ID A0A095ZH60_9BACT Unreviewed; 853 AA.
AC A0A095ZH60;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:KGF33686.1};
GN ORFNames=HMPREF2137_10640 {ECO:0000313|EMBL:KGF33686.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF33686.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF33686.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF33686.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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:KGF33686.1}.
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DR EMBL; JRNN01000079; KGF33686.1; -; Genomic_DNA.
DR RefSeq; WP_036874288.1; NZ_JRNN01000079.1.
DR AlphaFoldDB; A0A095ZH60; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000029556; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1}.
FT DOMAIN 22..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 853 AA; 98908 MW; 40E07A345F73F3FD CRC64;
MKIKTSNVNA PQWRELTIKS RLPEQLKCLD ELAHNMWFGW NHDARSLFKS LDEKLYEAVG
HNPVLLLERL NYDRKEEIVN DAKLMKRVKD VYAQFRAYMD VKPDKKRPSV AYFCMEYGIN
QILKIYSGGL GMLAGDYLKE ASDSNVDMCA VGFLYRYGYF KQSLSMEGQQ IAQYEAQNFN
SLPIEREIDE NGNPVVVDVP YLDYVVHAYV WRVNVGRIKL YLLDTDNDLN SQFDKSITHS
LYGGDWENRL KQEILLGIGG ILTLKKLGIK KDIYHCNEGH AALCNLQRLC DYVEGGLTFN
QAMELVRASS LYTVHTPVPA GHDYFDEALF GKYMQGYPQR LGITWDEFIG MGRQNPDDHT
EKFCMSTFAC NTSQEVNGVS KLHGWVSQKM FAPIWKGYYP EESHVGYVTN GVHFPTWTST
EFRDIYDKYF DKSFMSDQSN EKIWHAFLKI PDGEIWQTRM MLKKKLVKYI REKFTENWLK
NQGDPSRVMS LLECINPNAL MIGFCRRFAT YKRAHLLFTD IDRLSKIVNN PDRPVLFFFS
GKAHPADGAG QDLIKRIYEI SQRPEFLGKI IFLEDYDMQL ARRLVSGVDI WMNTPTRPLE
ASGTSGEKAE MNGVVNLSVL DGWWVEGYRE GAGWALPQKR TYQNQEYQDQ LDAATIYSLL
ENEIIPMYYN RNEEGYSEQW LDVVKKSVAT IAPHYTMKRQ LDDYYSKFYE KEAARFAELT
ADDAKLAKEI AHWKETVAER WDAIRVVSKD TEFLTTGGET GVEYRLKYVI DEQGLDDAVG
LELVTLKPMP DDDGREVYRV RPFEMIGHEG NQYTFETVVD PDDAGTFKSC VRMFPKHKNL
PHRQDFNYVK WLD
//
