ID S0LDL2_9ENTE Unreviewed; 813 AA.
AC S0LDL2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=I573_00117 {ECO:0000313|EMBL:EOT87062.1};
OS Enterococcus sulfureus ATCC 49903.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1140003 {ECO:0000313|EMBL:EOT87062.1, ECO:0000313|Proteomes:UP000015961};
RN [1] {ECO:0000313|EMBL:EOT87062.1, ECO:0000313|Proteomes:UP000015961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49903 {ECO:0000313|EMBL:EOT87062.1,
RC ECO:0000313|Proteomes:UP000015961};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sulfureus ATCC_49903 (PacBio/Illumina
RT hybrid assembly).";
RL Submitted (MAR-2013) 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:EOT87062.1}.
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DR EMBL; ASWO01000001; EOT87062.1; -; Genomic_DNA.
DR RefSeq; WP_016184610.1; NZ_KE136393.1.
DR AlphaFoldDB; S0LDL2; -.
DR STRING; 1140003.OMY_00118; -.
DR PATRIC; fig|1140003.3.peg.116; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000015961; 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:UP000015961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 813 AA; 93312 MW; CA35C06B09E456C6 CRC64;
MTISKELFKE KFMDMLTEKY ALSVEEASPY DLYTTLATLI RATYAKDWGI TRRAYNTTHE
KQVYYFSIEF LPGRMMKSNL LNMGWLDTVE ASLKDLGIDL EDILEIEPDM ALGNGGLGRL
ASCFMDSIAS EGLPGNGNGI RYKYGLFKQK FIDGYQVELP NEWLSRGNTW EVRRDSKAVT
VKFNGHAYLK ELEDGSLVPI HENPTVVRAI PYDTGMVGYQ NGTVNTLRLW DAEIPLEEEI
NYRSIQQRRE IEDLTSVLYP DDSNEAGRRL RLMQEYFFVS AGTQSIIRHF KANGYNLNNI
DEYVAIHIND THPAMCVPEF MRILVDEEQM NWERAWALTI KVMSYTNHTI LAEALEKWPV
EMLRSVQPRI YQIIEEIDRR FVEQMTGTID WGIIERTRII SNGIVHMAHL AIIGSHSTNG
VAKLHSDLLK NVVLHDFYRL YPSRFNNKTN GIAERRWMQL ANPTLSHLLD ETIGTSWRFE
ASDLYLLMNY KDDKKVLHAL AKAKQVNKTR LAKFIEKETG VIVNDHAIFD VQIKRLHAYK
RQLLNLLHII KLYLDLKEDP KKKIQPRVFI FGAKAAPSYH YAKAIIKVIN ELANLINNDE
SIKDQLKIVF LENYSVSLAE KIIPAADVSE QISLASKEAS GTSNMKLMLN GAITLATLDG
ANIEIRDAVG DDNIVIFGLT EAEVYAYYEQ ANYRAFEYYE SSVELRKVID ALIDGTIPNS
SQEGIEIYDS LLKYNDEFFV LRDFADYVAA QEKVAHLYSD QEKWLKMSLI NIANAGRFSA
DDTVKKYAED IWRIKPNKTP QQVKDETHDS YSI
//
