ID R6EJG7_9FIRM Unreviewed; 755 AA.
AC R6EJG7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN538_02305 {ECO:0000313|EMBL:CDB00733.1};
OS Lachnospiraceae bacterium CAG:215.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1262985 {ECO:0000313|EMBL:CDB00733.1, ECO:0000313|Proteomes:UP000018007};
RN [1] {ECO:0000313|EMBL:CDB00733.1, ECO:0000313|Proteomes:UP000018007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:215 {ECO:0000313|Proteomes:UP000018007};
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:CDB00733.1}.
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DR EMBL; CBCV010000354; CDB00733.1; -; Genomic_DNA.
DR AlphaFoldDB; R6EJG7; -.
DR Proteomes; UP000018007; 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 601
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 755 AA; 86460 MW; D85FF1B539EEDA20 CRC64;
MKMEEMLREK LGKEIAQAGD EEIYAALLEI VQGLAKEKEV DETKKKVYYI SAEFLIGKLL
SNNLINLGLY EETRRVLAEN GKELSRIEEI EPEPSLGNGG LGRLAACFLD SMATLGLCGA
GIGLNYHLGL FRQKFEDHLQ KEEPNPWIEP ESWLVRTDVS YPVSFRGMTL KSRMYEIEVT
GYRNRTNKLH LFDVETVDEE IVEEGITFDK EEIRKNLTLF LYPDDSDENG RLLRIYQQYF
MVSNAAQLIL DECVVKGCAL YDLPDYAVIQ INDTHPTMVI PELIRLLTER GLEMDEAIDV
VSKTCAYTNH TILAEALEKW PVSYLKKVVP QLMPIIEILD DKIRRKYEDE RVAIIDRNDV
VHMAHIDIHY GFSVNGVASL HTEILKENEL NHFYKIYPEK FNNKTNGITF RRWLLHCNPK
LAALLDEVIG EDYRTDASKL EKLLDHAEDE QVLERILSIK KENKRALCTY LKETEQIDVD
PDSIFDIQIK RLHEYKRQQM NALYVIGKYL DIKAGKIPKT PITVLFGAKA APAYVIAKDI
IHLILCLQEI VNNDPEVSPY LKVVMVENYN VTKAEKLIPA CDISEQISLA SKEASGTGNM
KFMLNGAVTL GTEDGANVEI HELVGDENIY VFGASSDEVI AHYEKADYKS KEFYEADERI
KAAVDFITSE KMLAVGQEEN LKRLQAELLN KDWFMTLLDL KAYTKAKEEA FADWTDQKAW
AKKMLINIAK AGYFSSDRTI EEYNRDIWHL EKSGI
//
