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Database: UniProt
Entry: A0A2V1IJY5_9BACT
LinkDB: A0A2V1IJY5_9BACT
Original site: A0A2V1IJY5_9BACT 
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
//
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