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Database: UniProt
Entry: E6KRG3_9ACTO
LinkDB: E6KRG3_9ACTO
Original site: E6KRG3_9ACTO 
ID   E6KRG3_9ACTO            Unreviewed;       788 AA.
AC   E6KRG3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=glgP {ECO:0000313|EMBL:EFU61395.1};
GN   ORFNames=HMPREF9006_0815 {ECO:0000313|EMBL:EFU61395.1};
OS   Actinomyces sp. oral taxon 180 str. F0310.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=888052 {ECO:0000313|EMBL:EFU61395.1, ECO:0000313|Proteomes:UP000006252};
RN   [1] {ECO:0000313|EMBL:EFU61395.1, ECO:0000313|Proteomes:UP000006252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0310 {ECO:0000313|EMBL:EFU61395.1,
RC   ECO:0000313|Proteomes:UP000006252};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC       glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC       glucose-1-phosphate, and plays a central role in maintaining cellular
CC       and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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       {ECO:0000256|ARBA:ARBA00025174}.
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         Evidence={ECO:0000256|ARBA:ARBA00001275,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU61395.1}.
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DR   EMBL; AEPP01000011; EFU61395.1; -; Genomic_DNA.
DR   RefSeq; WP_009212276.1; NZ_GL622194.1.
DR   AlphaFoldDB; E6KRG3; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_11; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000006252; Unassembled WGS sequence.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         631
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   788 AA;  89600 MW;  8C1C4A291C7FFA6D CRC64;
     MTLDLTQSLP SHVRATSGRP VEDSTLMEVW QGLSAAIVDQ IADNWAATTE RYAKGRQEHY
     FSAEFLMGRA LLNNLSNLGL VDEAREALAR YGLDLGQVLE EEPDAALGNG GLGRLAACFL
     DSCATLDLPV RGYGILYRYG LFKQLFDNGF QTEHPDPWME EGYPFVIRRE ERARIVSYAD
     LTVRAVPYDI AITGYGTKNV GTLRLWKAEP IEEFDYDAFN SQRFTDAIVD RERTMDISRV
     LYPNDTTFEG KVLRVRQQYF FCSASLQEIV ENYVRHHGSD LTGFAEYNAV QLNDTHPVLA
     IPELMRILMD EHGLGWEDAW AVVSKTFAYT NHTVLAEALE TWDIHIFDRL FPRISEIVRE
     IDRRFRIDMA DRGLDQGTID YMAPVAGNSV RMAWIACYAS YSINGVAALH TEIIKRDTLK
     EWYAIWPERF NNKTNGVTPR RWLKQCNPRL AALLDEVTGS DTWVRDLTEL SKFTSAGSDA
     VLERLDRIKY ENKVEFAAWV KEREGVDIDP TAIFDVQIKR LHEYKRQLLN AFYVLDLYFR
     IKDDPTLDTP NRVFIFGAKA APGYIRAKAI IKLINAIAEL VNNDADINGR IKVVFVHNYN
     VSPAEHIIPA ADVSEQISMA GKEASGTSNM KFMMNGALTL GTLDGANVEI LEAVGEENAY
     IFGATDDELP ELRRHYDPRW HYENVPGLKR VIDALTDGTL DDAHSGWFHD IRHSILEGGF
     DPADVYYVLG DFASYRETKD RMAADYRDRA AWNARVWVNI TRSGRFSSDR TISDYAREVW
     RIEGEPIA
//
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