ID A0A073CGD2_PLAAG Unreviewed; 845 AA.
AC A0A073CGD2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:KEI67329.1};
GN ORFNames=A19Y_2412 {ECO:0000313|EMBL:KEI67329.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI67329.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI67329.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI67329.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(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; CM002803; KEI67329.1; -; Genomic_DNA.
DR RefSeq; WP_026796549.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CGD2; -.
DR STRING; 388467.A19Y_2412; -.
DR GeneID; 77289109; -.
DR PATRIC; fig|388467.6.peg.2359; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_3; -.
DR Proteomes; UP000027395; 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 Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 677
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 845 AA; 97118 MW; C3CEF4DAD1D3BAB8 CRC64;
MTEPLIPVNE CPIQIEDDRT GTSVETLKRA FADNLFYELG KYEAIASKED FYMALAYTLR
DRLLSRWLKT FKTYDDNNVK IVYYLSAEFL MGRHLGNSLI NLHLYDRIRQ AVEESGLDLD
ELLEQEPDPG LGNGGLGRLA ACFLDSLATL EIPAVGYGIR YEFGIFHQIM QDGWQAEIPD
KWLRFGNPWE IPRPDQAIDV NFGGHTETYH DEKGRERIRW IPAKTVIGIP YDTPVPGYDT
NTVNPLRLWK AEASDAFNFD AFNAGNYDGA VADKMRSETI SKVLYPNDNT PQGKQLRLEQ
QYFFVACSLR DIIKRHLKHN SSLSNLNETA AIQLNDTHPA IAIAELMRLL LDEYGIDWDS
AWRVTQKTFA YTNHTLLPEA LEKWSVGLFE YLLPRHLQVI YEINRRFIED VRRWYPGDND
LIGRLSLIEE SGEKYVRMAH LACVGSHAVN GVAALHTELL KQDTLRDFYK LWPEKFFNKT
NGVTPRRWIL LSNPTLSEFY SSKIGDGWLK DLDKLRQLEA YVDDPEFCEQ WHQIKLYNKK
LLADYIWKFN GIEADPHSIF DIQVKRIHEY KRQHLDVLHI ITLYNRIKQN PNTHICPRTF
IFGGKAAPGY FMAKLIIKLI NAVAEVVNKD PDVRGRLKVV FLANFNASLG QRIYPAADLS
EQISTAGKEA SGTGNMKFAM NGSLTIGTLD GANIEIREEA GFENFFLFGL TAEEVYNLKL
KGYKPSDYYN NNPELKAVID RISSGYFSHG NQEMFKPLVD SLMYHDEYML FADYQSYIDC
QREVSVAFQD SKKWTRMSIL NALRMGKFSS DRTIGEYCNE IWNVKSVPVE MEGYNPESAG
LRVIN
//
