ID R5ER28_9FIRM Unreviewed; 777 AA.
AC R5ER28;
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=BN466_00272 {ECO:0000313|EMBL:CCX93819.1};
OS Firmicutes bacterium CAG:110.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263000 {ECO:0000313|EMBL:CCX93819.1, ECO:0000313|Proteomes:UP000018021};
RN [1] {ECO:0000313|EMBL:CCX93819.1, ECO:0000313|Proteomes:UP000018021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:110 {ECO:0000313|Proteomes:UP000018021};
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:CCX93819.1}.
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DR EMBL; CAXG010000416; CCX93819.1; -; Genomic_DNA.
DR AlphaFoldDB; R5ER28; -.
DR Proteomes; UP000018021; 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 Reference proteome {ECO:0000313|Proteomes:UP000018021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 622
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 777 AA; 88335 MW; 4D55C037533F8A53 CRC64;
MNNNCLNILK WTEAQLKYTY DVSLQEATPQ ELHEALGQAV MMAISDDWSH SKKTRMPNRK
AYYISAEYLI GRLVYSNLFN LGILDEMKEL FAEHGVDLAI LEDIEDDALG NGGLGRLAAC
FLDSAASTDI PLSGYGLRYK FGLFKQSFDA DGSQVENADD WTKFGDPWSF RRYNHTVKVK
FPDHTVLAVP YDVPVIGYGT ENVGTLRLWQ CEAEEELDFN AFNNQDYLRA LDAKNKAEDI
TRVLYPNDST WEGKRLRIKQ QYVLSSASLQ DMLRTFKIAH GDDLSRFAEF YAVQLNDTHP
AMSIPELIRL LMLEGMSFDD AFNVAQKTFS YTNHTVMGEA LEKWPLDLMR SVVPEIVDII
CRIDQKLKWE HPGLFIVKDN TAHMANLSIY VGSYINGVAE IHTQILKDDC FKDWYYAFPE
RFQNKTNGIT PRRWLGLCNP ELTAMLREKV GGDFLKNLDL IGELKDQIYD ETVVEFNDIK
HLKKEQLCAV IAKHEGVTLN PDFIFDVQVK RLHEYKRQLM NILSIVDIYF RLKEGRLPDF
HPTVYLFGAK SAPGYARAKA IIRYINRVAK LINSDPAVAD KLKVVFVQNY NCSYAEHIIP
AADISEQISP AGTEASGTGN MKLMLNGAVT LGTLDGANVE IAQEAGRENE YIFGHTVDEI
NAAKPTYHAR GIYDSNADLR RAINTLVDGT VPTDDAQKEL FHSLLDGTDW HQADHYFLLL
DYASYLGTKL QANRDYADRI AFGRKCLMNV ASAAKFSSDR TIRQYAEEIW HIKPTEY
//
