ID A0A0M8U0A2_9ACTN Unreviewed; 876 AA.
AC A0A0M8U0A2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=ADK57_02875 {ECO:0000313|EMBL:KOU77256.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU77256.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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:KOU77256.1}.
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DR EMBL; LGDG01000009; KOU77256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8U0A2; -.
DR STRING; 1415546.ADK57_02875; -.
DR PATRIC; fig|1415546.3.peg.636; -.
DR Proteomes; UP000037741; 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; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..124
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 619
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 876 AA; 96834 MW; 5C2C6D42DB9AD0E4 CRC64;
MRWNVKAIRR FTVRPVLPDP LRPLSDLARN LRWSWHAETR DLFQSVDPER WAASGGDPVR
LLGSVPPARL AELAEDRRFL RRLTAAADDL NDYVTGARWY QAQTSALPLA VAYFSPEFGI
TAALPQYSGG LGILAGDHLK AASDLGVPLI GVGLLYRHGY FRQSLSRDGW QQEHYPVLDP
NELPVALLKE PDGTPAQVSL ALPGGKRLHA RIWLAQVGRV PLLMLDSDVE ENDLGERGVT
DRLYGGGSEH RLLQEMLLGI GGVRALRTYC RLTGHAEPEV FHTNEGHAGF LGLERIAELC
AEGLDFDSAL EAVRAGTVFT THTPVPAGID RFDRELVAHH FGPDAELPRI DVGRVLQLGM
ETYPGGEPNL FNMAVMGLRL AQRANGVSLL HGKVSREMFS GLWPEFDAEE VPITSVTNGV
HAPTWVAPEV FRLGARQIGA QRTEDAMTVG GSDRWDAVAD IPDQDIWELR RNLREQLVTE
VRERLRASWR QRGAGTAELG WIDGVLDPDV LTIGFARRVP SYKRLTLMLR DRDRLMDLLL
HPERPIQIVV AGKAHPADDG GKRLVQELVR FADDPRVRHR IVFLPDYGMA MAQKLYPGCD
IWLNNPLRPL EACGTSGMKA ALNGCLNLSV LDGWWDEWFQ PDFGWSIPTA DGAGTDPDRR
DDIEADALYD LLEQRVTPRF YERGQGGLPD RWIEMVRQTL TLLGPKVLAG RMVREYVERL
YAPAAHAHRT MDPDAARELA EWKSRLRSAW HGVTVDHVET TTAIATAELG TTLGLRVRVG
LGGLAPEDVE VQAVSGRVDG EDRITDATTV PLKPAGGPDP EGRWVYEGPL SLDRTGPYGY
TVRILPAHRL LASGAEPGLV ALPSEDVVEA AGVLMR
//