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
//