ID A0A3P1S8Q2_9FIRM Unreviewed; 752 AA.
AC A0A3P1S8Q2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:RRC93613.1};
GN ORFNames=EII25_01520 {ECO:0000313|EMBL:RRC93613.1};
OS Erysipelotrichaceae bacterium OH741_COT-311.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC93613.1, ECO:0000313|Proteomes:UP000270315};
RN [1] {ECO:0000313|EMBL:RRC93613.1, ECO:0000313|Proteomes:UP000270315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC93613.1,
RC ECO:0000313|Proteomes:UP000270315};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRC93613.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RQZE01000003; RRC93613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1S8Q2; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000270315; 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 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:UP000270315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 602
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 752 AA; 86642 MW; 31CEA1E565BD33FE CRC64;
MNLETNLLKH LNKPISEASN QELYDATLNL VKEYTLNKKP IEGNRKLYYI SAEFLIGKLL
SNNLINLGIY DELKTVLQSN NKNITEIEEL EQEPSLGNGG LGRLASCFID SIATLGLNGD
GVGLNYHFGL FKQQFKQGLQ HEIKNEWMTP KSWLNKTDVS FQVQLADKVV TANMYDIDVI
GYDNGVNKLH LFDLANVDET LVHDQSISFD KENFEKNLTL FLYPDDSDEA GHLLRIYQQY
FMVSSAAQLI IKEEKEKGHN LRDLHKHVVV QINDTHPSLV IPELIRLLMQ EGIRMKEAID
IVSNTTCYTN HTILSEALEK WPRSYLQKVV PHLMPIIEAL DSLVAYIFSN PDVQIIDEQD
RVHMARIDMH YGYSINGVAA LHTDILKNSE LKPFYDIYPD KFNNKTNGIT FRRWLMHCNP
ELANYITSLI GEGWKKDANE LEKLLAYYDN QEVLDHLYDI KQNNKRKLAS YIQKHENIEL
DPNSIFCIQI KRIHEYKRQQ MNALYIIYKY LEIKNGNLPK RPITILFGGK AAPAYYIAKD
IIHLIITLSK LINNDPVVSK YLKVVMVENY NVTYAEQLIP ACDISEQISL ASKEASGTGN
MKFMLNGAIT LGTMDGANVE IAQLVGNDNI YTFGESSQQV IDHYNHHDYS SKTLYQQDEL
IKKLVDFIVS DELLQLGSKE HLQALHNELI NKDWFMTLLD VKNYIETKEH VFDEYENTEK
WKRMSLVNTA KAGFFSSDRT INDYNQDIWK LK
//
