ID E0IE78_9BACL Unreviewed; 724 AA.
AC E0IE78;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:EFM09432.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:EFM09432.1};
GN ORFNames=PaecuDRAFT_3969 {ECO:0000313|EMBL:EFM09432.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM09432.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM09432.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM09432.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; AEDD01000011; EFM09432.1; -; Genomic_DNA.
DR RefSeq; WP_006039952.1; NZ_AEDD01000011.1.
DR AlphaFoldDB; E0IE78; -.
DR STRING; 717606.PaecuDRAFT_3969; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000005387; 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:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EFM09432.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW Transferase {ECO:0000313|EMBL:EFM09432.1}.
FT MOD_RES 483
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 724 AA; 80520 MW; E5B093C137C2EB85 CRC64;
MPNGEVAYFS AEFGLDESLP IYSGGLGILA GDHIKAAADL NIPLTGVGLF YKKGYFQQQI
NESGWQQQHY PDVDRKASIY PLQPVMDAEE RPIIIDVTIA GRQVHATAWC IRLGSVTLYL
LSTDVDANSD ADRDLTNTLY PSHPDVRISQ EIMLGIGGAR LLAALGIQPA VWHMNEGHSA
FLAFERIRML SAEGVPFETA LEAVKASTVF TTHTPVPAGH DVFSIGMIDH YLGSYYWQLG
ADRARILSLG ELDGVFNMTR LAVSSSSKVN GVSKLHGEVT RELFHRWMPH IPIPDIPVDS
VTNGVHVGTW LADGIKKLYD KHLVPDWAFR TQEPQVWAAV RDIPAHELWE EHQQAKSVMV
QQLGLALASP DENPLIIGFA RRFATYKRAL LIFSDLERLA RLLSDPERPV CLVFAGKAHP
ADEPGKELIR KIVELSREER FKGRVHIVEN YAMDKAKKLV QGVDVWLNTP VKPMEASGTS
GQKAAMNGVI NCSVLDGWWV EGYNGRNGWA IDGDTSGDPD QQAQQDSDML YRLLEEQIIP
LYYERGDTAI PTEWVNMMKE SICSLTPVYN THRMVSDYWN QIYVPAMARG RRFAADGLEI
ASRVGAYKQF IRDNWSAVHV KKVELLDADG GSNGRQKSIF RAEIALGAIW SKDVRVEAVG
SDGRSGIWRS KLEPVHQLTA GQFVYEGASP DIPIDVWRAN VNVRVTPISP DFANDFELEL
GAWG
//
