ID A0A069PN19_9BURK Unreviewed; 817 AA.
AC A0A069PN19;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BG61_38910 {ECO:0000313|EMBL:KDR38651.1};
OS Caballeronia glathei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR38651.1, ECO:0000313|Proteomes:UP000027466};
RN [1] {ECO:0000313|EMBL:KDR38651.1, ECO:0000313|Proteomes:UP000027466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR38651.1,
RC ECO:0000313|Proteomes:UP000027466};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-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:KDR38651.1}.
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DR EMBL; JFHC01000081; KDR38651.1; -; Genomic_DNA.
DR RefSeq; WP_035937084.1; NZ_JFHC01000081.1.
DR AlphaFoldDB; A0A069PN19; -.
DR STRING; 60547.GCA_000751215_05127; -.
DR Proteomes; UP000027466; 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:UP000027466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 663
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 93482 MW; 803D41117EEDC74D CRC64;
MTSVDLEFDQ LNSTVDALRR SISNRLMYGV GKDSVTAQPR DWLHAAELAV RDRLVARWMR
TTRQQYEQDV KRVYYLSMEF LIGRTFTNAL LALGIYDEVR DALAGLGVDI NTLENLEPDA
ALGNGGLGRL AACFLDSMAT VGIPGFGYGI RYEYGMFRQT IVDGNQVETP DYWLRAGNPW
EFPRPEVVYL VHFGGRTVQY DDRTEWIETE HVNAMAYDTV IPGFATTATN TLRLWSARAT
DEFDLSAFNQ GDYRRAVEAK NTSEHVSRLL YPDDSTQAGR ELRLRQEYFF VSATMQDLIR
RYQRTHSHFG RLAEKVAVHL NDTHPVLAIP ELMRLLVDTH HVPWDKAWKL VQQMFSYTNH
TLMPEALETW DVEMLARLLP RHLEIIFDIN AQFLKQVTEK FGRDVDLIRR ISLVDEYGQR
RVRMAHLAIV ASHKVNGVSK LHSQLMTQNI FSDFARMYPE RFTNVTNGIT PRRWLAQASP
SLSSLIDARL GPRWRTDLFE LGRLREWRDD PEFRQAFHDA KFASKLTLVE RAKREAGAII
DPHALFDLQV KRIHEYKRQL LNILHVIVRY NRIREEPELD WTPRVVMFAG KAASAYKMAK
NIIKLINDVA KKVNADPLIG DRLKVGFIPN YGVSVAELII PAADLSEQIS MAGTEASGTG
NMKLALNGAL TIGTLDGANI EICDAVGREN MFVFGHSTDE IESLRAAGYR PRHIYEHNPE
LKLALDQIRL GHFSPDEPHR FYDIFHTLVD WGDHYMVLAD FDSFDRAQTE VDAKFRDKDA
WTRSAIENVA GMGIFSSDRT IAEYARDIWH VEPLSLG
//
