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Database: UniProt
Entry: A0A2Z4FHD1_9DELT
LinkDB: A0A2Z4FHD1_9DELT
Original site: A0A2Z4FHD1_9DELT 
ID   A0A2Z4FHD1_9DELT        Unreviewed;       712 AA.
AC   A0A2Z4FHD1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AWV88128.1};
DE   SubName: Full=Starch phosphorylase {ECO:0000313|EMBL:TDP77251.1};
GN   ORFNames=DFR33_101151 {ECO:0000313|EMBL:TDP77251.1}, DN745_01765
GN   {ECO:0000313|EMBL:AWV88128.1};
OS   Bradymonas sediminis.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX   NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV88128.1, ECO:0000313|Proteomes:UP000249799};
RN   [1] {ECO:0000313|EMBL:AWV88128.1, ECO:0000313|Proteomes:UP000249799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA350 {ECO:0000313|EMBL:AWV88128.1,
RC   ECO:0000313|Proteomes:UP000249799};
RA   Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT   "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT   member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT   fam. nov.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TDP77251.1, ECO:0000313|Proteomes:UP000294609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28820 {ECO:0000313|EMBL:TDP77251.1,
RC   ECO:0000313|Proteomes:UP000294609};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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; CP030032; AWV88128.1; -; Genomic_DNA.
DR   EMBL; SNXT01000001; TDP77251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4FHD1; -.
DR   KEGG; bsed:DN745_01765; -.
DR   OrthoDB; 7229284at2; -.
DR   Proteomes; UP000249799; Chromosome.
DR   Proteomes; UP000294609; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249799}.
FT   DOMAIN          11..115
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         600
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   712 AA;  80516 MW;  FB90FB371FAD7906 CRC64;
     MTTKTKYPLV RKLEALAHNL RWCWQPDGWR VFRDLDAQLW HKCSHNPIAF LEEWEPAELE
     ARAQRTGLAG RIHNGHQKLV DYLARRGPEA RMSAGPLHTR PVAYFCAEFG IHESLPIYSG
     GLGILAGDHM KAASDLSIPL VGVGLFYPLG YFQQSIDEDG WQQEHYGRTD VAKLPLTKVV
     DADGAPLEIE IDMGSERIKA YVWRAPVGRN ELLMLDSDVP GNNPDDRLLT SQLYGGDRRM
     RIRQEILLGV GGVRALAALG IDPAVYHLNE GHSAFATFEL AARYMEREGI FFEEARDKVA
     RQTVFTTHTP VPAGHDRFHI ELFEEMLGWM RPRLGIDHRE FHGFGRIDLN NPNESFCMTV
     LALKMSRYRN GVSNLHGEVS RQMWRDLWPH GELKDVPIGH ITNGVHVPSF LAPEMRTLYD
     KYLEPGWEHH QEKPEAWAGL ANLEPGELWE THQLLKAKLI EFINDRVATQ TAPKGEGEGQ
     VVPGSGFAPE TLTIGFARRF ATYKRADLIM DDLERFKRLI RDADRPIQII YAGKAHPADE
     YGKALIQKIV QVTTDPEFEG RVVFLADYEM NVARHMLHGV DIWLNNPRRP QEACGTSGQK
     VVLNGALNCS ILDGWWAEAY DGRNGFAIGD TSEYADPGQQ DVHDARALYD VLENEVIPLY
     YDTDASGLPI EWIERVKWSI ISLGWRFNAS RMLLDYLNLA YLPAAGATSA QM
//
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