ID A0A0S8KRL3_9CHLR Unreviewed; 850 AA.
AC A0A0S8KRL3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:KPL23589.1};
GN ORFNames=AMJ93_04300 {ECO:0000313|EMBL:KPL23589.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL23589.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL23589.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL23589.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL23589.1}.
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DR EMBL; LJUZ01000042; KPL23589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KRL3; -.
DR PATRIC; fig|1703388.3.peg.3811; -.
DR Proteomes; UP000052016; 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..122
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 850 AA; 96069 MW; CAE9A2F341881EF9 CRC64;
MQPMFSINVV PSLPAELGVL RELAHNLWWS WTPDAIALFR RLDRDAWEES EHNPVRMLGM
VDQAGLEAAA RDDAFLAHME RVNDDFQRYM SAPTTWYDKN HGSQPQPSVA YFCLEFGLTE
CLPIYSGGMG VLAGDYLKSA SDLGVPMVAV GLAYQQGYFR QYLNADGWQG ELYQENDFYT
MPLTLEVRDG TPVTIDVDFP GRQVLARIWR VQVGRVPLYL LDTNVPENRS DDRHITHQLY
GGDGEMRIRQ EILLGIGGVK ALRALGIRSG VCHMNEGHAA LLGIERIRQL VSEHNLTADE
ARQVVTASSV FTTHTSVPAG IDLFDATLVD KYLGQYYDAL GMSRSEFLAL GRKNPGDERE
PLNMAVLALR LAGATNAVSP LHGQVSRRLW QGVWPGVPEW EVPIISIDNG VHTRSWISED
MASLFDRYLG PRWAERPADQ TVWEAVDDIP DEELWRVRER RRARLVAFAR HRLREQLEQR
GAPPPEIVRA TEKLDPDALT IAFARRFALY KRATLLLRRP ERLGEILDNQ ERPVQVIFAG
KAHPQDNPAK ELIRDVIHLT RTNGLQNVVF IEDYDMNVAR YLLQGADLWL NTPVPLREAS
GTSGMKAAAN GALNLSVRDG WWAEAYHPDI GWAIGRGEVY EDHEYQNEVE ADAIYDLLAK
EIVPLFYNRG ADGLPREWIA RMKNAMNAVV PAYNTNRMVI EYVERLYSPA FRRHERLSAD
GFERARGLAE WKARLRQHWA EVQVVGVETD THDQLPVGAE LEVRASVKLG HLSHEDVLVE
TYEGALDANR EITKGRATPM PFVRVEKGVS LFVGKVCCQV SGLRGFTIRV LPRHEDLAHP
FEPRLIAWGP
//
