ID R5Y6M1_9FIRM Unreviewed; 802 AA.
AC R5Y6M1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN680_01494 {ECO:0000313|EMBL:CDA20484.1};
OS Ruminococcus sp. CAG:488.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262959 {ECO:0000313|EMBL:CDA20484.1, ECO:0000313|Proteomes:UP000018248};
RN [1] {ECO:0000313|EMBL:CDA20484.1, ECO:0000313|Proteomes:UP000018248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:488 {ECO:0000313|Proteomes:UP000018248};
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 -!- 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|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:CDA20484.1}.
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DR EMBL; CBBI010000103; CDA20484.1; -; Genomic_DNA.
DR AlphaFoldDB; R5Y6M1; -.
DR STRING; 1262959.BN680_01494; -.
DR Proteomes; UP000018248; 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 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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 654
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 802 AA; 91185 MW; EF3D7CA0C9A1CD4D CRC64;
MNYKLTKKEA KELIVNKLSH FYGVSPEEAT YEHYYKAIAL ILRDMMMQGR KEFHNEAKKS
DSKKIYYLCM EFLMGRSLKN NLYNLNLTKT MESALKDFGI KLDKLYDCEP DAGLGNGGLG
RLAACYLDGL ASQGYYAKGY SILYEYGIFK QKLVDGWQTE LPDFWLPGGD VWLVPREEEA
VDILFEGWVD ESWDNQYHHV EQRDCNKVKA IPYDMYVSGK DGKGISVLRL WSAKAPGLDM
DMFNQGDYMR AMEQNAMAEV ISKVLYPSDN HPEGKSLRLR QQYFLVSASI QDIINNHLRV
YGTVENLADR IAIHINDTHP TLAIPELMRI LLDDCGYGWD EAWKIVTDTV AYTNHTVMAE
ALECWPEDLF KRLLPRIYEI TKEIDNRFRS YVWNATGDAD KVERMAIVSN GVIRMANMSV
AGSHCVNGVS ALHSEILKES VFKDFYSLTP DKFTNVTNGI AHRRWLCQSN PELTKLLTEL
IGNGFVYNGD DLEKLKPYAT DAEVLKKLEK IKLHNKERLT ELVKKSNGVE LDPTSIFDVQ
VKRLHEYKRQ HLNAFHILSK YLAIKENPDG DFTPHTYIFA AKAAPGYFMA KKIISFICSL
SELINNDPDV RGRLKVVYLE DYNVTMAEHL MPAADISEQI SLSGTEASGT GNMKLMINGA
VTLGTMDGAN VEIHEAVGED NIIIFGMSTP EVNELKRVGY NPMNYYQNNV DIRKVVDFIN
GGINGKVFPE IGGTITHNDP YMVLADFADY KAAQAKAEKL FADRKTWNRM SLMNIAGAGR
FACDRAINDY ARDIWHTKPL RK
//
