ID M5B8G4_9MICO Unreviewed; 851 AA.
AC M5B8G4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP {ECO:0000313|EMBL:CCE75322.1};
GN ORFNames=CMN_01371 {ECO:0000313|EMBL:CCE75322.1};
OS Clavibacter nebraskensis NCPPB 2581.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE75322.1, ECO:0000313|Proteomes:UP000012170};
RN [1] {ECO:0000313|EMBL:CCE75322.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE75322.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA Eichenlaub R., Rueckert C.;
RT "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT nebraskensis.";
RL Submitted (APR-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE614873; CCE75322.1; -; Genomic_DNA.
DR RefSeq; WP_015490085.1; NC_020891.1.
DR AlphaFoldDB; M5B8G4; -.
DR KEGG; cmc:CMN_01371; -.
DR PATRIC; fig|1097677.3.peg.1180; -.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000012170; 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:CCE75322.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE75322.1}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 851 AA; 93316 MW; 5365063DAAEF8600 CRC64;
MKAIRRFTVR AVLPEELSAL DELAGNLRWS WYEPTRRVFA HVSPELWEGT GHDPVALLGV
VDQERLRELA DDEGFVAWAE EQRADLRAYV REPRWYQQLE GDVPEAIGYF SPEFGIAAAL
PQYSGGLGIL AGDHLKSASD LGVPLVGVGL FYRSGYFRQG ISSDGWQQES YPVFDPDGLP
LQVLRDADGA PVHVALELPG DRTLHARIWG ARVGRIPLLL LDTDVPENDD ELRRVTDRLY
GGGGEHRLHQ ELLLGVGGVR AIAAHARVTG APVPRVFHTN EGHAGFLGVE RISTLMADGL
DFDEALQVVR AGTVFTTHTP VPAGIDRFDV ELVRQHVTER LLPGVPTERV LGLGAELHEG
GSPDVFNMAL MGLRLAQRAN GVSQLHGEVS RGMFAGLWPG FDTEEVPITS VTNGVHAPTW
TDPMLMSLAR ERLGTWDTTA ADWSSSAVTD GDLWDVRGRM RRQLVEDARR RVVRAWREQN
PGAVEPAWLE DVLDPEVLTI GFARRVPTYK RLTLMLHDRE RLRRILTDPE RPVQIVVAGK
SHPADDEGKR LIQELVRFAA EPGIRGRLVF LPDYDIGMAQ LLYPGTDVWL NNPLRPLEAC
GTSGMKAALN GALNLSILDG WWNEYFDGGN GWAIPSADRA HDGAERDAME ATALYDLIEN
RIAPRFYERD GDGVPTGWVH DIRHTLRTLS PELSADRMVR QYVERLYVPA GRAQAVVAAD
GSARARELAA WRGRVVAAWP SVQVAHVESE GVEHQAQVGD ELRVRAWVAL GGLGSEDVTV
EVVHGRTGEG DVLTDVVRQA LAPVGGSGGQ QEYAGTVRLA SAGPFGYTVR VVPRHELLAS
SAEPGLVAVA G
//
