ID R5GUN0_9FIRM Unreviewed; 786 AA.
AC R5GUN0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN782_00657 {ECO:0000313|EMBL:CCY20888.1};
OS Eubacterium sp. CAG:786.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262893 {ECO:0000313|EMBL:CCY20888.1, ECO:0000313|Proteomes:UP000018127};
RN [1] {ECO:0000313|EMBL:CCY20888.1, ECO:0000313|Proteomes:UP000018127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:786 {ECO:0000313|Proteomes:UP000018127};
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:CCY20888.1}.
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DR EMBL; CAXS010000367; CCY20888.1; -; Genomic_DNA.
DR AlphaFoldDB; R5GUN0; -.
DR STRING; 1262893.BN782_00657; -.
DR Proteomes; UP000018127; 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 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 631
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 786 AA; 89152 MW; D2346115FD855ECE CRC64;
MKIENFKEKL VSLCEKEYRA QPKELTANQL HCAVSKLVME ELSPAWDKSR MAHDKARKAS
YLSMEFLVGR AVYNNLLCLG ILDSTAEELK ALGVDISEFE EVEDAALGNG GLGRLAACFL
DSAAALDLPL DGYGIRYKYG LFKQGIKDGF QTETADDWQR YGDPWSIRRE QETVVVHYAD
GDVNAVPYDY PVIGYGTENV GTLRLWQAET DDEFDFDLFN RSKFTEAGEK KRAAEDISRV
LYPNDETEAG KILRLKQEYF FSAAAVADLI RKHKKLFGTM ENFADYNSIQ MNDTHPVIAL
PEFIRVVMRD EGWDFDKAFA MAKKVFNYTN HTIMQEALEK WDSRLIERVV PEVYSVMIML
NEAFESEMHR LNVPQEKRAV MRLIRNGTVH MANIAVFGSS YVNGVAAIHT ELLKSTVLRD
WYELYPGRFQ NKTNGITQRR WLALCNQELS ALITELLGDN SWVTDLYKLQ ALKKYADDET
VLRRFIDIKH TKKQQLADFI EKSEGIKVDP TSIFDIQIKR LHEYKRQLLN AFSILYLYYE
IKDGNLKDFR PTTFIFGAKS APGYYRAKGI IKYINEVAKL VNSDPDTKDL LKVVFVSNYR
VSYAEKLVAA ADISEQISTA GTEASGTGNM KFMLNGAVTL GTLDGANVEI AEEAGAENEY
IFGATVEKLE KIMPNYVPRD VTESDAKIKR VVTSLIDGTV SDGGNGVFRE LYFALMEGAS
WHVPDHYYLL GDLDSYVKAK LAANRDCNDE LAFAKKCWLN ICSAGKFSSD RTIAEYAKDI
WHIEKA
//
