ID C7MW60_SACVD Unreviewed; 851 AA.
AC C7MW60;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=Svir_28480 {ECO:0000313|EMBL:ACU97829.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97829.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU97829.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU97829.1; -; Genomic_DNA.
DR RefSeq; WP_015787141.1; NC_013159.1.
DR AlphaFoldDB; C7MW60; -.
DR STRING; 471857.Svir_28480; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; svi:Svir_28480; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000000841; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..125
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 610
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 851 AA; 94643 MW; 0FC412401FDC308A CRC64;
MKAVRRFTVH ARVPDELSGL AELATNLRWT WHPPTRDLFA SMDDALFRRI RDPLRMLAEV
PASRLDELAR DPEFLDRTRK ASEDLQRYLT EPRWYQRRME QAEDGERFPR AIAYFSMEFG
VHEALPNYSG GLGVLAGDHL KAASDLGVPV IGVGPLYRAG YFRQSLSLDG WQVEHYPVID
PSGLPLELLT EPSGEPVYVH VAMPGGRDLL AQIWLARVGR VPLLLLDTDV EGNDEDLRGV
TDRLYGGDDD HRIRQEILAG IGGMRAVRRY CELTGHPQPE VFHTNEGHAG FLGLERVREV
LAEGELTFEE ALSAVRAGTV FTTHTPVPAG IDRFGVDLVR HYFGDGRLLP GVDVERVLAL
GSEDNPERFN MAHMGLRLAQ RANGVSALHG KVSRRMFSRL WPGFDIEEVP ISSVTNGVHG
PTWVAREMSA LLGGSDEEWG HDGNGSGIDP NVTDEQLWAL RRELRGNLVA EVRRRAREAW
LQRGASALEL GWTERIFDPD VLTVGFARRV PTYKRLTLML RDPERLRALL LDDERPIQIV
VAGKSHPADE GGKALIQQIV RFVDDPAVRE HIVFLPDYDM SMARYLYRGC DVWLNNPTRP
LEACGTSGMK AALNGCLNLS IRDGWWDEYY DGSNGWAIPT ADGVTDPLLR DDLEAAALYD
LLGQQVAPLF YDRDENGVPR GWLSMIWHTL RTLGPRVQAS RMVREYVESF YRPAATTVAA
AVADDYAGAR SLAAYRARVD ACWPLLRVVS TELSVEDSDV PVVGARARIT ARVELAELDE
DDVEVQAVVG RVGDTDDLSD VVTATMAPCG RGEFVTSLRL PFAGSLGYTV RVLPKHPLLA
TPAELGRVVL A
//
