ID B2TR27_CLOBB Unreviewed; 813 AA.
AC B2TR27; U4PD01;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=CLL_A3415 {ECO:0000313|EMBL:ACD22947.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22947.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
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 ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP001056; ACD22947.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TR27; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; cbk:CLL_A3415; -.
DR PATRIC; fig|935198.13.peg.3375; -.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000001195; 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:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 656
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 813 AA; 93566 MW; 7A85DEB7E09A72D0 CRC64;
MIEMDKKTFK KAYVNKFLEM HGIELKEGTN QQKYEALGSL VRDYVTRTWL KTNKKYNRTG
EKQVYYFSME FLLGRLLGNS LLNIGIRDIC KEALEELNIN LKDLENLEED QGLGNGGLGR
LAACFLDSMA SLNIPGHGCG IRYKYGFFEQ KIIDGKQVEV SDNWLKEGNV WEKRKTNKSE
IVKFGGEIKV EEKNGRLNFV HADYEPILAI PYDTPVVGFK NEIVNTLRLW SAEPLSNEFD
FSSFNRGDFL QALQYKNSVE AISQVLYPED SFYEGKMLRL KQQYFFVSAG IQSIIRHFKK
HGGKIPDFAE KIAIHINDTH PTLAIPELMR ILLDEEELNW DDAWRITENT ISYTNHTILS
EALEKWPIDM FKKLLPRIFM IVEEINRRYC EELKVKFQGQ EAKISNMAII GEGQIRMANL
AIVGSHSVNG VAKLHTDILK KKEMKDFYYL YPKKFNNKTN GITHRRWLLK CNPDLTRLLS
DTIGDGFIKH PLDLENFQKH LDDKNVLDEL GKIKLENKKK LAKTILDNEG IVVDPNSIFD
VQVKRIHAYK RQTLNCLRIM DLYNKLIDNP NLDVYPRTFI FGGKAAPGYY LAKNIIELIN
NIANKVNNDP RVNKKMKVVF MENYDVSLAE EIVPGADVSE QISTTTKEAS GTSNMKFMMN
GAITVATLDG ANIEIKDEVG EDNIVIFGLE ADEVLSYYKN GGYSSLEMYN NDSRIKNVIN
DLTNGKYHND KQRFKTVYQN LINYNDEFFV LKDFDSYLKA QDKIDTLYRD KNIWNKICGI
NISHSGIFSS DRTIEQYATG IWGSEVIYKN LGI
//
