PHSM_ECOLI
ID PHSM_ECOLI Reviewed; 797 AA.
AC P00490; Q2M782; Q9R783;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 7.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Maltodextrin phosphorylase;
DE EC=2.4.1.1;
GN Name=malP; OrderedLocusNames=b3417, JW5689;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3037809; DOI=10.1515/znc-1987-0411;
RA Palm D., Goerl R., Weidinger G., Zeier R., Fischer B., Schinzel R.;
RT "E. coli maltodextrin phosphorylase: primary structure and deletion mapping
RT of the C-terminal site.";
RL Z. Naturforsch. C 42:394-400(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION TO 701.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-688.
RX PubMed=3155826; DOI=10.1038/313500a0;
RA Palm D., Goerl R., Burger K.J.;
RT "Evolution of catalytic and regulatory sites in phosphorylases.";
RL Nature 313:500-502(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-797.
RX PubMed=2845225; DOI=10.1111/j.1365-2958.1988.tb00053.x;
RA Pugsley A.P., Dubreuil C.;
RT "Molecular characterization of malQ, the structural gene for the
RT Escherichia coli enzyme amylomaltase.";
RL Mol. Microbiol. 2:473-479(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=6283313; DOI=10.1007/bf00333795;
RA Debarbouille M., Cossart P., Raibaud O.;
RT "A DNA sequence containing the control sites for gene malT and for the
RT malPQ operon.";
RL Mol. Gen. Genet. 185:88-92(1982).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RX PubMed=6339728; DOI=10.1016/0022-2836(83)90065-7;
RA Raibaud O., Debarbouille M., Schwartz M.;
RT "Use of deletions created in vitro to map transcriptional regulatory
RT signals in the malA region of Escherichia coli.";
RL J. Mol. Biol. 163:395-408(1983).
RN [9]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=6986282; DOI=10.1016/0014-5793(80)81311-1;
RA Schiltz E., Palm D., Klein H.W.;
RT "N-terminal sequences of Escherichia coli and potato phosphorylase.";
RL FEBS Lett. 109:59-62(1980).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9009262; DOI=10.1093/emboj/16.1.1;
RA Watson K.A., Schinzel R., Palm D., Johnson L.N.;
RT "The crystal structure of Escherichia coli maltodextrin phosphorylase
RT provides an explanation for the activity without control in this basic
RT archetype of a phosphorylase.";
RL EMBO J. 16:1-14(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS).
RX PubMed=10220320; DOI=10.1021/bi9828573;
RA O'Reilly M., Watson K.A., Johnson L.N.;
RT "The crystal structure of the Escherichia coli maltodextrin phosphorylase-
RT acarbose complex.";
RL Biochemistry 38:5337-5345(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10469642; DOI=10.1093/emboj/18.17.4619;
RA Watson K.A., McCleverty C., Geremia S., Cottaz S., Driguez H.,
RA Johnson L.N.;
RT "Phosphorylase recognition and phosphorolysis of its oligosaccharide
RT substrate: answers to a long outstanding question.";
RL EMBO J. 18:4619-4632(1999).
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; X06791; CAA29949.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAT48180.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77874.1; -; Genomic_DNA.
DR EMBL; X02003; CAA26035.1; -; Genomic_DNA.
DR EMBL; M32793; AAA24105.1; -; Genomic_DNA.
DR EMBL; M24342; AAA24108.1; -; Genomic_DNA.
DR EMBL; V00304; CAA23584.1; -; Genomic_DNA.
DR PIR; D65137; PHECGM.
DR RefSeq; WP_000081909.1; NZ_STEB01000004.1.
DR RefSeq; YP_026218.1; NC_000913.3.
DR PDB; 1AHP; X-ray; 3.00 A; A/B=1-795.
DR PDB; 1E4O; X-ray; 2.90 A; A/B=2-797.
DR PDB; 1L5V; X-ray; 2.00 A; A/B=2-797.
DR PDB; 1L5W; X-ray; 1.80 A; A/B=2-797.
DR PDB; 1L6I; X-ray; 2.20 A; A/B=2-797.
DR PDB; 1QM5; X-ray; 2.00 A; A/B=2-797.
DR PDB; 2ASV; X-ray; 1.95 A; A/B=2-797.
DR PDB; 2AV6; X-ray; 2.01 A; A/B=2-797.
DR PDB; 2AW3; X-ray; 2.20 A; A/B=2-797.
DR PDB; 2AZD; X-ray; 2.16 A; A/B=2-797.
DR PDB; 2ECP; X-ray; 2.95 A; A/B=2-795.
DR PDBsum; 1AHP; -.
DR PDBsum; 1E4O; -.
DR PDBsum; 1L5V; -.
DR PDBsum; 1L5W; -.
DR PDBsum; 1L6I; -.
DR PDBsum; 1QM5; -.
DR PDBsum; 2ASV; -.
DR PDBsum; 2AV6; -.
DR PDBsum; 2AW3; -.
DR PDBsum; 2AZD; -.
DR PDBsum; 2ECP; -.
DR AlphaFoldDB; P00490; -.
DR SMR; P00490; -.
DR BioGRID; 4259324; 12.
DR DIP; DIP-10146N; -.
DR IntAct; P00490; 28.
DR STRING; 511145.b3417; -.
DR DrugBank; DB02843; alpha-D-glucose-1-phosphate.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03323; Maltose.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P00490; -.
DR jPOST; P00490; -.
DR PaxDb; P00490; -.
DR PRIDE; P00490; -.
DR DNASU; 947922; -.
DR EnsemblBacteria; AAT48180; AAT48180; b3417.
DR EnsemblBacteria; BAE77874; BAE77874; BAE77874.
DR GeneID; 66672701; -.
DR GeneID; 947922; -.
DR KEGG; ecj:JW5689; -.
DR KEGG; eco:b3417; -.
DR PATRIC; fig|1411691.4.peg.3311; -.
DR EchoBASE; EB0555; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR InParanoid; P00490; -.
DR OMA; HCACSVA; -.
DR PhylomeDB; P00490; -.
DR BioCyc; EcoCyc:MALDEXPHOSPHORYL-MON; -.
DR BioCyc; MetaCyc:MALDEXPHOSPHORYL-MON; -.
DR BRENDA; 2.4.1.1; 2026.
DR SABIO-RK; P00490; -.
DR EvolutionaryTrace; P00490; -.
DR PRO; PR:P00490; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0031220; F:maltodextrin phosphorylase activity; IDA:EcoliWiki.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030980; P:alpha-glucan catabolic process; IDA:EcoliWiki.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:EcoliWiki.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Direct protein sequencing; Glycosyltransferase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6986282"
FT CHAIN 2..797
FT /note="Maltodextrin phosphorylase"
FT /id="PRO_0000188560"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 294
FT /note="K -> E (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="E -> V (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="F -> L (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="Q -> L (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="E -> V (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="E -> D (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="H -> R (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="E -> K (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="L -> D (in Ref. 5)"
FT /evidence="ECO:0000305"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1L5V"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2ECP"
FT STRAND 195..208
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 263..290
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 366..386
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1E4O"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 435..440
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1QM5"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 494..519
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 580..597
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 616..622
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 662..669
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:1L5W"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 681..690
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 694..700
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 702..713
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 714..719
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 721..724
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 725..730
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 741..760
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 762..775
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 777..779
FT /evidence="ECO:0007829|PDB:1L5W"
FT HELIX 781..791
FT /evidence="ECO:0007829|PDB:1L5W"
FT TURN 792..794
FT /evidence="ECO:0007829|PDB:1L5W"
SQ SEQUENCE 797 AA; 90522 MW; 61E450AAF75C896A CRC64;
MSQPIFNDKQ FQEALSRQWQ RYGLNSAAEM TPRQWWLAVS EALAEMLRAQ PFAKPVANQR
HVNYISMEFL IGRLTGNNLL NLGWYQDVQD SLKAYDINLT DLLEEEIDPA LGNGGLGRLA
ACFLDSMATV GQSATGYGLN YQYGLFRQSF VDGKQVEAPD DWHRSNYPWF RHNEALDVQV
GIGGKVTKDG RWEPEFTITG QAWDLPVVGY RNGVAQPLRL WQATHAHPFD LTKFNDGDFL
RAEQQGINAE KLTKVLYPND NHTAGKKLRL MQQYFQCACS VADILRRHHL AGRKLHELAD
YEVIQLNDTH PTIAIPELLR VLIDEHQMSW DDAWAITSKT FAYTNHTLMP EALERWDVKL
VKGLLPRHMQ IINEINTRFK TLVEKTWPGD EKVWAKLAVV HDKQVHMANL CVVGGFAVNG
VAALHSDLVV KDLFPEYHQL WPNKFHNVTN GITPRRWIKQ CNPALAALLD KSLQKEWAND
LDQLINLEKF ADDAKFRQQY REIKQANKVR LAEFVKVRTG IEINPQAIFD IQIKRLHEYK
RQHLNLLHIL ALYKEIRENP QADRVPRVFL FGAKAAPGYY LAKNIIFAIN KVADVINNDP
LVGDKLKVVF LPDYCVSAAE KLIPAADISE QISTAGKEAS GTGNMKLALN GALTVGTLDG
ANVEIAEKVG EENIFIFGHT VEQVKAILAK GYDPVKWRKK DKVLDAVLKE LESGKYSDGD
KHAFDQMLHS IGKQGGDPYL VMADFAAYVE AQKQVDVLYR DQEAWTRAAI LNTARCGMFS
SDRSIRDYQA RIWQAKR
