ID Q8FP06_COREF Unreviewed; 860 AA.
AC Q8FP06; C8NPU4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18797.1, ECO:0000313|Proteomes:UP000001409};
RN [1] {ECO:0000313|EMBL:BAC18797.1, ECO:0000313|Proteomes:UP000001409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC {ECO:0000313|Proteomes:UP000001409};
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18797.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FP06; -.
DR STRING; 196164.gene:10742415; -.
DR KEGG; cef:CE1987; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000001409; 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; 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; 2.
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:UP000001409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..127
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 617
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 860 AA; 95990 MW; D4B4593279348229 CRC64;
MESVKSVGTV KFSNQLPTQL EPLVQLAHNL RWSWREETKQ LFRDIDPELW SKLGEDPKQM
LHQAPASRLR ELAGDDGYLG RINNESQNLS EYLTAPLWYQ KTCATSDRSN NLITAYFSME
FGIHPSLPIY SGGLGVLAGD HMKSASDLGV PLIGVGLLYT HGYFTQSLTA DGWQQEKYEY
HDPANLPIVA VTDDKGEQLK VTVAFPEGRQ ITIALWVANV GRVPLLLLDT NIDENPEDMR
SVTDRLYGGD SEHRIKQEIV LGVGGIRAVD AYCEQKGIPR PDVAHLNEGH AGFLTLERIR
QRMAQGMDYA AAFEQVRASN IFTTHTPVPA GIDRFDMSMV RRYLGDGLPE DQQLCPGIPL
DKAIELGRED DPSLFNMAHM GLRASQRANG VAKLHGEVSR EMFAGLYPGY EPAEVPIGHV
TNGVHLPTWV KPEMLELIER VSGGADLAVA DTWSNPDAVP NEKIWEVRNK LRADLVEVAR
AATFESWATR GHAEAQLGWT RRVLDPEVLT IGFARRVSTY KRLTLMLRNP ERLRSILLNE
ERPVQFVIAG KAHPHDMGGK KLMQEIVQFA DQAGVRDRFL FLPDYDINLA SYLVAGTDVW
LNNPVRPQEA SGTSGMKAVM NGGLTLSISD GWWDEMPQEE TGWTIPTVET PDFEYRDHLE
SQALYDLLEN DVAPLFYDRD DNGIPQGWLE MIRRSWTTLS PMVTSTRMVR DYTTDYYRPT
QHQAMLIAKP EDASSYAAWL ETVKSEWSTV ALSNLRVADT APGAEAHAET ETETLITVDV
DPGSLEHGDI RVQAIIGDQD DHGQIVDPVV YDMDKTGKST YTVAIHRDLP GTVGYTARVV
PCHDMLVNAA ETGLITYYPA
//
