Crystal structure of human phosphofructokinase-1 in complex with atp and mg, northeast structural genomics consortium target hr9275 (see paper)
42% identity, 100% coverage: 3:737/738 of query aligns to 11:751/761 of 4xyjF
- active site: G20 (= G12), R83 (= R75), C84 (≠ S76), D114 (= D106), G158 (= G149), S159 (= S150), D161 (= D152), D163 (= D154), R205 (= R196)
- binding adenosine-5'-triphosphate: G20 (= G12), Y50 (= Y42), R83 (= R75), C84 (≠ S76), F87 (= F79), R88 (= R80), G113 (= G105), D114 (= D106), G115 (= G107), S116 (= S108), G119 (= G111), S159 (= S150)
- binding cobalt (ii) ion: E475 (= E466), K510 (≠ S501), H511 (≠ L502)
- binding magnesium ion: G19 (= G11), G20 (= G12), G112 (= G104), D114 (= D106), G158 (= G149), D163 (= D154), R205 (= R196)
- binding phosphate ion: R30 (= R22), R34 (= R26), S69 (≠ G61), S70 (≠ G62), G219 (= G210), K250 (≠ R241), R416 (≠ S406), R420 (= R410), G453 (≠ T443), G454 (≠ S444)
4xyjA Crystal structure of human phosphofructokinase-1 in complex with atp and mg, northeast structural genomics consortium target hr9275 (see paper)
42% identity, 100% coverage: 3:737/738 of query aligns to 13:758/768 of 4xyjA
- active site: G22 (= G12), R85 (= R75), C86 (≠ S76), D116 (= D106), G160 (= G149), S161 (= S150), D163 (= D152), D165 (= D154), R207 (= R196)
- binding adenosine-5'-triphosphate: G21 (= G11), G22 (= G12), Y52 (= Y42), C86 (≠ S76), F89 (= F79), R90 (= R80), G115 (= G105), D116 (= D106), G117 (= G107), S118 (= S108), G121 (= G111), S161 (= S150), R207 (= R196)
- binding magnesium ion: G21 (= G11), G22 (= G12), D116 (= D106), D165 (= D154)
- binding phosphate ion: R32 (= R22), R36 (= R26), S72 (≠ G62), G221 (= G210), K252 (≠ R241), R418 (≠ S406), G456 (≠ S444)
Q01813 ATP-dependent 6-phosphofructokinase, platelet type; ATP-PFK; PFK-P; 6-phosphofructokinase type C; Phosphofructo-1-kinase isozyme C; PFK-C; Phosphohexokinase; EC 2.7.1.11 from Homo sapiens (Human) (see paper)
42% identity, 100% coverage: 3:737/738 of query aligns to 25:770/784 of Q01813
- S386 (= S363) modified: Phosphoserine; mutation to A: Decreased interaction with ATG4B.
P47859 ATP-dependent 6-phosphofructokinase, platelet type; ATP-PFK; PFK-P; 6-phosphofructokinase type C; Phosphofructo-1-kinase isozyme C; PFK-C; Phosphohexokinase; EC 2.7.1.11 from Oryctolagus cuniculus (Rabbit) (see paper)
42% identity, 100% coverage: 3:737/738 of query aligns to 25:770/791 of P47859
Sites not aligning to the query:
- 12 modified: Phosphoserine; by PKA
4rh3A Amppcp-bound structure of human platelet phosphofructokinase in an r- state, crystal form ii (see paper)
43% identity, 98% coverage: 5:729/738 of query aligns to 3:731/731 of 4rh3A
- active site: G10 (= G12), R73 (= R75), C74 (≠ S76), D104 (= D106), G148 (= G149), S149 (= S150), D151 (= D152), D153 (= D154), R195 (= R196)
- binding phosphomethylphosphonic acid adenylate ester: G9 (= G11), R73 (= R75), C74 (≠ S76), F77 (= F79), R78 (= R80), G103 (= G105), D104 (= D106), G105 (= G107), S106 (= S108), G109 (= G111)
- binding phosphate ion: K240 (≠ R241), R406 (≠ S406), R410 (= R410), G443 (≠ T443), G444 (≠ S444), R457 (= R457), R552 (= R552), R641 (= R641), H647 (= H647)
8w2hA Human liver phosphofructokinase-1 in the t-state conformation (see paper)
41% identity, 99% coverage: 3:731/738 of query aligns to 6:744/761 of 8w2hA
- binding adenosine-5'-triphosphate: G14 (= G11), G15 (= G12), Y45 (= Y42), R78 (= R75), C79 (≠ S76), F82 (= F79), G108 (= G105), D109 (= D106), G110 (= G107), S111 (= S108), G114 (= G111), I117 (≠ V114), Q187 (≠ A183), W217 (= W213), L218 (≠ V214), W372 (≠ L368), Y375 (≠ V371), K376 (= K372), K382 (≠ E378), R409 (≠ S406), R413 (= R410), A446 (≠ T443), G447 (≠ S444), R451 (= R448)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R460 (= R457), T517 (= T515), S519 (≠ D517), R555 (= R552), M562 (= M559), R644 (= R641), H650 (= H647), R724 (≠ G711)
7lw1A Human phosphofructokinase-1 liver type bound to activator na-11 (see paper)
41% identity, 99% coverage: 3:731/738 of query aligns to 6:744/744 of 7lw1A
- binding adenosine-5'-diphosphate: R78 (= R75), C79 (≠ S76), T83 (≠ R80), G108 (= G105), G110 (= G107), S111 (= S108), G114 (= G111), I117 (≠ V114)
- binding 6-O-phosphono-beta-D-fructofuranose: I155 (= I151), D156 (= D152), R191 (= R187), M198 (= M194), R200 (= R196), E254 (= E250), R282 (= R278), H288 (= H284), R291 (= R287)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: A399 (= A396), R460 (= R457), S519 (≠ D517), R555 (= R552), M562 (= M559), E618 (= E615), R644 (= R641), H650 (= H647), R724 (≠ G711)
- binding N-{(11S)-2-[2-(5-hydroxypent-1-yn-1-yl)phenyl]-4H,10H-pyrazolo[5,1-c][1,4]benzoxazepin-7-yl}acetamide: M164 (= M160), F298 (= F294), I301 (= I297), K305 (≠ R301), N331 (= N327), F527 (= F525), D532 (= D530), V535 (≠ L533), Y568 (≠ F565), F660 (= F657), W730 (= W717), L734 (= L721)
4xykA Crystal structure of human phosphofructokinase-1 in complex with adp, northeast structural genomics consortium target hr9275 (see paper)
42% identity, 99% coverage: 3:730/738 of query aligns to 9:737/737 of 4xykA
- active site: G18 (= G12), R81 (= R75), C82 (≠ S76), D112 (= D106), G156 (= G149), S157 (= S150), D159 (= D152), D161 (= D154), R203 (= R196)
- binding adenosine-5'-diphosphate: Y48 (= Y42), R81 (= R75), C82 (≠ S76), R86 (= R80), G111 (= G105), D112 (= D106), G113 (= G107), S114 (= S108)
- binding phosphate ion: R28 (= R22), R32 (= R26), S67 (≠ G61), K248 (≠ R241), R414 (≠ S406), R418 (= R410), G451 (≠ T443), G452 (≠ S444)
P17858 ATP-dependent 6-phosphofructokinase, liver type; ATP-PFK; PFK-L; 6-phosphofructokinase type B; Phosphofructo-1-kinase isozyme B; PFK-B; Phosphohexokinase; EC 2.7.1.11 from Homo sapiens (Human) (see 3 papers)
41% identity, 99% coverage: 3:731/738 of query aligns to 16:754/780 of P17858
- G81 (= G68) natural variant: G -> A
- R151 (= R137) to W: in dbSNP:rs755851304
- T527 (= T515) mutation to A: Does not affect GlcNAcylation.
- S529 (≠ D517) modified: carbohydrate, O-linked (GlcNAc) serine; mutation to A: Prevents GlcNAcylation and enhance enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
O42938 ATP-dependent 6-phosphofructokinase; ATP-PFK; Phosphofructokinase; Phosphohexokinase; EC 2.7.1.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 99% coverage: 3:729/738 of query aligns to 195:936/942 of O42938
- S600 (≠ T403) modified: Phosphoserine
- T602 (≠ V405) modified: Phosphothreonine
Sites not aligning to the query:
- 43 modified: Phosphoserine
- 45 modified: Phosphoserine
- 85 modified: Phosphoserine
- 160 modified: Phosphoserine
- 163 modified: Phosphoserine
- 167 modified: Phosphoserine
- 171 modified: Phosphoserine
- 175 modified: Phosphothreonine
4xz2A Human platelet phosphofructokinase in an r-state in complex with adp and f6p, crystal form i (see paper)
41% identity, 98% coverage: 5:729/738 of query aligns to 3:708/708 of 4xz2A
- active site: G10 (= G12), D88 (= D106), G132 (= G149), S133 (= S150), R171 (= R196)
- binding 6-O-phosphono-beta-D-fructofuranose: R162 (= R187), R253 (= R278)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: A372 (= A396), R433 (= R457), V491 (≠ I516), S492 (≠ D517), M535 (= M559), E591 (= E615), H623 (= H647), Q626 (≠ R650)
- binding phosphate ion: G185 (= G210), K216 (≠ R241), R382 (≠ S406), R386 (= R410), G419 (≠ T443), G420 (≠ S444)
Q8TGA0 ATP-dependent 6-phosphofructokinase subunit beta; ATP-dependent 6-phosphofructokinase 2; ATP-PFK 2; Phosphofructokinase 2; Phosphohexokinase 2; EC 2.7.1.11 from Komagataella pastoris (Yeast) (Pichia pastoris) (see 2 papers)
39% identity, 96% coverage: 3:714/738 of query aligns to 182:917/941 of Q8TGA0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3opyB Crystal structure of pichia pastoris phosphofructokinase in the t- state (see paper)
38% identity, 98% coverage: 3:727/738 of query aligns to 138:874/884 of 3opyB
- active site: G147 (= G12), R211 (= R75), D242 (= D106), S279 (= S150), D281 (= D152), D283 (= D154), R324 (= R196)
- binding adenosine-5'-triphosphate: Y341 (≠ W213), I342 (≠ V214), K347 (≠ E219), S350 (≠ D222), S351 (≠ L223), R352 (= R224), Q357 (≠ K228), I361 (≠ A232), F500 (≠ L370), I501 (≠ V371), N504 (≠ L374), S505 (≠ T375)
Q92448 ATP-dependent 6-phosphofructokinase subunit alpha; ATP-dependent 6-phosphofructokinase 1; ATP-PFK 1; Phosphofructokinase 1; Glucose-induced selective autophagy 1 protein; Phosphohexokinase 1; EC 2.7.1.11 from Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) (see paper)
41% identity, 90% coverage: 3:665/738 of query aligns to 211:882/989 of Q92448
- D361 (= D152) mutation to S: Abolishes catalytic activity, but not the ability to modulate glucose-induced microautophagy of peroxisomes.
P16861 ATP-dependent 6-phosphofructokinase subunit alpha; ATP-dependent 6-phosphofructokinase; ATP-PFK; Phosphofructokinase 1; Phosphohexokinase; EC 2.7.1.11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
41% identity, 90% coverage: 3:665/738 of query aligns to 206:877/987 of P16861
- D309 (= D106) mutation to T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta.
- SID 354:356 (= SID 150:152) binding beta-D-fructose 6-phosphate
- D356 (= D152) mutation to S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta.
- R391 (= R187) binding beta-D-fructose 6-phosphate
- MGR 398:400 (= MGR 194:196) binding beta-D-fructose 6-phosphate
- R447 (≠ P242) mutation to S: Reduces maximal activity of the holoenzyme by less than 25%.
- E455 (= E250) binding beta-D-fructose 6-phosphate
- K482 (≠ R278) binding beta-D-fructose 6-phosphate
- H488 (= H284) mutation to S: Increases the KM for fructose 6-phosphate 20 fold.
- HVQR 488:491 (= HVQR 284:287) binding beta-D-fructose 6-phosphate
- R665 (= R457) binding beta-D-fructose 2,6-bisphosphate
- TVSNN 722:726 (≠ TIDNN 515:519) binding beta-D-fructose 2,6-bisphosphate
- S724 (≠ D517) mutation to D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta.
- P728 (= P521) mutation to L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition.
- R760 (= R552) binding beta-D-fructose 2,6-bisphosphate
- QGG 767:769 (≠ MGR 559:561) binding beta-D-fructose 2,6-bisphosphate
- E827 (= E615) binding beta-D-fructose 2,6-bisphosphate
- R853 (= R641) binding beta-D-fructose 2,6-bisphosphate
- H859 (= H647) mutation to S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta.
- HVQQ 859:862 (≠ HLQR 647:650) binding beta-D-fructose 2,6-bisphosphate
Sites not aligning to the query:
- 952 binding beta-D-fructose 2,6-bisphosphate
3o8oE Structure of phosphofructokinase from saccharomyces cerevisiae (see paper)
38% identity, 99% coverage: 3:729/738 of query aligns to 4:742/752 of 3o8oE
- active site: G13 (= G12), R76 (= R75), D107 (= D106), S152 (= S150), D154 (= D152), D156 (= D154), R198 (= R196)
- binding 6-O-phosphono-beta-D-fructofuranose: D154 (= D152), R189 (= R187), M196 (= M194), R198 (= R196), E253 (= E250), K280 (≠ R278), H286 (= H284), R289 (= R287)
- binding 2,6-di-O-phosphono-beta-D-fructofuranose: R463 (= R457), S522 (≠ D517), Q565 (≠ M559), G567 (≠ R561), E625 (= E615), H657 (= H647), R724 (≠ G711)
P16862 ATP-dependent 6-phosphofructokinase subunit beta; ATP-dependent 6-phosphofructokinase; ATP-PFK; Phosphofructokinase 2; Phosphohexokinase; EC 2.7.1.11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 5 papers)
39% identity, 90% coverage: 3:669/738 of query aligns to 197:875/959 of P16862
- D301 (= D106) mutation to T: Reduces maximal activity of the holoenzyme by 30%.
- SID 346:348 (= SID 150:152) binding beta-D-fructose 6-phosphate
- D348 (= D152) mutation to S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'T-309' or 'S-356' in subunit alpha.
- R383 (= R187) binding beta-D-fructose 6-phosphate
- MGR 390:392 (= MGR 194:196) binding beta-D-fructose 6-phosphate
- R439 (≠ P242) mutation to V: Reduces maximal activity of the holoenzyme by less than 25%.
- E447 (= E250) binding beta-D-fructose 6-phosphate
- R475 (= R278) binding beta-D-fructose 6-phosphate
- H481 (= H284) mutation to S: Increases the KM for fructose 6-phosphate 50 fold.
- HVQR 481:484 (= HVQR 284:287) binding beta-D-fructose 6-phosphate
- R658 (= R457) binding beta-D-fructose 2,6-bisphosphate
- TLSNN 716:720 (≠ TIDNN 515:519) binding beta-D-fructose 2,6-bisphosphate
- S718 (≠ D517) mutation to D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-724' in subunit alpha.
- P722 (= P521) mutation to L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition.
- QGG 761:763 (≠ MGR 559:561) binding beta-D-fructose 2,6-bisphosphate
- H853 (= H647) mutation to S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-859' in subunit alpha.
- HVQQ 853:856 (≠ HLQR 647:650) binding beta-D-fructose 2,6-bisphosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 935 binding beta-D-fructose 2,6-bisphosphate
Query Sequence
>WP_073040638.1 NCBI__GCF_900129305.1:WP_073040638.1
MVRTVAVMTSGGDAPGMNAGVRAVVRRALDCGLEVYGIHNGYEGLVSGGDAIRPLGWNDV
GGILPRGGTFLGTARSERFRTVEGRRKAVENLCRRGVQALVVIGGDGSLMGARVLAEEWV
THCAELRRQASEDVCARMPDRLHVVGLPGSIDNDLYGTDMSIGADTALNHIVHAIDDLTS
TAASHQRTFIVETMGRHCGYLALMGALGGGASWVLVPEEELDLRWHQKMSRAIERARAIG
RPHQMVVVAEGARHPDGLPIRTEELKKILAERLGIDVRVTVLGHVQRGGPPSAFDRILAT
RLGVAAVDLLLSASEEPLCHMLGLQKNRVTATPLSEVVEKSRAVGSHIDQGNYREAQKLR
GESFARTLELVKTLTRIEPASSPKGDGCVAILTGGADAPGMNTAVSIAARCLLNEGYAVV
GVRDAFRGLIAGDFQELEWNELTSWVNRPGSELGTARHDVNGRDLERMAQNIRERNIRGL
IAIGGLGTYLNAARLAAAAESLPELALPMVLVPATIDNNLPCTEFTIGCDTALNNIVQAI
DKIRHTAGANRRAFVVEVMGRQSGFLALAGALASGAEKAYLPEKGICLAELNRDVAALQE
SFRCGKRMVIFLRNENASRHYTTDFIARLLEEESRGLYQVRTAILGHLQRGGAPTAFDRI
LACRMGSAAAREMSLLLEQGRAEAVALGLRGRGVEAVPFREALEEMDLETGRPRGQWFLE
LTSVAEILARHAPSCTVE
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