ID A0A077JG05_9CYAN Unreviewed; 837 AA.
AC A0A077JG05;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:BAP17841.1};
GN ORFNames=ETSB_1057 {ECO:0000313|EMBL:BAP17841.1};
OS cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP17841.1, ECO:0000313|Proteomes:UP000031625};
RN [1] {ECO:0000313|EMBL:BAP17841.1, ECO:0000313|Proteomes:UP000031625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP17841.1};
RX PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA Archibald J.M., Inagaki Y.;
RT "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT recent adaptations to an intracellular lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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 ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; AP012549; BAP17841.1; -; Genomic_DNA.
DR RefSeq; WP_044106621.1; NZ_AP012549.1.
DR AlphaFoldDB; A0A077JG05; -.
DR STRING; 1228987.ETSB_1057; -.
DR KEGG; ceo:ETSB_1057; -.
DR HOGENOM; CLU_010198_1_1_3; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000031625; 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 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 ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 674
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 837 AA; 95677 MW; 06F27A2624FB9643 CRC64;
MDTFTPQSNI KVEDDRTGMS AETLKRAFLD NLFYLQGIDR SNASLYNYYV AIAYTVRDRL
LHRFLKTIET YKKEKVKIVS YFSAEFLMGR HLGNNLINLD MYDKMREIVE ELGLDFDKII
EQEPDPGLGN GGLGRLAACF LDSLASLEIP AIGYGIRYEF GIFHQTLRDG WQAEIPDNWL
RFGNPWELSH PTESVEVKLG GHTEMVHDEA GNMRIVWIPA RTILAVPYDT PVPGYQTNTV
NPLRLWKAEA SEAFNFDAFN AGQYDQAVAE KMDAETISKV LYPNDNTPAG RQLRLAQQYF
FVSASLQDLI RIHLRTHNSL DDFHEKVAVQ LNDTHPAVSV AELMHLLIDK HNYSWEKAWD
ITQKTFAYTN HTLLPEALER WPAGLFASLL PRHLEIIYEI NYRFLEDVRT WFPGDDQLIS
SLSLIEEREE KLIRMANLAC VGSHAINGVA ALHTELLKRD TLKDFAKLWP EKFYNKTNGV
TPRRWILLSN PELATLITEK IGDGWLKNLD EMRNIEAVVH DPDFRHRWRE IKQGNKRSLA
AYILKNRNIQ VDPNSLFDVQ VKRIHEYKRQ HLMVLHIIAL YNRIKQNPYI DILPRTFIFG
GKAAPGYFLA KLVIKLINAV AEVVNKDPDV RGRLKVVFLP NFNVSLGQRI YPAADLSEQI
STAGKEASGT SNMKFAMNGA LTIGTLDGAN IEIREAAGAE NFFLFGLTAQ EVYDLKTNGY
NPIDYYHNNE ELRGVIDRIA SGYFSHGDGE LFQPIVGPLI CHDPYMLMAD YQSYIDVQEA
VSHAYCDHEK WTDMSILNSA RMGKFSSDRT IREYCKEIWN VDPVSITIEN YNPATSG
//
