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Database: UniProt
Entry: W0R7U4_BIBTR
LinkDB: W0R7U4_BIBTR
Original site: W0R7U4_BIBTR 
ID   W0R7U4_BIBTR            Unreviewed;       837 AA.
AC   W0R7U4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=F544_13040 {ECO:0000313|EMBL:AHG86532.1};
OS   Bibersteinia trehalosi USDA-ARS-USMARC-190.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Bibersteinia.
OX   NCBI_TaxID=1263832 {ECO:0000313|EMBL:AHG86532.1, ECO:0000313|Proteomes:UP000019086};
RN   [1] {ECO:0000313|EMBL:AHG86532.1, ECO:0000313|Proteomes:UP000019086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA-ARS-USMARC-190 {ECO:0000313|EMBL:AHG86532.1,
RC   ECO:0000313|Proteomes:UP000019086};
RA   Harhay G.P., McVey S., Clawson M.L., Bono J., Heaton M.P.,
RA   Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT   "Annotation of the Bibersteinia trehalosi USDA-ARS-USMARC-190 complete
RT   genome.";
RL   Submitted (DEC-2013) 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; CP006956; AHG86532.1; -; Genomic_DNA.
DR   RefSeq; WP_025289441.1; NZ_CP006956.1.
DR   AlphaFoldDB; W0R7U4; -.
DR   KEGG; btra:F544_13040; -.
DR   PATRIC; fig|1263832.3.peg.1295; -.
DR   HOGENOM; CLU_010198_1_1_6; -.
DR   Proteomes; UP000019086; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         664
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   837 AA;  95660 MW;  D1E7000972CD6A83 CRC64;
     MAQRQPTNQL SPENIQSVKN AILHKLVFAL GVEPRDATRR NWLNAALRVV RDLSTESWLQ
     TRRSQAENTS RRVYYLSMEF LMGRTFSNAM ISEGVYELMR AAFKELGQDL EDIINEEGDP
     GLGNGGLGRL AACYMDSLAA MKIPAIGYGI RYEYGMFRQE IKNGEQVEHP DDWLEKEFVW
     PYLRASKRFP VRFGGRTWQE GKKTVWQADD EIIAQAHDQL IPGFETASTN SLRLWSAHAG
     DKVFGLSDFN RGDYFAAMSK QNSSENVSRV LYPDDSTYNG RELRLRQEYF LCSASVQDIV
     RRHEVESGSC LNLAEKVAIH LNDTHPTLAI PELMRILIDE KGYSWEQAWN TTRKTFFYTN
     HTLMSEALET WPVEMVARVL PRHLQIIFEI NEWFLQQVRE QFPGDEELIQ RVSIIDEHGD
     RRVRMAWLAV IASGKVNGVA KIHSDLMVDS IFADFAKIYP ERFTNVTNGV TPRRWIQIAN
     PGLANILDKY IGRDWRTELT QLEQLNAFAD DADVQAQIAA VKVENKRKLA EYVAQTQGIK
     LNPEAIFDVQ IKRIHKYKRQ QLNVLHIIAL YNRILRNPSA DWQPRVFIFA GKAASAYYAA
     KKVIRLINDV ANVINNDSRI NDLIKVVFIP NYSVTLAQLI IPAADVSEQI SLAGTEASGT
     SNMKFALNGA LTIGTLDGAN VEILERVGNE HIFIFGNTVE QVEELRRRGY SPYHYFERDA
     ELNEAISQIL NGKFSPEDPY RYQDLILNSG DYYQACADFR AYVDMQEQVA KAFRNKQAWN
     KSAIINIANM GYFSSDRSVL DYARDIWHIE PMDEKQLAEQ PSVAELMSDA SKLLIIK
//
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