ID D4M140_9FIRM Unreviewed; 826 AA.
AC D4M140;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=RTO_01600 {ECO:0000313|EMBL:CBL24952.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL24952.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL24952.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL24952.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL24952.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL24952.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929055; CBL24952.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M140; -.
DR STRING; 33039.ERS852502_00709; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; rto:RTO_01600; -.
DR PATRIC; fig|657313.3.peg.1151; -.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000008956; 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 659
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 826 AA; 95546 MW; 867879D53CB4C417 CRC64;
MFSKRFEKKA FKAAVKDNVK TLYRKTIDEA TPQQLFQAVS YAVKDVIIDD WIETQKRYDE
TDAKTVYYMS MEFLMGRALG NNLINMTAYK EVKEALEEMN IDLNVIEDQE PDAALGNGGL
GRLAACFLDS LATLNYPAYG CGIRYRYGMF KQKIKDGYQV EVPDNWLKEG NPFEIRREEY
AKEVRFGGNI RFEKDPVTGK DKFIQENYES VMAVPYDMPI VGYGNHVVNT LRVWDAKPIT
DFKLDEFDRG NYHKAVEQEN LAKLIVDVLY PNDNHYSGKE LRLKQQYFFI SASLQALIEK
YKKKHGDIRK LHEKVVIQMN DTHPTVAVPE LMRLLIDVEG LSWEDAWEVT SKTCAYTNHT
IMAEALEKWP IDLFSKLLPR IYQIVQEIDR RFLIKVREMY PGNEEKVRKM AILMNGQVRM
ANMAIVAGFS VNGVAQLHTE ILEKQELKDF YQMMPEKFNN KTNGITQRRF LAHGNPLLAD
WITDKIGDGW ITDLSQIAKL KPLVEDEDAR REFMEIKYQN KVRLAKYIKE HNGIDVDPRS
IFDIQVKRLH EYKRQLLNIL HIMYLYNQIK EHPEMSFYPR TFIFGAKAAA GYLRAKETIK
LINSVADVVN NDRSINGKLK VVFIEDYRVS NAEILFAAAD VSEQISTASK EASGTGNMKF
MLNGAPTLGT MDGANVEIVH EVGEENAFIF GLSSQEVINY ENNGGYNPTD VYFNDWEIKR
VVDQLMDGTY SNGDHNMYIN LYNSLLNTQC TDKADTYFIL KDFRSYADAQ KRVEEAYRDQ
QRWSKMAMMN TACSGKFTSD RTIEEYVRDI WHLEKVEVPS GQDLFE
//
