ID   B2KBT0_ELUMP            Unreviewed;       850 AA.
AC   B2KBT0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ACC97834.1};
DE            EC=2.4.1.1 {ECO:0000313|EMBL:ACC97834.1};
GN   OrderedLocusNames=Emin_0273 {ECO:0000313|EMBL:ACC97834.1};
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC97834.1, ECO:0000313|Proteomes:UP000001029};
RN   [1] {ECO:0000313|EMBL:ACC97834.1, ECO:0000313|Proteomes:UP000001029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191 {ECO:0000313|EMBL:ACC97834.1,
RC   ECO:0000313|Proteomes:UP000001029};
RX   PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC97834.1; -; Genomic_DNA.
DR   RefSeq; WP_012414449.1; NC_010644.1.
DR   AlphaFoldDB; B2KBT0; -.
DR   STRING; 445932.Emin_0273; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   KEGG; emi:Emin_0273; -.
DR   HOGENOM; CLU_015112_0_0_0; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000001029; 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   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:ACC97834.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001029};
KW   Transferase {ECO:0000313|EMBL:ACC97834.1}.
FT   DOMAIN          12..120
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   850 AA;  97491 MW;  EE460AD1D5AF732C CRC64;
     MKIHSFNVQP NLPENIKFLE ELADNMWFSW NWQAILLFFK IDPALWNKSK RNPKWFLGAI
     SQKRLEEISN DTEFVNHLNK VKEDFYKYKE SSGWYHSNKK EGEENFLTAY FSMEYGIGEG
     LPIYSGGLGM LSGDHMKSAS DLGLPLIGVG LFYQRGYVQQ VLNRDGWQTE AYPENDWAHM
     PVEKVKDAQG QDLRVSIELG KDIIYAALWA VSVGRIKLYL LDTNLQENAH EFRTITEQLY
     GGDRENRIRQ EVVLGIGGVK ALAAMGIKPT VFHINEGHSA FLLCQRIIDI MRERNLQFAQ
     AADIVWSTSV FTTHTPVIAG NEHFDPALVR KYMEVYAQKM GISWDEFVSL GKDEPTSATF
     CMTVLALKLS AYDNGVSKLH GEISREMWQK IWPTLPVKEI PITSITNGVH VSSWLSHEHS
     ELYKKYSFND RDINSVDITD RNTWSGVDSI PANEFWDVHN IRKDKLINMA RLRLKKQLQR
     YGADATQINK ASKILKPDVL TIGFARRFAT YKRANLLFKD LNRLDKLINN PKQPIQFVFA
     GKAHPADIEG KEFVKYISNI QADPRFAGKI IFVEDYNMNL ARYMVQGVDV WLNNPIRPME
     ASGTSGMKAA ANGALTLSVL DGWWDEVGPC DFSWSIGGIE HYKTPDERDL VESEAIYNII
     EQEIAPLFYE RNEDNVPEKW VSYMKQSIKT IAPFFNTHRM VCEYYERFYS HAHKHFNILS
     DNKKVQDIGE RRKVIAANWY RVNITDISPK LETETKIGDT ITLRARVFLG AIPAEYVNVQ
     AAIGVRGTTG DLISGQLINM TQTGKEEDAL IYETVIRPEN SGRQDYALRI LQNIPYLPNQ
     YMPLYISWEN
//