ID A0A417YXP7_9BACI Unreviewed; 799 AA.
AC A0A417YXP7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=D1B31_05970 {ECO:0000313|EMBL:RHW42175.1};
OS Neobacillus notoginsengisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1578198 {ECO:0000313|EMBL:RHW42175.1, ECO:0000313|Proteomes:UP000284416};
RN [1] {ECO:0000313|EMBL:RHW42175.1, ECO:0000313|Proteomes:UP000284416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30743 {ECO:0000313|EMBL:RHW42175.1,
RC ECO:0000313|Proteomes:UP000284416};
RX PubMed=28786779; DOI=10.1099/ijsem.0.001975;
RA Zhang M.Y., Cheng J., Cai Y., Zhang T.Y., Wu Y.Y., Manikprabhu D., Li W.J.,
RA Zhang Y.X.;
RT "Bacillus notoginsengisoli sp. nov., a novel bacterium isolated from the
RT rhizosphere of Panax notoginseng.";
RL Int. J. Syst. Evol. Microbiol. 67:2581-2585(2017).
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:RHW42175.1}.
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DR EMBL; QWEG01000003; RHW42175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417YXP7; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000284416; 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 645
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 799 AA; 92209 MW; 4B88E3B023D52C8E CRC64;
MFSSVPEFKE AYIRKLEMAY GTNFEESSRR EQFQTLGILI REYVSKNWIK TNEMYRTSGK
KQVYYLSIEF LLGRLLRHNL MNLGVEDVVG KGLKELGIEL DDLEEFEADA GLGNGGLGRL
AACFLDSLAS LSLPGHGCGI RYKHGLFEQT IVDGYQVELP EQWLKHGHVW EVRKGDEAEE
IPFWGEVEST VENGRLVFKH INAEIVTAVP YDMPVLGHHN KTVNTLRLWD AEPSKFTANT
DILKYKKETE AICEFLYPDD THDEGKILRL KQQYLLVAAS LRAITKSFKK KNRSILELHE
HTSIHINDTH PALAVPELMR ILMDDEGLGW DEAWHLTVNT LSYTNHTTLS EALERWPVRI
FKTLLPRIYM IVEEINERFC KGLWDRYPGD WNRIENMAII AHDEVRMAPL SIVGSHSING
VAKLHTDILK EREMNLYYQI FPERFNNKTN GITHRRWLMK ANPRLTDLIT DSIGPDWVND
TMQLEKLLQF RDSSFLEKMA EIKHGNKERL ASRILEKTGI AVDPHSIFDV QVKRLHAYKR
QLLNVLHIMY LYNRIKENPH YDMYPRTFIF GAKASPGYYF AKKVIKLINS VADKVNHDPE
VNKKMKVVFL ENYRVSLGEE IFPAADVSEQ ISTASKEASG TGNMKFMMNG ALTVGTLDGA
NVEITELVGR ENIFLFGLSA AEVLEYQRNG GYHAQEYYHY DRRIRTVVDQ LVNGFFPDTY
NEFTEIYDSL LASNDQYFVF RDFSSYADIQ EEIGRQFGDQ TAWNKKSLIN IAKSGFFSSD
RTILEYADDI WHAEPVIIK
//
