ID A0A2V1IJY5_9BACT Unreviewed; 852 AA.
AC A0A2V1IJY5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Alpha-glucan family phosphorylase {ECO:0000313|EMBL:PWB02238.1};
GN ORFNames=C5O23_07205 {ECO:0000313|EMBL:PWB02238.1};
OS Duncaniella muris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Duncaniella.
OX NCBI_TaxID=2094150 {ECO:0000313|EMBL:PWB02238.1, ECO:0000313|Proteomes:UP000244905};
RN [1] {ECO:0000313|Proteomes:UP000244905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103720 {ECO:0000313|Proteomes:UP000244905};
RA Clavel T., Strowig T.;
RL Submitted (FEB-2018) 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:PWB02238.1}.
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DR EMBL; PUEC01000014; PWB02238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1IJY5; -.
DR Proteomes; UP000244905; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000244905}.
FT DOMAIN 22..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 607
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 852 AA; 97714 MW; 65BFCBD3CF99C051 CRC64;
MKLPVSKTNA PVWRDITVKS VLPEALKPLE TLSRNLWWVW NSAAKNLFRD LDPDLWRATG
ENPVMLLQQL SSERLEEVMN DADMMDRIKN VFAMFNSYMA KPMRKDIPSV SYFSMEYGLC
NCLKIYSGGL GVLAGDYIKE ASDSCVDMTA IGFLYRYGYF TQSLSVDGQQ IANYEPQNFN
QLPIEQVTDE NGHPLILEVP YPGRIIYSHI WRVNVGRMKL YLLDTDFDMN SEYDRSITHQ
LYGGDWENRI KQEYLLGIGG VLALKKLGIS NTIYHANEGH AALLNLQRLV DYVESGLDFN
TSLELVRSSS LYTVHTPVPA GHDYFDEGLA HKYLNEFPAR LGISWQDLMN MGRENPDSQD
RFSMSVFALN TCQEANGVSW LHGEVSKKMF AGVWKGYSWE ESHVGYVTNG VHMPTWAASE
WKAFYTEKLG EQVFDHQSDP KAWEGIFKAK DEEIWEMRTT MKNKFINFVK RDFKAKWLAN
QGDPSAVIKI LEKINPNALI IGFARRFATY KRAHLLFTDL DRLARIVNNE QFPVQFIFSG
KAHPADGAGQ GLIKRIIEIS RMPQFQGKII FLEDYNMVVA KRLVTGVDIW LNTPTRPLEA
SGTSGEKAEM NGVLNFSVLD GWWYEGYRLD EKAGWALTDK RTYTDQGQQD KLDAATIYSM
LENEIIPLYF AKNSKGYSPE WIQYIKRSIG HIAPQYTMQR MIEDYIDRFY LPESKRFEKL
SADGDKLAKE LAAWKEKVAA AWDGIQVLEV STNEDLNHNN HSGQKFVTTV KIEANGLADD
LGLELVVDKV HDNQEHRVDT IPFKVVAKEG NTVTFQLEDK LRDPGVFRYS YRLYPSNALL
PHRQDFAFVR WI
//