ID A0A0F6QYV5_9CORY Unreviewed; 798 AA.
AC A0A0F6QYV5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:AKE39463.1};
GN ORFNames=UL81_07540 {ECO:0000313|EMBL:AKE39463.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39463.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AKE39463.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39463.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
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; CP011311; AKE39463.1; -; Genomic_DNA.
DR RefSeq; WP_035105139.1; NZ_CP011311.1.
DR AlphaFoldDB; A0A0F6QYV5; -.
DR KEGG; ccj:UL81_07540; -.
DR PATRIC; fig|161896.4.peg.1475; -.
DR HOGENOM; CLU_010198_1_1_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000033566; 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:UP000033566};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 635
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 798 AA; 90375 MW; 88E8AEADB691EED7 CRC64;
MSQPQHSAFQ AAIPSHVRAA SGVSPQKATD RKYWSGLSAA VMEQIADNWE ATRRTYAAGR
QQHYFSAEFL QGRALLNNLT NLDLVDDAQV AAKASGRELS DILEAEHDAA LGNGGLGRLA
ACFLDSAVTQ DYPVTGYGLL YRYGLFRQSF DNGYQHEAPD AWMENGYDFV IRRASEQRIV
HFDDMDVRAI PYDMPITGYG TDNVGTLRLW KSEPIDEFDY DAFNSQRFTE AIVDRERVMD
ICRVLYPNDT TYEGKVLRVR QQYFFVSASL QNMVDNYIAH HGEDLSDFAK YNCIQLNDTH
PVLAIPELLR ILLDEHGMGW DEAWKIVTET FAYTNHTVLA EALESWEISI IQKLFWRIWE
LIEEIDRRFR EDMIGRGLDS ARIDYMAPVS NGKVHMAWIA CYAAYSVNGV AALHTEIIKA
DTLRDWYDLW PEKFNNKTNG VTPRRWLKMC NSRLADLLTE ALGSDSWVTN LTDLAKLAPL
ADDADIRKQL REVKTANKQA FAEWINDHQG AEVDPDSIFD VQIKRLHEYK RQLLNGLYIL
DLYFRIKEDG ESVPKRTFIF GAKAAPGYVR AKAIIKLINT IGDLVNNDPD TKDILRVVFV
ENYNVSPAEH IIPAADVSEQ ISVAGKEASG TSNMKFMMNG ALTLGTMDGA NVEIVEAVGE
ENAYIFGARN EELPKLRKGY NPGELYNQVP GLSRVLDALT DGTLGAENNG MFGDLRSSLL
DGYGEHAQDT YYVLGDFADY RETRDRMADD YVNDPEGWDR MAWLNICYSG RFSSDRTIED
YANEVWKLEP TPARPVED
//
