ID A0A1L8QR44_9ENTE Unreviewed; 817 AA.
AC A0A1L8QR44;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=RU93_GL000441 {ECO:0000313|EMBL:OJG09991.1};
OS Enterococcus aquimarinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG09991.1, ECO:0000313|Proteomes:UP000182149};
RN [1] {ECO:0000313|EMBL:OJG09991.1, ECO:0000313|Proteomes:UP000182149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG09991.1,
RC ECO:0000313|Proteomes:UP000182149};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG09991.1}.
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DR EMBL; JXKD01000011; OJG09991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8QR44; -.
DR STRING; 328396.RU93_GL000441; -.
DR Proteomes; UP000182149; 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 Reference proteome {ECO:0000313|Proteomes:UP000182149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 93260 MW; 0118996054268CB1 CRC64;
MFQSVFVIKG GKGMITKKQL IKELRKNVQE MYAIEIEDAT EQELFFSLGT TIKGIYNKNW
QKTWNNYLAE EQKQVYYFSI EFLPGKLLKS NLLNLGILEV VRESLAEFSV DLEDLAAVEK
DMALGNGGLG RLASCFMDAI ASSGLPGNGN GIRYDYGLFK QQFVDGYQVE LPDEWLRNGN
VWEIRRDSKA VNVHFGGDVY MQPKSNGKLG VVAENETILR AVPYDTGMVG FENGIVNTMR
LWSVEIPSSE EGKYRSIEER RVFEDLTAVL YPDDSNARGR LIRLAQEYFF VSAGIQSIIR
YFKKLNHPWH VLSEKVAIHI NDTHPALCIP ELMRILMDEY EVSWEQAWDL TSKVMSYTNH
TIMAEALEKW PTYLMKRSLP RMYQIIKEID RRYVVSMSGI HDAALIERTR IIQGEDIHMA
NLAIIGSHST NGVAKLHSDL LKAVVLHDFY TIYPERFNNK TNGIAQRRWL QLSNEPLSRV
LDETIGKSWR HEPADLKLLM NYQNDPIVLE KLAKAKQQKK EELAKYIQET TGIIVNPTAI
FDVQIKRLHA YKRQLLNLLH ILKLYFEIKE NPQASIYPRV FIFGAKAAPS YAYAKSIIKV
INEVANLVNH DQTIGDKLKI VFLPNYNVSL AEKIIPAADV SEQISLASKE ASGTSNMKLM
LNGAITIATL DGANVEIRDA VGDENIYIFG LTEAEVYAYY ENKNYSAREV YETNPIVHRV
LNAFVDGSIP NIEREGQEIV DSLLLYNDEY FLLRDFDAYC EAQARLNQAY QDATHWQKCS
LINIANAGTF SADKTVKQYA EDIWQIEPLF AHTHQGR
//
