ID R7FVS1_9FIRM Unreviewed; 810 AA.
AC R7FVS1;
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=BN797_01631 {ECO:0000313|EMBL:CDE17802.1};
OS Eubacterium sp. CAG:841.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262894 {ECO:0000313|EMBL:CDE17802.1, ECO:0000313|Proteomes:UP000017924};
RN [1] {ECO:0000313|EMBL:CDE17802.1, ECO:0000313|Proteomes:UP000017924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:841 {ECO:0000313|Proteomes:UP000017924};
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:CDE17802.1}.
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DR EMBL; CBIL010000041; CDE17802.1; -; Genomic_DNA.
DR AlphaFoldDB; R7FVS1; -.
DR STRING; 1262894.BN797_01631; -.
DR Proteomes; UP000017924; 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 Reference proteome {ECO:0000313|Proteomes:UP000017924};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 810 AA; 92252 MW; 3982C31A8AE36633 CRC64;
MGKTNTTTKA DIKTLLSEKL SRHFGAVAED ATKAQIYKAV IMSVRDALTE KRAKFKHAVK
AQQKKRVYYM SMEFLIGRSL KNNLLNMGLE KQYRGALRDM GFDLDEIYEM EPDPGLGNGG
LGRLAACFMD SLTTGNYPAT GFSICYEYGL FRQKIIDGNQ VETPDTWMQN GSTWLVPRTD
KTFPVRFGGK VSEKWENGRL EIVYTDYDEV EAVPYDMMIS GSDCDAVSNL RLWKASDMRN
FNMKLFTQGQ YMQAVEENTS AETLSRVLYP SDDHTEGKLL RLSQQYFLVS ASLQNILSDH
IAVYGTLSNL PDKVAIHIND THPALCIPEL MRLLMDIYSF SWETAWDTVV KTVSYTNHTV
MPEALECWNE ELFRMRLPRI YTIVCEINRR LCADLWNIYP GDWARISRMS IVANGQVRMA
NLSVAGSHMV NGVSKLHSEI LRQTVFHDYY KTTPEKFTNV TNGIAHRRWL CLGNPLLSAL
LDETIGTKYR KNPEAIGDFI KYRDDQSVID RVRAIKHENK ERFAEAYYKK TGDKLDTHSL
FDVQVKRIHE YKRQLLNALK IVALYDEIKK NPNISIRPQT FIFGGKAAPG YYLAKEIIRF
ICMLGKQIDN DPDVRGRLKV VFLEEYNVSL AEILMPASDI SEQISLAGKE ASGTGCMKFM
INGAMTVGTL DGANVEMADA VGNDNIYIFG LTANEVDELW KRGYNSAVYY KESERLHGAI
DRIGCGLAGE DFSNIENYLL HNPGVSDPYM CFADFDSYYA TYNRALDDYD HRNLWTKKAI
TNIAKAGYFA SDRSIKEYAE NIWHIEPCKI
//
