ID S3ZK31_9ACTN Unreviewed; 876 AA.
AC S3ZK31;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=STRAU_3863 {ECO:0000313|EMBL:EPH43089.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH43089.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH43089.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH43089.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-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 -!- 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:EPH43089.1}.
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DR EMBL; AOPZ01000183; EPH43089.1; -; Genomic_DNA.
DR RefSeq; WP_016641990.1; NZ_AOPZ01000183.1.
DR AlphaFoldDB; S3ZK31; -.
DR PATRIC; fig|1286094.4.peg.3817; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000014629; 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 Reference proteome {ECO:0000313|Proteomes:UP000014629};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..124
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 619
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 876 AA; 96355 MW; 3E7419467DBA07B1 CRC64;
MKAIRRFTVR PVLPAPLGPL AELARNLRWS WHAGTRDLFR DVDPGLWESS GGDPVRLLGS
VPPARLAELA ADDGFLRRLD EAADALREYV TGVRWYQERQ GDTDAELPGA IAYFSPEFGV
TAALPQYSGG LGILAGDHLK AASDLGVPLI GVGLLYRHGY FRQSLTRDGW QQEHYPVLDP
NELPLTLLRE ADGTPARVRL ALPGGRALAA HVWQAQVGRV PLLLLDSDVE ENDPGAREVT
DRLYGGGSEH RLLQEMLLGI GGVRAVRTYC RLTGHPEPEV FHTNEGHAGF LGLERIHELV
HDGADFDSAL ESVRGGTVFT THTPVPAGID RFDRELVAHH FGPAAELPDI DVELILRLGM
ETYPGGEPNL FNMAVMGLRL GRCANGVSTL HGKVSREMFQ GLWPGFDPEE VPITSVTNGV
HAPTWVAPEV IRLGARQIGQ ERTDRALSVG GSERWDAVAD IQDADIWLLR RELRAQLVHE
VRRRLHVSWR QRGAATAELG WIDEVLDPDV LTIGFARRVP SYKRLTLMLR DQDRLMELLT
HPERPVQIVV AGKAHPADDG GKRLIQDLVR FTDDPRVRHR VVFLPDYGMA MAQKLYAGCD
VWLNNPLRPL EACGTSGMKA ALNGCLNLSV LDGWWDEWFE PDFGWAIPTA DGAATDDHRR
DDLEAAALYD LLERRVTPRF YEHGPGGLPD RWIEMVRRTL TRLGPKVLAG RMVREYVERL
YVPAARAHRM LAPDAAASLA AWKSRVRAAW PGVAVDHVEA TAVGATAELG ATLALRVRVQ
LGELTPDDVE VQAIAGRVDP EDHITDATPV PLKPASGPDT EGRLLYEGPL SLDRTGPFGY
TVRILPAHRL LADATELGLV AVPSETTGEA AGVLMR
//
