ID A0A3N2AWZ4_9MICO Unreviewed; 852 AA.
AC A0A3N2AWZ4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=EDD26_2702 {ECO:0000313|EMBL:ROR67292.1};
OS Agrococcus jenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=46353 {ECO:0000313|EMBL:ROR67292.1, ECO:0000313|Proteomes:UP000275456};
RN [1] {ECO:0000313|EMBL:ROR67292.1, ECO:0000313|Proteomes:UP000275456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9580 {ECO:0000313|EMBL:ROR67292.1,
RC ECO:0000313|Proteomes:UP000275456};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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 -!- 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:ROR67292.1}.
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; RKHJ01000001; ROR67292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2AWZ4; -.
DR Proteomes; UP000275456; 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 20..126
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 852 AA; 93857 MW; 521CB1ACCDD0F553 CRC64;
MPLGSVLVRA IRKFTVRTSL PARLGRLEAL ASNLRWSWHE PTRELFREIS LDGWRATGHD
PVQLLGWVGP ERLHQLAEDD DFVARVDALA DDLDDYLSQA RWYQSLDDAP ESIAYFSPEF
GITSALPQYS GGLGILAGDH LKAASDLGVP IVGVGLFYQS GYFKQAISRE GWQQESYPVL
DPDGLPLTIL RNPDGRHATV ALALPGHRTL HARIWVATIG RVPLLLLDTN IHENDPDLRS
VAERLYGGGG ELRLQQELLL GIGGVRALAV YSELTGAPVP AVFHSNEGHA GFLGIERISQ
LTATGLSFDA ALQLVRAGTV FTTHTPVPAG IDRFDVELVR RHLTRELVPG VDVERVLALG
RESDPTIFNM AQLGFSIAQR ANGVSKLHGK VSRQMFQDRW PGFDVQDVPI TSVTNGVHAP
TWTSPILKHL AERELGTLDT ARCDWASEAI TDETLWGVRR EMREHLVEEA RDRTRVKHER
NDGVVPSWVD TMLDPDVLTI GFARRVPTYK RLTLMLHDRD RLRSILTNAE RPVQLVIAGK
SHPADEMGKA LIQELVRFTQ EPDVRGRIVF LENYDISMAK SLYPGCDVWL NNPLRPLEAC
GTSGMKAALN GSLNLSILDG WWEEYFDGKN GWAIPSAHEQ MDAAERDAFE ANALYDLIEH
QVAPRFYDRD ERGLPTAWIA SIRHTLATLS PELSAERMLA EYVGRLYTPA AKAAAAAAAD
GASAARDFAE WTARMRDAFG GVQVHHVEVE GVDVPPIIGD AVTVRAFVAL GSLQPSDVAV
EVVAGTVTEE GELRHARRFP LADAGAEDGN HRFESAIGLE RAGTFGYTVR VVPRHPMLAS
DAELGLVAYP RS
//
