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
//