ID K9YDX8_HALP7 Unreviewed; 858 AA.
AC K9YDX8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=PCC7418_2463 {ECO:0000313|EMBL:AFZ44610.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ44610.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003945; AFZ44610.1; -; Genomic_DNA.
DR RefSeq; WP_015226484.1; NC_019779.1.
DR AlphaFoldDB; K9YDX8; -.
DR STRING; 65093.PCC7418_2463; -.
DR KEGG; hao:PCC7418_2463; -.
DR PATRIC; fig|65093.3.peg.2599; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_3; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000010481; 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 ECO:0000313|EMBL:AFZ44610.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ44610.1}.
FT DOMAIN 13..122
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 609
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 858 AA; 97821 MW; 247E798143BD8127 CRC64;
MKPIRTFNVS PSLPPKLEPL KKLAYNIHWD WDIEAKDLFR RLDQQLWESC RHNPVSLLGN
ISQERLAEVA EDEGFLAQME RAEQQLDLYL QERTWFRKNR GQIAQKECYA YFCAEYGLTD
CLPLYSGGLG VLAGDHLKSA SDLGLPLVAV GLLYQEGYFS QYLNADGWQQ EAYPINDFSN
MPLHLEHNPD GSELRVEVDY PGRTVHARVW RIDVGIVRLY LLDTNIEGNS EYDHNITDRL
YGGDLDMRIH QEMMLGIGGF RALKALGYTP TVFHLNEGHS AFLVLERMRR LIEDDGLTFD
EAKQMVQASQ MFTTHTPVSA GFDMFNPDQT MYYVGHYADI FDLSREEFLA MGRENTGDLS
SPFSMAALAL RTSSFLNGVS KLHGEVSREM FKGMWKGLPV EEVPITSITN GVHARSVVTK
SKQQLYDRYL GPSWSEKGPE NPLWEKVDSI PDEELWRNHE RARADMVVMV RDWLGKKLRQ
RGASQAELDK ATEVLDPDVL TIGFARRFAT YKRATLFLRD IERIKKIIMG NPNRRLQFVI
AGKAHPKDMP GKDLIRQLIH TAREEGIEDY LVFVPDYDTH VARSMVSGCD IWLNTPRRPR
EASGTSGMKA AMNGLPNLSI PDGWWDEADY TATGWAIGQG EMYEDQEYQD EVEANALYDL
LEQEIMPLFY NRDANGVPRG WVKKMKNAIR LNTPQFNTAR MLRDYSVYGY FPSSDRYFAM
TENKYANAKA VAQWKKQLFE RWYDIRIESI DVSEGTDIVV NETIEVKAVL DLAGLKPDDV
SVELYLGNLN SDGEIVKGTP IPMEYTGESS AAGTIYKGSL VYRSSGLQGL SLRVLPKNQY
MAHPHELGLI LWADDCQQ
//
