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
//