ID R7I322_9CLOT Unreviewed; 784 AA.
AC R7I322;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN648_02224 {ECO:0000313|EMBL:CDE44912.1};
OS Clostridium sp. CAG:411.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262802 {ECO:0000313|EMBL:CDE44912.1, ECO:0000313|Proteomes:UP000018022};
RN [1] {ECO:0000313|EMBL:CDE44912.1, ECO:0000313|Proteomes:UP000018022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:411 {ECO:0000313|Proteomes:UP000018022};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDE44912.1}.
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DR EMBL; CBIY010000091; CDE44912.1; -; Genomic_DNA.
DR AlphaFoldDB; R7I322; -.
DR STRING; 1262802.BN648_02224; -.
DR Proteomes; UP000018022; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000018022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 633
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 784 AA; 89181 MW; 11915A21908A0258 CRC64;
MLEIEPILRC KVRMDFPNKQ AHKKGAHLMS NLAEVVKKQF GRSIAECTNE EVYVSLLSLT
KDALKNKGYN EGKKKIYYIS AEFLIGKLLS NNLINLGIYD EISKELAENG KNIAEIEEVE
MEPSLGNGGL GRLAACFIDS IATLGMNGAG VSLNYHLGLF KQVFENKLQK ETPNPWITDN
CWSTKVPERS YTVPFKGFEL KSTLYDIDVS GYDSKSIKLH LFDVDTVDEN LVQGDGISFD
QHDIAKNLTL FIYPDDSTRE GQLLRIYQQY FMVSNGAQLA IDEAKERGMK DLRELADYVT
IQINDTHPSM VIPELIRLMT ADGLSTDEAV EVVKKVCAYT NHTILAEALE KWPIDYLEEV
VPHLLPIIRD LDARVKAQYS DPSVAIIDDT NRVHMAHMDI HFSYSVNGVA ADHTRILEES
ELNNFYKIYP EKFNNKTNGI TFRRWLMHCN HELTDFITSK IGDGFKKNAD ELEKLLQFVD
DDATLEELLN IKKSAKKRLQ AFIKSNVNQD LDDEAIYDIQ IKRLHEYKRQ QLNVLYIIHK
YLEIKEGKKP ATPINFIFGA KAAPAYIIAK DIIHTIICLQ ELINNDPEVS PYMKVVMVEN
YNVTAAEKLF PACDISEQIS LASKEASGTG NMKFMLNGAV TLGTDDGANV EIHGLVGDEN
IYIFGESSDQ VIEHYAKADY CSFDYIKKDP EIARCVGFLL SPEMLSVGHY DHLARLHKEL
VTKDWFMTLL DFKDYVRVKD QAFADYADRK TWAKKMLVNI AKAGFFSSDR TIKQYNDDIW
KLND
//
