ID A6W7J7_KINRD Unreviewed; 858 AA.
AC A6W7J7;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=Krad_1298 {ECO:0000313|EMBL:ABS02786.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02786.1, ECO:0000313|Proteomes:UP000001116};
RN [1] {ECO:0000313|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000313|Proteomes:UP000001116};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA Fliermans C., Richardson P.;
RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL Submitted (JUL-2007) 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}.
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DR EMBL; CP000750; ABS02786.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W7J7; -.
DR STRING; 266940.Krad_1298; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; kra:Krad_1298; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000001116; 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 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 ECO:0000313|EMBL:ABS02786.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABS02786.1}.
FT DOMAIN 17..124
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 613
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 858 AA; 93705 MW; BEE77218BB891EDF CRC64;
MSAPVRAIRR FTVRTVLPAP LAPLGELASN LRWSWHKPTR DLFESMDPTA WVAVHREPGA
LLGALSTERL EVLAADPRFV ERVHAAAADL RTYLQRPGWY AGLGDDAPAS VAYFSMEFGI
TGALPQYSGG LGILAGDHLK SASDLAVPIV GVGLFYATGY FKQSLSRDGW QQETYPVLDP
DGLPLSLLRE ADGTAAKVSL DLPGGRRLWA QVWKAQVGRV PLLLLDSDVE ENDDAARGVT
DRLYGGGGEH RLQQELLCGI GGVRALRTWS RLTGAPEPEV YHTNEGHAGF LSVERIREHV
ERGLTFDEAL EAVRAATVFT THTPVPAGID RFGRDQIELY FGAGNPLPGV PLDRVLALGA
EDYEGGDPGV FNMAVMGLRL AQRANGVSQL HGAVSRGMFD GLWPGFDAPE VPIASITNGV
HAPTWVAPEV ITMGKQYIGP ELPREGLGFE KVGQVPDEEI WRTRRLLRAR LVEDARRRLK
LSWLQRGASE AELAWTKDVL DPDVLTIGFA RRVPTYKRLT LMLRDPERLR SMLLHPQRPV
QLVIAGKSHP ADETGKRLIQ QMVRFADDPA VRHRIVFLPN YDITMALTLY PGCDVWLNNP
LRPFEACGTS GMKAALNGGL NLSILDGWWD EWYDGGNGWA IPTADGVDDP EHRDDLEAAA
LYDLVENSVA ARFYDRDERG LPARWLEMVR HTLASLGPKV LASRMVTDYV EQLYVPAARA
GRAALASSAA AARDLARWKA AVRSGWAEVR VEHVESAGVG DSAQIGDVVH VRANVSLGEL
SVDDVEVQVV HGRVSESDEL RPSGTVPLHH GEALGGGRHR FEGEFALRQT GPFGYTVRVL
PRHPGLAGPA ELGLVANA
//
