ID A0A1Y4RTV4_9FIRM Unreviewed; 815 AA.
AC A0A1Y4RTV4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=B5E80_16825 {ECO:0000313|EMBL:OUQ21028.1};
OS Flavonifractor sp. An135.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965558 {ECO:0000313|EMBL:OUQ21028.1, ECO:0000313|Proteomes:UP000196472};
RN [1] {ECO:0000313|Proteomes:UP000196472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An135 {ECO:0000313|Proteomes:UP000196472};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ21028.1}.
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DR EMBL; NFLG01000040; OUQ21028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4RTV4; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000196472; 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:UP000196472};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 657
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 815 AA; 92876 MW; 4E9CE350704C04A2 CRC64;
MHQYTKKELM DLITGKLRRN FGRDIDEATS LHMFKACALV LRDIMSAQQM KTQDKVQATH
ARQVHYLSLE FLMGRSLMKN AYNLGVLEPL KEAIEGLGFS ASDLFESEPD AGLGNGGLGR
LAACYLDSMT TLEIPATGYS ICYELGIFKQ KIVDGEQVEL ADNWLGLGDA WLIPKMDEVE
EVRFGGQVKD VWDDQGHHSI QHTGYTSVLA IPKDMEIAGF KTEHGNTLRL WDAKSPTPVD
MSLFSRGEYL KAVEQRAMAE TISKILYPDD NHYEGKSLRL KQQYFFVSAT VQSIVRKHRA
EYGTLRNFHL KHVLQINDTH PTLVIPELMR ILLDEEGYGW DEAWNIVTHS VAYTNHTVMA
EALERWPQQL VIDLLPRIWQ IIVEISNRYQ NELTTYFHGD MSKVEPMAII WGGDVRMANL
CICACYAVNG VSALHSDILK KEVFHDAYVR TPAKFKNVTN GIDHRRWLAE CNPKLNALIQ
ECTGGDRYLL QPEAMKDLEK YKDDASVLER LENIKKENKR AFASWVARES GIVLNTDAMF
DVQVKRLHEY KRQLLNVLHI IYEYQHLKDD PNFMITPKVY LFGAKAAPGY YVAKEIIHLI
NSLADTVNSD PVCKDKLQVV FLENYRVSLA EKLMPASELS EQISTAGKEA SGTGNMKFMM
NGAVTIGTLD GANVEMHEVL GDENIFLFGL KAHEVTELKN KNYRSYEYYM HNADLRAVID
NLSHGFKDGV SYDNLTKRLL FGNGSPADEY MLLADFDSYR NAHKRAAEQY LDRKTWNQMS
LINVARSGIF AADRSIRDYA RDIWNVPVRD LSEKK
//
