ID A0A0F2PW60_9FIRM Unreviewed; 845 AA.
AC A0A0F2PW60;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:KJS17586.1};
GN ORFNames=VR69_04450 {ECO:0000313|EMBL:KJS17586.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS17586.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS17586.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS17586.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS17586.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LADO01000017; KJS17586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PW60; -.
DR STRING; 1629717.VR69_04450; -.
DR PATRIC; fig|1629717.3.peg.1831; -.
DR Proteomes; UP000033446; 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; 3.
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 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 601
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 845 AA; 97387 MW; 24B360E79C8E4CF0 CRC64;
MYAFRTISVK PKLPEEIKRL KELAYNFWFS WNTNARALFR KINETLWDDV NHNPVKFLLH
VNEEDLEDIA QNDEYIKDYN RVFADFDRYM NRKTWFEKIY PQYNTAPVAY FSAEFGLHES
HPIYSGGLGL LAGDHLKSAS DLGIPLVGVG LLYRHGYFNQ AINRDGSQVA QYLHHTFSER
PIIPVADGKE KLISVEMSGR TVYAKVWKCL VGRITLYMLD SNIPQNSLED RKITDQLYGG
DRETRISQEI LLGIGGVKAL RLEGINPAAW HINEGHAAFL ILERIRELVA GGLSFETARE
IVSSNTLFTT HTPVPAGHDL FSAEQIERYL GNLYEQLNIE REDLLELGWD EERKEFNMTL
LALRISSYCN GVSKLHGEVT KEMFSYLYPG VPVEEVPVHY ITNGVHTGSW LAQEIKDLYY
IYLGEDWHEN ITDRNVWKKV REIPDNLLWA VHQSLKEKMI SFARKNLKKQ RLRNQEPTNR
VKEVEQFLRP NVFTIGFARR FATYKRAGLL FLDRERLEKL INNPHMPVQI VFAGKAHPAD
TAGQELISQV YSLSNEEPFK GKIVFLENYD IHMARILVQG VDIWLNTPRR PMEASGTSGQ
KAAANGVLNL SILDGWWPEG YNGENGFAIG EKKHYDSEDM QDRDDCYSLY ATLEEKVLPA
YYGLDGAFPR EWLRMMKNSI VTISPVFSTE RMVQEYSERF YIPSIKRWSY FTEDNYSAAR
RFKDFKQAIT ENWQHVSINR VETNANREIN VGSLLKITAY VHLGPLCPDD VDLEVVYGNI
TDRGLTNISI SPMTYEDSGE DGAHRYLGQL ILPQGTYGYT VRVIPGHQDF VRKFELPLII
WSGNF
//
