ID J2Y0S8_9PSED Unreviewed; 816 AA.
AC J2Y0S8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PMI38_05322 {ECO:0000313|EMBL:EJN30580.1};
OS Pseudomonas sp. GM84.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144340 {ECO:0000313|EMBL:EJN30580.1, ECO:0000313|Proteomes:UP000007504};
RN [1] {ECO:0000313|EMBL:EJN30580.1, ECO:0000313|Proteomes:UP000007504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM84 {ECO:0000313|EMBL:EJN30580.1,
RC ECO:0000313|Proteomes:UP000007504};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN30580.1}.
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DR EMBL; AKJC01000364; EJN30580.1; -; Genomic_DNA.
DR RefSeq; WP_008100943.1; NZ_AKJC01000364.1.
DR AlphaFoldDB; J2Y0S8; -.
DR PATRIC; fig|1144340.3.peg.5099; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000007504; 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 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 816 AA; 91798 MW; 78647BBA0CA2FECF CRC64;
MSQEPKARDA EVADFRAAVL DKLTYAVGKD PEHAFDHDWF EAIALAARDH MVDHWMDHTR
RAYRRSQKRV YYLSLEFLIG RLLYDSLSNL GLLDVAREAL QGLDVDLERI RLLEPDAALG
NGGLGRLAAC FMESMSTLGI AAHGYGIRYE HGLFRQAVVD GWQQEQTENW LDFGNPWEFE
RAEVIYPISF GGSVETLNDA DGAQRQVWTP GETVRAVAYD TPVVGWRGAS VNTLRLWRAR
ALEELHLERF NAGDHLGAVA EVARAESISR VLYPADSTEA GQELRLRQEY FFVSASLQDL
LRRHLNMHKD LLNLPDAAAI QLNDTHPSIA VAELMRLLVD QHEIPWEKAW ELTVGTLAYT
NHTLLPEALE TWPVALMERM LPRHMQIIYL INAFHIDALR AKGLHDFDVL RAVSLIEEEN
GRRVRMGNLA FLGSHSVNGV SALHSQLMKS TVFAELHKLY PKRINNKTNG ITFRRWLYLS
NPQLTAMLVE AVGPELLDDP QGRLADLVPF AEKSSFRKAF AAQRLHSKRA LASIIQDRVG
VTVNPEALFD VQVKRIHEYK RQLLNLLHTV ALYQAMRNDP GTDWVPRVKI FAGKAAASYH
QAKLIIKLAN DIARVVNNDP TVRGLLKVVF LPNYNVSLAE SIIPAADLSE QISTAGYEAS
GTSNMKFGLN GALTIGTLDG ANVEMCEHVG ADNMFIFGLT AQQVEARKRA NDFGAGAAIA
SSHRLNDVLQ AIRSGVFSSD DPGRYAGLID GLVAYDRFLV CADFDAYWDA QRRVEELWHT
PQEWWRMAVL NTARMGWFSS DRTIREYATE IWKALD
//
