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Database: UniProt
Entry: A0A0M8U0A2_9ACTN
LinkDB: A0A0M8U0A2_9ACTN
Original site: A0A0M8U0A2_9ACTN 
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
//
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