ID   A0A0Q7J0I2_9BACL        Unreviewed;       851 AA.
AC   A0A0Q7J0I2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:KQX45462.1};
GN   ORFNames=ASD40_20575 {ECO:0000313|EMBL:KQX45462.1};
OS   Paenibacillus sp. Root444D2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX45462.1, ECO:0000313|Proteomes:UP000051657};
RN   [1] {ECO:0000313|EMBL:KQX45462.1, ECO:0000313|Proteomes:UP000051657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root444D2 {ECO:0000313|EMBL:KQX45462.1,
RC   ECO:0000313|Proteomes:UP000051657};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX45462.1, ECO:0000313|Proteomes:UP000051657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root444D2 {ECO:0000313|EMBL:KQX45462.1,
RC   ECO:0000313|Proteomes:UP000051657};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQX45462.1}.
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DR   EMBL; LMEO01000052; KQX45462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7J0I2; -.
DR   STRING; 1736538.ASD40_20575; -.
DR   Proteomes; UP000051657; 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:UP000051657}.
FT   DOMAIN          12..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   851 AA;  97143 MW;  61301A444B82B917 CRC64;
     MQIAFPQDAK HLPPAIERLN ELSFNLWFSW NHDALQLFAQ MDPVKWDQCG HNPVLLLHLL
     DNSQIEALSG NQDFAANYQQ VIAKFDAYMN GTTWFQEKHP DQGYVQIAYF SAEFGFHESL
     PIYSGGLGIL AGDHTKSASD LGIPLIGVGL LYKKGYFTQK IDTSGGQQSE LYPYDFSKLP
     IEPVQQNGQQ LTVSIDMPGR AITLQVWRVR VGRNSIYLLD ADHEANNTAD KELTAQLYGG
     NQDTRIAQEM VLGIGGVKAL RLLNIYPNVY HINEGHAAFL TLERLKELLH LGLPFHVAVE
     TVRSATVFTT HTPVPAGHDT FSIEMVEHYL GPLLSELSRH KQDIVALGLD HHTGQFNMTH
     LAMNTAGLRN GVSKLHGQVS REMFKEFHGH IDASEVPISS ITNGVHMDTW TAPQWKELLD
     RFLPGSWREE QANKHQWAQI EVIPDESIWK VHQQLKENLV RYARRNLLEQ RKRNGESEER
     IEEVRQYLNP KALTIGFARR FATYKRANLI FNDLYRLKKL INDPDRPVQF IFAGKAHPAD
     YPGQELIREI YRVSQMKEFV GKIVILENYD MNMARYLVQG VDVWLNNPRR PLEASGTSGQ
     KAAMNGVLNF SVLDGWWEEG YNGTNGWAIG STGAADWAAQ EKENTQAIYH ILEKEIIPLY
     YNQGALPHQW ISRMKRSIQS LSPVYNTHRM VQDYTELTYL PTAQRARLFV SNHYEVATKV
     ADYKQFIRSN WYHVKIIGID DRSAKLSTEV PLNEIKPSTK EITTQVHFGP IWPQDTAVEV
     IYYEENGETW EQKIIPMVPI GELIEQMQSY KATIPSHLIH GPHFSIRVRP ISSNFAHSFE
     LSLVTTTLSW Q
//