ID A0A0S7YX54_9DELT Unreviewed; 714 AA.
AC A0A0S7YX54;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=AMJ54_00325 {ECO:0000313|EMBL:KPJ79142.1};
OS Deltaproteobacteria bacterium SG8_13.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ79142.1, ECO:0000313|Proteomes:UP000051346};
RN [1] {ECO:0000313|EMBL:KPJ79142.1, ECO:0000313|Proteomes:UP000051346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ79142.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ79142.1}.
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DR EMBL; LJNK01000001; KPJ79142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YX54; -.
DR STRING; 1703398.AMJ54_00325; -.
DR PATRIC; fig|1703398.3.peg.1494; -.
DR Proteomes; UP000051346; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 604
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 714 AA; 81017 MW; 980ED1FA2E293CD5 CRC64;
MTDIRALFPN LPDRIVGLGE LAENLWWSWR PRARMLFKML DRQAWKDSGH NPDKMLRELP
AEILNSAAVN PDYLRHYDVV LSIFRNYMNR KQCPILKTPL ESGSVAVAYF SAEYGLHRSL
PFYAGGLGFL AGDFLKESSD LNLPVVAVGF MYPEGYLHQK IGEDGWQENI EEYFDRDAAA
ISRVLNSQGN QLVVKVPVIE PVVHVAVWKV AVGRVPLFLL DTDIEQNDPW NRVMSARLYT
GDLEQRMRQE IVLGIGGATV LKTLGVAYQV MHLNEGHAAF ALLERIRDLT ADGDNFEEAF
EKVKQRTVFT THTPVPAGHD VFSFQMMEKY FHRYWPALGI ERERFLQLGV SPAAPQAGFN
MTAFALRSSL CRNAVSKKHA AVTGEMWQGL LPAAGTGQEA MEHVTNGIHL PTWVEPKLKM
LFDRYLGAGW VDDHDNPLVW EMIDKIPDQE LWQVHYWMKI KLIDAVRERS RRRWVQDRAG
SSIILAGGAL LDPSVLTVGF ARRFATYKRA ALILNDLERL KRLVNDRWRP VQIIFAGKAH
PADSPGKMIL QQIFNACRNP ELGGRIAFVE DYGEQLAQYL VHGVDLWLNT PLPPMEASGT
SGMKAALNGV PQLSILDGWW IEGYNGKNGW AFEHRAQEGD RDSLDANEIY RLLEHDIIPL
YYRVSDDGIP TGWVDMMKET IKASAARFSA RRMVKDYVEK FYAPALEVKR QNGL
//
