ID B2JWR5_PARP8 Unreviewed; 832 AA.
AC B2JWR5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Bphy_6361 {ECO:0000313|EMBL:ACC75392.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OG Plasmid pBPHY01 {ECO:0000313|EMBL:ACC75392.1,
OG ECO:0000313|Proteomes:UP000001192}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC75392.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RC PLASMID=Plasmid pBPHY01 {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001045; ACC75392.1; -; Genomic_DNA.
DR AlphaFoldDB; B2JWR5; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; bph:Bphy_6361; -.
DR HOGENOM; CLU_010198_1_1_4; -.
DR Proteomes; UP000001192; Plasmid pBPHY01.
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}; Plasmid {ECO:0000313|EMBL:ACC75392.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 675
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 832 AA; 93434 MW; 76BBE56E89B65C9F CRC64;
MATVAFPTKL PGTDSARSAM DADALRRGVL DNLICLQARP PAIATPHDWY MALAYSVRDR
MLARWAATIQ TYAAQELRVA CYLSAEFLIG PQLGNNLVNL GIEDNARAAM QSLGQDLDSL
LALEEEPGLG NGGLGRLAAC YLDSLATLEI PSVGYGIRYE FGIFDQEIHN GCQVEVTDKW
LQKGNPWEIV RPNVAYYVAF GGHAESGVDE QGRYTVRWMP ARMVKGVACD TPMLGFRVNT
CNTLRLWKSE AIESFDLQDF NAGDYYQAVQ EKVISETLSK VLYPNDEPEA GKRLRLAQQY
FFVSCSLQDM LRLLDLKGEP IARFADMFTV QLNDTHPSIA VAELMRLLVD VRSVPWDDAW
ATTCRALAYT NHTLLPEALE TWGLPLFSSL LPRPLEIIYE INRRFLELVR RKYPGDEARV
ARMSLIDESG EKRVRMAHLS TIGSHAVNGV AQLHSTLLRQ TVLRDFAELW PERFLNVTNG
VTPRRFMLLS NPGLASLLDE TVGKGWVTDL TRLRTLEAFA DNLAFQQKWR DVKLANKKML
AERIGHVTRI AVDPDALFDI QVKRIHEYKR QHLNALYIIT LYQRLRRNIE QGVVPRCFIF
GGKAAPGYAM AKLMIRLITG IAEVVNNDAS MKGRLKVVFY PDFNVKNAHF IYPAADLSEQ
ISTAGKEASG TGNMKFMMNG ALTIGTLDGA NIEIRDEAGS DNFFLFGLTA SQVDSVKREG
YRPAVHVERN EELRETLGLI ADGYFSRGDR QVFRPLVDNL LNADPFLVLA DYADYVACQE
RVSSAWQDPV RWTRMSILNT ARSGKFSSDR AIGEYCERIW TISPVRIALD RG
//
