SitesBLAST
Comparing WP_078715801.1 NCBI__GCF_900167125.1:WP_078715801.1 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)
2fuvA Phosphoglucomutase from salmonella typhimurium.
60% identity, 98% coverage: 7:545/549 of query aligns to 5:543/545 of 2fuvA
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
26% identity, 88% coverage: 37:521/549 of query aligns to 9:510/553 of 7pjcB
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
26% identity, 87% coverage: 72:547/549 of query aligns to 19:550/565 of 4qg5A
Q9VUY9 Phosphoglucomutase 1; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
26% identity, 71% coverage: 44:434/549 of query aligns to 19:428/560 of Q9VUY9
- K28 (vs. gap) natural variant: K -> N
- T36 (≠ N58) natural variant: T -> M
- S116 (= S148) modified: Phosphoserine
- E351 (≠ T367) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
- 17 natural variant: K -> Q
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
25% identity, 87% coverage: 43:522/549 of query aligns to 5:433/455 of 1wqaA
- active site: R11 (= R49), S101 (= S148), H102 (= H149), K111 (= K158), D243 (= D306), D245 (= D308), D247 (= D310), R248 (= R311), G330 (= G396), R340 (≠ K411)
- binding magnesium ion: S101 (= S148), D243 (= D306), D245 (= D308), D247 (= D310)
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
26% identity, 67% coverage: 82:450/549 of query aligns to 70:442/573 of 6snoA
- active site: S130 (= S148), H131 (= H149), K143 (= K158), D301 (= D306), D303 (= D308), D305 (= D310), R306 (= R311), G393 (= G396)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S148), E389 (= E392), S391 (= S394)
- binding zinc ion: S130 (= S148), D301 (= D306), D303 (= D308), D305 (= D310)
Sites not aligning to the query:
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
26% identity, 67% coverage: 82:450/549 of query aligns to 70:442/566 of 6snqA
- active site: S130 (= S148), H131 (= H149), K143 (= K158), D301 (= D306), D303 (= D308), D305 (= D310), R306 (= R311), G393 (= G396)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S148), T370 (≠ V373), G371 (= G374), E389 (= E392), S391 (= S394)
- binding zinc ion: S130 (= S148), D301 (= D306), D303 (= D308), D305 (= D310)
Sites not aligning to the query:
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
26% identity, 67% coverage: 82:450/549 of query aligns to 56:428/561 of 3pmgA
- active site: S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G396), K388 (= K411)
- binding magnesium ion: S116 (= S148), D287 (= D306), D289 (= D308), D291 (= D310)
Sites not aligning to the query:
1c4gA Phosphoglucomutase vanadate based transition state analog complex
26% identity, 67% coverage: 82:450/549 of query aligns to 56:428/561 of 1c4gA
- active site: S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G396), K388 (= K411)
- binding cobalt (ii) ion: S116 (= S148), D287 (= D306), D289 (= D308), D291 (= D310)
- binding alpha-d-glucose-1-phosphate-6-vanadate: S116 (= S148), H117 (= H149), K129 (= K158), R292 (= R311), E375 (= E392), S377 (= S394), K388 (= K411)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
26% identity, 67% coverage: 82:450/549 of query aligns to 56:428/561 of 1c47A
- active site: S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G396), K388 (= K411)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S116 (= S148), D291 (= D310), R292 (= R311), E375 (= E392), K388 (= K411)
Sites not aligning to the query:
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
26% identity, 67% coverage: 82:450/549 of query aligns to 57:429/562 of P00949
- S117 (= S148) active site, Phosphoserine intermediate; binding alpha-D-glucose 1,6-bisphosphate; binding via phosphate group; modified: Phosphoserine
- D288 (= D306) binding Mg(2+)
- D290 (= D308) binding Mg(2+)
- D292 (= D310) binding alpha-D-glucose 1,6-bisphosphate; binding Mg(2+)
- R293 (= R311) binding alpha-D-glucose 1,6-bisphosphate
- T357 (≠ V373) binding alpha-D-glucose 1,6-bisphosphate
- E376 (= E392) binding alpha-D-glucose 1,6-bisphosphate
- S378 (= S394) binding alpha-D-glucose 1,6-bisphosphate
- K389 (= K411) binding alpha-D-glucose 1,6-bisphosphate
Sites not aligning to the query:
- 23 binding alpha-D-glucose 1,6-bisphosphate
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 63% coverage: 105:450/549 of query aligns to 76:424/554 of O74374
- T111 (= T146) modified: Phosphothreonine
- S113 (= S148) modified: Phosphoserine
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
25% identity, 74% coverage: 44:450/549 of query aligns to 18:429/562 of P36871
- T19 (= T45) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ G60) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ L63) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D87) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ E93) to M: in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs200390982
- T115 (= T146) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S148) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (vs. gap) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ G234) to C: in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs1126728
- D263 (= D282) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D306) binding Mg(2+)
- D290 (= D308) binding Mg(2+)
- G291 (≠ F309) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D310) binding Mg(2+)
- G330 (= G346) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E393) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D410) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ F441) to H: in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs11208257
Sites not aligning to the query:
- 467 modified: Phosphothreonine; by PAK1
- 516 L → P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
24% identity, 74% coverage: 44:450/549 of query aligns to 19:430/559 of 5jn5A
- active site: R24 (= R49), S118 (= S148), H119 (= H149), K131 (= K158), D289 (vs. gap), D291 (vs. gap), D293 (= D310), R294 (= R311), G381 (= G396), K390 (= K411)
- binding calcium ion: S118 (= S148), D289 (vs. gap), D291 (vs. gap), D293 (= D310)
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
23% identity, 79% coverage: 31:461/549 of query aligns to 9:448/572 of 6y8yA
Sites not aligning to the query:
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
26% identity, 91% coverage: 19:519/549 of query aligns to 30:546/581 of P18159
- G162 (= G164) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ S241) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G396) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D412) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
25% identity, 70% coverage: 44:426/549 of query aligns to 19:405/499 of 7s0wB
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
25% identity, 74% coverage: 44:450/549 of query aligns to 20:449/570 of 1kfiA
- active site: S124 (= S148), H125 (= H149), D306 (= D306), D308 (= D308), D310 (= D310), R311 (= R311), K403 (= K411)
- binding sulfate ion: S124 (= S148), H125 (= H149), D310 (= D310), R311 (= R311)
- binding zinc ion: D306 (= D306), D308 (= D308), D310 (= D310)
Sites not aligning to the query:
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
25% identity, 74% coverage: 44:450/549 of query aligns to 21:450/571 of 1kfqA
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
23% identity, 82% coverage: 44:491/549 of query aligns to 20:472/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T45), R25 (= R49), S117 (= S148), H118 (= H149), K130 (= K158), D286 (= D310), R287 (= R311), T350 (≠ V373), E369 (= E392), S371 (= S394), K382 (≠ D403)
- binding magnesium ion: S117 (= S148), D282 (= D306), D284 (= D308), D286 (= D310)
Sites not aligning to the query:
Query Sequence
>WP_078715801.1 NCBI__GCF_900167125.1:WP_078715801.1
MTDPQPRPGTPAPASMLVDPEALIQAYYTLSPHPDIPGQAVSFGTSGHRGRALEGGFNEG
HILAVTQALCEHRARAGVNGPLFLGMDTHALSEPAQRTAIEVLAGNGVHVFIQQDNGHTP
TPVISHAILSWNRGGKGSLADGVVVTPSHNPPSDGGFKYNPPSGGPAGPNITGPVQERAN
QILRDGLHEVRRLPYERAIQSELVHLHDYVRPYVLDLENVVDMETIRSAGLKIGADPLGG
SGLAYFDPIADLYGLDIEVVNRSTDPRFAFMPLDHDLKIRMDCSSAHAMAGLIRLKDQFD
VAFGNDPDFDRHGIVTSQGLMNPNHFLAVACEHLFQTRTGWSRAAGLGKTLVSSSMLDRV
AAHLDRTLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRKDGTAWSTDKDGIIMDLLA
CEITATGNNPAQRYTSLTERFGEPVYARIDAPASPDQKAAFKQLTPDMVTAEHLAGEPIL
ARLTRAPGNNAPIGGLKVTTKNGWFAARPSGTEDIYKIYAESFLGAEHLADIQDEAKAIV
NAAFQATGA
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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