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Database: UniProt/TrEMBL
Entry: A0A0P0GMD0_9BACE
LinkDB: A0A0P0GMD0_9BACE
Original site: A0A0P0GMD0_9BACE 
ID   A0A0P0GMD0_9BACE        Unreviewed;       854 AA.
AC   A0A0P0GMD0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Maltodextrin phosphorylase {ECO:0000313|EMBL:ALJ62402.1};
DE            EC=2.4.1.1 {ECO:0000313|EMBL:ALJ62402.1};
GN   Name=malP_2 {ECO:0000313|EMBL:ALJ62402.1};
GN   ORFNames=BcellWH2_05199 {ECO:0000313|EMBL:ALJ62402.1};
OS   Bacteroides cellulosilyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=246787 {ECO:0000313|EMBL:ALJ62402.1, ECO:0000313|Proteomes:UP000061809};
RN   [1] {ECO:0000313|EMBL:ALJ62402.1, ECO:0000313|Proteomes:UP000061809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH2 {ECO:0000313|EMBL:ALJ62402.1,
RC   ECO:0000313|Proteomes:UP000061809};
RX   PubMed=26430127;
RA   Wu M., McNulty N.P., Rodionov D.A., Khoroshkin M.S., Griffin N.W.,
RA   Cheng J., Latreille P., Kerstetter R.A., Terrapon N., Henrissat B.,
RA   Osterman A.L., Gordon J.I.;
RT   "Genetic determinants of in vivo fitness and diet responsiveness in
RT   multiple human gut Bacteroides.";
RL   Science 350:AAC5992-AAC5992(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}.
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DR   EMBL; CP012801; ALJ62402.1; -; Genomic_DNA.
DR   RefSeq; WP_029428226.1; NZ_CP012801.1.
DR   AlphaFoldDB; A0A0P0GMD0; -.
DR   KEGG; bcel:BcellWH2_05199; -.
DR   PATRIC; fig|246787.4.peg.5364; -.
DR   Proteomes; UP000061809; 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:ALJ62402.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000313|EMBL:ALJ62402.1}.
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;  98275 MW;  3C0C1E56A3D4224A CRC64;
     MKIKVSNVNT PNWKDVNVKS HVPAELEKLS ELAHNIWWSW NYEATELFKD LDPALWKEVG
     HNPVLLLERM SYAKLEALAN DKVILKRMND VYAMFRTYMD VKPDQKRPSV AYFSMEYGLN
     QVLKIYSGGL GVLAGDYLKE ASDSNVDLCA VGFLYRYGYF TQTLSMDGQQ IANYEAQNFG
     QLPIERVMDE NGNQVIVDVP YLDYFVHAFV WRVNVGRISL YLLDTDNEMN SEFDRPITHQ
     LYGGDWENRL KQEILLGIGG ILTLKKLGIK KDVYHCNEGH AALINVQRIC DYVAEGLSYD
     QAIELVRASS LYTVHTPVSA GHDYFDEGFF GKYMGGYPAR MGISWEDLMD LGRNNPGDKG
     ERFCMSVFAC NTSQEVNGVS WLHGKVSQEM FSTIWKGYFP EEMHVGYVTN GVHFPTWSAT
     EWKHLYAANF DENFLYDQSN PKIWEAIYNV PDEKIWETRM ALKNKLIDYV RKQYRETWLK
     NQGDPSRIVS LMDKINPNAL LIGFGRRFAT YKRAHLLFTD LDRLAKIVNN PDYPVQFLFT
     GKAHPHDGAG QGLIKRIIEI SRRPEFLGKI IFLENYDMQL ARRLVSGVDI WLNTPTRSLE
     ASGTSGEKAL MNGVVNFSVL DGWWLEGYRE GAGWALTEKR TYQNQEHQDQ LDAATIYSIL
     ETEILPLYYA RNKKGYSEGW VKTIKNSIAQ IAPHYTMKRQ LDDYYSKFYT KLAKRFSALS
     ANDNAKAKEI AAWKEEVVSK WDSIEVVSYD KCEELLQATI ESGKEYTITY VIDEKGLNDA
     IGLELVTTYT AGDGKQHVYS VEPFSVVKKE GNLYTFQVKH KLENAGSFKV SYRMFPKNSD
     LPHRQDFCYV RWFV
//
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