ID D4GD39_PANAM Unreviewed; 815 AA.
AC D4GD39;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:ADD78864.1};
GN OrderedLocusNames=PANA_3697 {ECO:0000313|EMBL:ADD78864.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78864.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD78864.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78864.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
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}.
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DR EMBL; CP001875; ADD78864.1; -; Genomic_DNA.
DR RefSeq; WP_013027535.1; NC_013956.2.
DR AlphaFoldDB; D4GD39; -.
DR STRING; 706191.PANA_3697; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR GeneID; 57266406; -.
DR KEGG; pam:PANA_3697; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR Proteomes; UP000001702; Chromosome.
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:UP000001702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 662
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 815 AA; 93390 MW; 5535C6FEDBC6AF97 CRC64;
MNTPFTYASP TLTVDALKHS IAYKLMFTIG KDPSIANKHE WLNAALLAVR DRMVERWLRS
NRAQLSQDVR QVYYLSMEFL MGRTLGNALL AMGIYDDLNL ALDEMGLDLA ELMEEENDPG
LGNGGLGRLA ACFLDSLATL GMPGRGYGIR YDYGMFKQNI VDGEQKESPD YWLEYGNPWE
FQRFNTRYKV RFGGRVQHEG AKVRWLETEE ILAMAYDQII PGYDTDSTNT LRLWGAQASN
EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SATVQDILNR
HWMMHRTWNN LADKIAIHLN DTHPVLAIPE LMRLLIDEHK FTWDDAFDVC CQVFSYTNHT
LMTEALETWP VDMIGKILPR HLSIIFEIND FFLKTIQEYY PDDWDLLSRI SIIDENDGRR
VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFSRLFPGR FCNKTNGVTP RRWLALANPP
LSELLDEQIG RNWRTDLSQL SELKSCVDYP AFIEKVAEAK LENKKRLAIW VAKNLDVVID
PNALFDVQIK RIHEYKRQLL NVLHVITRYN RIKADPDAEW VPRVNIFAGK AASAYYVAKH
IIHLINDVAK VINNDPQVKN KLKVVFIPNY SVSLAQIIIP AADLSEQIST AGTEASGTSN
MKFALNGALT IGTLDGANVE MLEHVGKENI FIFGNTTPQV EALRKAGYNP RKYYEEDAEL
HQVLTQLASG VFSPQDPGRY RNLFDLLVNF GDHYQLLADY RSYVDTQDKV DELYRQPDVW
QHRAAMNIAG MGYFSSDRTI QEYADEIWNI SPVRL
//
