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
//