PHSG_ECOLI
ID PHSG_ECOLI Reviewed; 815 AA.
AC P0AC86; P13031; Q2M792;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=glgP; Synonyms=glgY; OrderedLocusNames=b3428, JW3391;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2645169; DOI=10.1016/0014-5793(89)80128-0;
RA Choi Y.-L., Kawamukai M., Utsumi R., Sakai H., Komano T.;
RT "Molecular cloning and sequencing of the glycogen phosphorylase gene from
RT Escherichia coli.";
RL FEBS Lett. 243:193-198(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3047129; DOI=10.1016/s0021-9258(18)68298-5;
RA Yu F., Jen Y., Takeuchi E., Inouye M., Nakayama H., Tagaya M., Fukui T.;
RT "Alpha-glucan phosphorylase from Escherichia coli. Cloning of the gene, and
RT purification and characterization of the protein.";
RL J. Biol. Chem. 263:13706-13711(1988).
RN [3]
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 [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 1-383.
RC STRAIN=K12;
RX PubMed=2975249; DOI=10.1016/0378-1119(88)90208-9;
RA Romeo T., Kumar A., Preiss J.;
RT "Analysis of the Escherichia coli glycogen gene cluster suggests that
RT catabolic enzymes are encoded among the biosynthetic genes.";
RL Gene 70:363-376(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 657-815.
RA Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.;
RT "Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of
RT Escherichia coli and regulation by the cAMP-CRP complex.";
RL Agric. Biol. Chem. 53:1135-1143(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=3097003; DOI=10.1016/s0021-9258(18)66708-0;
RA Kumar A., Larsen C.E., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli
RT ADP-glucose:alpha-1,4-glucan, 4-glucosyltransferase as deduced from the
RT nucleotide sequence of the glgA gene.";
RL J. Biol. Chem. 261:16256-16259(1986).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34807.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X16931; CAA34807.1; ALT_FRAME; Genomic_DNA.
DR EMBL; J03966; AAA23874.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC76453.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77864.1; -; Genomic_DNA.
DR EMBL; M22368; AAA23875.1; -; Genomic_DNA.
DR EMBL; D00425; BAA00329.1; -; Genomic_DNA.
DR EMBL; J02616; AAA23871.1; -; Genomic_DNA.
DR PIR; G65138; PHECGG.
DR RefSeq; NP_417886.1; NC_000913.3.
DR RefSeq; WP_000993449.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P0AC86; -.
DR SMR; P0AC86; -.
DR BioGRID; 4261263; 32.
DR DIP; DIP-47899N; -.
DR IntAct; P0AC86; 2.
DR STRING; 511145.b3428; -.
DR jPOST; P0AC86; -.
DR PaxDb; P0AC86; -.
DR PRIDE; P0AC86; -.
DR DNASU; 947931; -.
DR EnsemblBacteria; AAC76453; AAC76453; b3428.
DR EnsemblBacteria; BAE77864; BAE77864; BAE77864.
DR GeneID; 66672688; -.
DR GeneID; 947931; -.
DR KEGG; ecj:JW3391; -.
DR KEGG; eco:b3428; -.
DR PATRIC; fig|1411691.4.peg.3300; -.
DR EchoBASE; EB0375; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR InParanoid; P0AC86; -.
DR OMA; KHKRTFT; -.
DR PhylomeDB; P0AC86; -.
DR BioCyc; EcoCyc:GLYCOPHOSPHORYL-MON; -.
DR BioCyc; MetaCyc:GLYCOPHOSPHORYL-MON; -.
DR PRO; PR:P0AC86; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:EcoCyc.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
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:0005980; P:glycogen catabolic process; IMP:EcoCyc.
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 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..815
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188553"
FT MOD_RES 662
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 13..14
FT /note="SV -> RL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> P (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="IY -> TH (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="L -> W (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Y -> S (in Ref. 1; CAA34807)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..187
FT /note="Missing (in Ref. 2; AAA23874)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="R -> V (in Ref. 1; CAA34807)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="N -> D (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..281
FT /note="EL -> DV (in Ref. 2; AAA23874/AAA58226)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="E -> G (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="P -> S (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="I -> S (in Ref. 5; AAA23875)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="F -> L (in Ref. 2; AAA23874)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..488
FT /note="EH -> GT (in Ref. 1; CAA34807)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..521
FT /note="KL -> NV (in Ref. 1; CAA34807)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="S -> T (in Ref. 2; AAA23874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 93173 MW; B8046B91D8D7B468 CRC64;
MNAPFTYSSP TLSVEALKHS IAYKLMFTIG KDPVVANKHE WLNATLFAVR DRLVERWLRS
NRAQLSQETR QVYYLSMEFL IGRTLSNAML SLGIYEDVQG ALEAMGLNLE ELIDEENDPG
LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VNGSQKESPD YWLEYGNPWE
FKRHNTRYKV RFGGRIQQEG KKTRWIETEE ILGVAYDQII PGYDTDATNT LRLWSAQASS
EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SSTIQDILSR
HYQLHKTYDN LADKIAIHLN DTHPVLSIPE MMRLLIDEHQ FSWDDAFEVC CQVFSYTNHT
LMSEALETWP VDMLGKILPR HLQIIFEIND YFLKTLQEQY PNDTDLLGRA SIIDESNGRR
VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKIFPGR FTNVTNGVTP RRWLAVANPS
LSAVLDEHLG RNWRTDLSLL NELQQHCDFP MVNHAVHQAK LENKKRLAEY IAQQLNVVVN
PKALFDVQIK RIHEYKRQLM NVLHVITRYN RIKADPDAKW VPRVNIFGGK AASAYYMAKH
IIHLINDVAK VINNDPQIGD KLKVVFIPNY SVSLAQLIIP AADLSEQISL AGTEASGTSN
MKFALNGALT IGTLDGANVE MLDHVGADNI FIFGNTAEEV EELRRQGYKP REYYEKDEEL
HQVLTQIGSG VFSPEDPGRY RDLVDSLINF GDHYQVLADY RSYVDCQDKV DELYELQEEW
TAKAMLNIAN MGYFSSDRTI KEYADHIWHI DPVRL
