ID   D6D4C5_9BACE            Unreviewed;       854 AA.
AC   D6D4C5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Alpha-glucan phosphorylases {ECO:0000313|EMBL:CBK65327.1};
DE            EC=2.4.1.1 {ECO:0000313|EMBL:CBK65327.1};
GN   ORFNames=BXY_00190 {ECO:0000313|EMBL:CBK65327.1};
OS   Bacteroides xylanisolvens XB1A.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK65327.1, ECO:0000313|Proteomes:UP000008795};
RN   [1] {ECO:0000313|EMBL:CBK65327.1, ECO:0000313|Proteomes:UP000008795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB1A {ECO:0000313|EMBL:CBK65327.1,
RC   ECO:0000313|Proteomes:UP000008795};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Bacteriodes xylanisolvens XB1A.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK65327.1, ECO:0000313|Proteomes:UP000008795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB1A {ECO:0000313|EMBL:CBK65327.1,
RC   ECO:0000313|Proteomes:UP000008795};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929033; CBK65327.1; -; Genomic_DNA.
DR   RefSeq; WP_009040972.1; NC_021017.1.
DR   AlphaFoldDB; D6D4C5; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GeneID; 69480558; -.
DR   KEGG; bxy:BXY_00190; -.
DR   PATRIC; fig|657309.4.peg.10; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_015112_0_0_10; -.
DR   Proteomes; UP000008795; Chromosome.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
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   Glycosyltransferase {ECO:0000313|EMBL:CBK65327.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000313|EMBL:CBK65327.1}.
FT   DOMAIN          22..123
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         608
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   854 AA;  98468 MW;  887DA31E5E23FB4E CRC64;
     MKIKVSNVNT PNWKEVTVKS RIPEELEKLS EIARNIWWAW NFEATELFRD LDPELWKECG
     QNPVLLLERM SYEKLEALAK DKVILRRMNE VYTKFRDYMD VKPDEQRPSI AYFSMEYGLS
     SVLKIYSGGL GVLAGDYLKE ASDSNVDLCA VGFLYRYGYF TQTLSMDGQQ IANYEAQNFG
     QLPIERVMDA NGQPLIVDVP YLDYFVHANV WRVNVGRISL YLLDTDNEMN SEFDRPITHQ
     LYGGDWENRL KQEILLGIGG ILTLKALGIK KDVYHCNEGH AALINVQRIC DYVATGLTFD
     QAIELVRASS LYTVHTPVPA GHDYFDEGLF GKYMGGYPSR MGITWDDLMD LGRNNPGDKG
     ERFCMSVFAC NTSQEVNGVS WLHGKVSQEM FSSIWKGYFP EESHVGYVTN GVHFPTWSAT
     EWKELYFKYF NENFWFDQSN PKIWEAIYNV PDEEIWKTRM TMKNKLVDYI RKSFRDTWLK
     NQGDPSRIVS LMDKINPNAL LIGFGRRFAT YKRAHLLFTD LDRLSKIVNN PDYPVQFLFT
     GKAHPHDGAG QGLIKRIIEI SRRPEFLGKI IFLENYDMQL ARRLVSGVDI WLNTPTRPLE
     ASGTSGEKAL MNGVVNFSVL DGWWLEGYRE GAGWALTEKR TYQNQEHQDQ LDAATIYSIL
     ETEILPLYYA RNKKGYSEGW IKVVKNSIAQ IAPHYTMKRQ LDDYYSKFYC KLAKRFQTLA
     ANDNAKAKEI AAWKEDVVAK WDAIEIVSCD KVEDLKNGDI ESGKEYTITY VIDEKGLNDA
     VGLELVTTYT TADGKQHVYS VEPFSVIKKE GNLYTFQVKH SLSNAGSFKV SYRMFPKNPE
     LPHRQDFCYV RWFI
//