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Database: UniProt
Entry: A0A0F2REH6_9PROT
LinkDB: A0A0F2REH6_9PROT
Original site: A0A0F2REH6_9PROT 
ID   A0A0F2REH6_9PROT        Unreviewed;       823 AA.
AC   A0A0F2REH6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=VR70_15480 {ECO:0000313|EMBL:KJS35692.1};
OS   Rhodospirillaceae bacterium BRH_c57.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae.
OX   NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS35692.1, ECO:0000313|Proteomes:UP000033468};
RN   [1] {ECO:0000313|EMBL:KJS35692.1, ECO:0000313|Proteomes:UP000033468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS35692.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJS35692.1}.
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DR   EMBL; LAEA01000220; KJS35692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2REH6; -.
DR   STRING; 1629718.VR70_15480; -.
DR   PATRIC; fig|1629718.3.peg.1705; -.
DR   Proteomes; UP000033468; Unassembled WGS sequence.
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         671
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   823 AA;  93222 MW;  2BE84012F3B31EE6 CRC64;
     MTKAVAESAC AELIDVGSVE GIKRQLLSYM VHNVGVSPEA ASPRDWLYAV AGLVRGILSE
     HYLETSRRER DQDARRIYYL SLEYLNGRSL IKHLLDLNLH GPFTQALKDL GQDLDTIQEF
     EFDAALGNGG LGRLAACFLD SMATHSYPGF GYGIRYEFGM FTQRIENGEQ VEHPETWLRY
     GNPWEYERPN IIYPVRFRGR IACFRDEHGK EVCQWVDTED VIAMAYDVPI AGHGSGVVTK
     LRLWSARATR DFDLKYFNQG NYIDAVKDKT ISENLSKVLY PADTTLMGQE LRVMQEYFFV
     SASLQDILAR HNRVYDSLDD LPVKVCIQLN DTHPSLAIPE LMRLLLDVYD YEWAQAWELT
     RQVFNYTNHT LLPEALETWP IAMLEQLLPR HLEIIYQINY DFLQEVKYHF PGQPDLLARM
     SLVNDGQRRI RMAHLCVVGS NHVNGVAALH TELMRSHVFA DFNRMNPDKF INVTNGVTQR
     RWLLQANPGL AELVTEAVGP GWRTDLLKIK GLENLVDDAS FQERFSAIKR ANKIRLAALI
     EARCGVRFNP DSLFDSQIKR IHEYKRQLLN LLHVITQYNH LRDGGTVGAH PRCVVIAGKA
     APGYFLAKLI IRLINDVAAV VNNDPRTRGQ LSLCFLPNYN VSSAEIIIPG TDLSEQISTA
     GTEASGTGNM KFALNGALTI GTLDGANIEI KDAVGDPNIF IFGKTADEVN DMRAHGYRPW
     DYYNSDADLK RAIDMIGQGF FCPDDPGRYR PVHDTLLSQG DHYFLMADYR DYVDTQARVD
     AYYADAKAWT RSAILNVANV GTFSSDRSIH EYASKIWRVK PLS
//
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