ID A0A3N2KUU4_9BACT Unreviewed; 852 AA.
AC A0A3N2KUU4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Alpha-glucan family phosphorylase {ECO:0000313|EMBL:ROS88735.1};
GN Name=glgP {ECO:0000313|EMBL:ROS88735.1};
GN ORFNames=EEL39_06320 {ECO:0000313|EMBL:ROS88735.1};
OS Muribaculaceae bacterium Isolate-080 (Janvier).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486468 {ECO:0000313|EMBL:ROS88735.1, ECO:0000313|Proteomes:UP000277934};
RN [1] {ECO:0000313|EMBL:ROS88735.1, ECO:0000313|Proteomes:UP000277934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-080 (Janvier) {ECO:0000313|Proteomes:UP000277934};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-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:ROS88735.1}.
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DR EMBL; RIBG01000004; ROS88735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2KUU4; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000277934; 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:UP000277934}.
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; 97777 MW; B921E6A75E31F1E7 CRC64;
MKLPVSKTNA PVWRDITVKS VLPEALKPLE TLSRNLWWVW NSAAKNLFRD LDADLWRATG
ENPVMLLQQL SNERLEEIMN DPEMMERIKV VFDMFNDYMS KPMRKDIPSV SYFSMEYGLC
NCLKIYSGGL GVLAGDYIKE ASDSCVDMTA IGFLYRYGYF TQSLSVDGQQ IANYEPQNFN
QLPIEQMTDG NGHPMILEVP FPGRIIYSHI WRVNVGRMKL YLLDTDFDMN SEWDRPITHQ
LYGGDWENRI KQEYLLGIGG VLALKKLGIH NTIYHANEGH AALLNLQRLV DYVEKGLDFT
TALELVRSSS LYTVHTPVPA GHDYFDEGLA HKYLNEFPGR LGITWQDLMN MGRENPDSQD
RFSMSVFALN TCQEANGVSW LHGEVSKKMF AGVWKGYSWE ESHVGYVTNG VHMPTWAASE
WKSFYAEKLG DQVFSHQSDP KAWEGIFKVK DEEIWNMRTT MKNKFINFVK RDFKAKWLAN
QGDPSAVIKI LERINPNALI IGFARRFATY KRAHLLFTDL DRLARIVNNE QFPVQFIFSG
KAHPADGAGQ GLIKRITEIS RMPQFQGKII FLEDYNMIVA KRLVTGVDIW LNTPTRPLEA
SGTSGEKAEM NGVLNFSVLD GWWYEGYRLD EKAGWALTDK RTFTDQSQQD KLDAATIYSM
LENEIIPLYF AKNSKGYSPE WIQYIKRSIG HIAPQYTMQR MIEDYIERFY EPEAKRFDKI
SADSFKLAKE IAAWKEKVAA AWDGVKVLEV STDRDLSQHT NSGEAFTTTI KIDANGLADD
LALELVIDKV HDNQESRVGS VPFKVVSKDG NIVTFQLADK LRDPGVFRYS YRLYPSNPEL
PHRQDFAFVR WI
//
