ID A0A0S8CLM2_9BACT Unreviewed; 710 AA.
AC A0A0S8CLM2;
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=AMK69_16990 {ECO:0000313|EMBL:KPK23947.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK23947.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK23947.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK23947.1};
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:KPK23947.1}.
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; LJNR01000334; KPK23947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CLM2; -.
DR PATRIC; fig|1704023.3.peg.2052; -.
DR Proteomes; UP000051394; 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 12..121
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 605
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 710 AA; 81442 MW; B0808F3AC25616D5 CRC64;
MTQIIQNLFP NLPTRLTGLG EIAENLWWSW HPAARMLFKT LNRQGWKDSG HNPDKMLREI
PKEVLESAAN DPEYLRHYDA VLSKFRKEIE GNTCRILQKD VHPDTPLVAY FSAEYGLHRS
LPFYAGGLGF LAGDYLKECS DLNLPLVSIG FMYPEGYFHQ IIREDGWQEG RDEILDREAA
SISRVLKEDG EQVVVKVPFI EPSIYVAVWK VCIGRVRLYL MDTDIEMNDP WNRGISARLY
SGDMEQRLRQ EIVLGIGGSE VLETLEIKHS VTHLNEGHPA FALLEGIRDC VQGGMQYEEA
AEKVRRTTVF TTHTPVPAGH DVFPFHLMEK YFSSYWPSLG LDHDAFLQLG IHPNEPQAGF
NMTAFALRMS GYCNAVSKRH GEVARRMWHG LWPGLTEDNI PISHVTNGVH VPTWVEPKME
LLFKKYLGPG WLEDHDDPHL WELIEEIPDD ELWKTHYWLK IKLIDAMRDR TRRRWAQDRV
SPSVSLAGGA LLDPSVLTIG FARRFATYKR ADLIFYDMER LKRLLNDRWR PIQIIFAGKA
HPADDPGKRI LQRIFNAARD PEMGGRIAFV EDYGELLAQY LVHGVDVWLN NPIPPMEASG
TSGMKAALNG VPHLSIIDGW WVEGFNGRNG WAFGHEEVDR NRDQADAEAI YRILEQEILP
LYYKVSDNGI PHDWVRIMKQ SIKSTAAAFS ARRMVKEYVE KFYVKALKEA
//
