ID K9PFR4_9CYAN Unreviewed; 854 AA.
AC K9PFR4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=Cal7507_1815 {ECO:0000313|EMBL:AFY32270.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32270.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY32270.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32270.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) 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}.
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DR EMBL; CP003943; AFY32270.1; -; Genomic_DNA.
DR RefSeq; WP_015128087.1; NC_019682.1.
DR AlphaFoldDB; K9PFR4; -.
DR STRING; 99598.Cal7507_1815; -.
DR KEGG; calo:Cal7507_1815; -.
DR PATRIC; fig|99598.3.peg.2036; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_3; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000010390; 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:AFY32270.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFY32270.1}.
FT DOMAIN 13..121
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 854 AA; 97033 MW; 5EC2E0E0185339EA CRC64;
MQPIRTFNVS PSLPQRLEPL RPLAHNLHWD WNVDTKDLFR RLDPDLWESS RHNPVLMLGT
ISQSRLSEVV EDEGFLAQMD RAARQLEDYL QEHTWYQKQR SQKPKEVYAY FSAEFGLVDC
LPVYSGGLGV LAGDHLKSAS DLGLPLVGVG LLYQQGYFAQ YLNADGWQQE RYPINDFYNM
PLHLERNPDG SELRIAVEYP GRQVYARVWR VQVGTVPLYL LDTNIEPNNP YDHDITDQLY
GGDIDMRIHQ EIMLGIGGVQ MLKALGYKVT AYHMNEGHAA FSALERIRGL MQEEGLSYAD
AKQVVASSNI FTTHTPVPAG IDLFAPDKIL YYLGYYADIF GLPKEQFLGL GRENTGDLSG
PFSMAVLALK MATFSNGVAQ LHGVVSRQMF QGLWKKVPVD EVPIAAITNG VHARSCVAKS
TQELYDRYLG PNWSSAPVDS QLWERMEAIP DEELWRNHER CRLDMVLYVR EHLVKHLRDR
GASASEIAQA QEVLDPKVLT IGFARRFATY KRATLWMRDL DRIRQILLGN KDRKVQFVIA
GKAHPKDIPG KELIRDINHF IREQHLEKQV VFVPNYDIHI SRLMVAGCDI WLNTPRRPRE
ASGTSGMKAA MNGLPNLSVL DGWWDEADFV RTGWAIGHGE NYDDPNYQDE VEANALYDLI
EKEVAPLFYD HRDADGLPRP WVAKMKDAIR LNCPFFNTAR MVREYAERAY FPASDRYHTL
TADNYLPAKE LAEWKANVSE HWFNITIKDI DVSAAADIEV NQTVAVKAKV DLATLTNNDV
QVELYQGAID ANGDIVNAIP VVMDYQGEDA QKLSIYTANI TYTTSGLQGL SLRVLPKHKY
LSSAYEPRLI VWAE
//
