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Database: UniProt
Entry: A0A2S0U9G3_9BACL
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ID   A0A2S0U9G3_9BACL        Unreviewed;       812 AA.
AC   A0A2S0U9G3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=DCC85_09675 {ECO:0000313|EMBL:AWB44468.1};
OS   Paenibacillus sp. CAA11.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB44468.1, ECO:0000313|Proteomes:UP000244407};
RN   [1] {ECO:0000313|EMBL:AWB44468.1, ECO:0000313|Proteomes:UP000244407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAA11 {ECO:0000313|EMBL:AWB44468.1,
RC   ECO:0000313|Proteomes:UP000244407};
RA   Um Y., Kim S., Gong G.;
RT   "Complete genome of CAA11.";
RL   Submitted (APR-2018) 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}.
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DR   EMBL; CP028922; AWB44468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0U9G3; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000244407; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000244407};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         656
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   812 AA;  93816 MW;  8F1452D273615ADB CRC64;
     MFENKEVFKE AFQRQLVRKL GKPLEEASET DVYNILSGMI REHIGKDWAE TNTAYKQRQE
     KQVYYFSLEF LIGRLLGSNL LNLGVLELVR DGLADLGYSL EQIEEQEADA GLGNGGLGRL
     AACFMDSLAS LQYAGHGSGI RYKYGLFEQK IMDGNQVELP DYWLQKGYEW EVRRPDKQVE
     VRFWGEVKTR EDNGRLVFET VNYEAVRAVP YDIPIIGYCH PHVNTLRMWS AESMMDPGRQ
     HLNGFNGSYH RYLDYNRSVE SISEFLYPDD SQYEGKLLRL KQQYFLCSAG VQSALRTYAK
     LGLPYNRLAE KVAFHINDTH PTLVIPELMR ILIDEHGFGW DDAWSLTTQI VAYTNHTILS
     EALEKWPVSM VRELLPRIYL IIEEIDRRFR LELHSRFPQD RERISQMAII EYGQIRMAHL
     AIVGSHSVNG VAALHTEILK AREMKSFYEV FPTRFNNKTN GITHRRWLMH ANPKLAELVS
     SCIGKRWIKH PQELNELIKC CEDSGFQEAF GAIKRYNKVR LAQYIYEEQG IHIHPDSIFD
     VQVKRLHAYK RQLLNVLHIM HLYQQLKENP NMDRVPRTFI FGAKAAPSYY LAKRIIKLIN
     TVADRVNNDP VISKTMKVIF LENYSVSLAE RIIPAADVSE QISTASKEAS GTGNMKFMMN
     GALTLGTMDG ANVEMYGLLG SENMFIFGLN ADEVQNYYQN GGYGAWDMYH SDPRIREVMD
     QLVKPGPFSQ VDGEFADIYQ SILDHNDEYF VLKDFADYVE AHLRIDLAYR NERAWQKKAI
     LNVAHSGKFS SDCTIRNYAS EIWRIQPVHR FP
//
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