ID A0A498R2N2_9FIRM Unreviewed; 809 AA.
AC A0A498R2N2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=LUCI_0226 {ECO:0000313|EMBL:VBB05020.1};
OS Lucifera butyrica.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Lucifera.
OX NCBI_TaxID=1351585 {ECO:0000313|EMBL:VBB05020.1, ECO:0000313|Proteomes:UP000277811};
RN [1] {ECO:0000313|EMBL:VBB05020.1, ECO:0000313|Proteomes:UP000277811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LUCI {ECO:0000313|EMBL:VBB05020.1};
RA Strepis N.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; UPPP01000052; VBB05020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498R2N2; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000277811; 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:UP000277811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 655
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 809 AA; 92769 MW; E3F87BD55DCE8102 CRC64;
MFQSKERFKQ AFLEKLQTLR GVTLEGASDS DKYIALSNLV REYISKNWAA TNNTYLERGE
KQIYYFSIEF LLGRLLHSNL LNIDQNHVVR DALQELDIDL ARLEEKEPDA GLGNGGLGRL
AACFLDSMAS LNLPGHGCGI RYKYGLFEQK IVNGYQVELP DNWLQDGNVW EYRKPEKSVE
VRFGGYVREA VAEGVRLFIH EGYEAIRAVP YDMPVVGYQN KTVNTLRLWS AEAAPQDFDF
SSFNRGEYLK AIEYKYSVEA ISEILYPDDS YQEGQKLRLK QQYFFVSAGI QSIVRRYKRK
NGSVYDFEDK IAIHINDTHP ALAVPELMRI LMDDEGLGWD EAWRITSNTI SYTNHTVLPE
ALEKWPVEMF KELLPRIYMI VHEINERFCR ELWDKYPGDW DRIARMAIVA NGYVHMAHLA
IVGSDHVNGV AHIHTEILKK QVMRNFYELS PHKFSNKTNG ITHRRWLLKA NPLLAKLITD
TIGASWITFP GDLVRLEHYA GDAAWRDNVR KVKLANKNRL AQYIKRKYDI TINPASIFDV
HVKRIHAYKR QLLNVFHIMD LYNRLRVNPD LDVMPRTFIF GGKSAPGYFM AKRTIKLINT
LAEMVNQDQS IGDKLKVVFM ENYGVSLAEM IIPAADISEQ ISTASKEASG TGNMKFMMNG
AITLGTLDGA NIEIRNAVGA ENFISFGLTA EQVLSYYAHG GYNAWDVYNS DERIQVIMDQ
LVNLFFPVAK EEFRTFYDTL LHSNDEFFVL QDFASYVEAQ NRVSKLYQNE EAWGRMAAAN
IAHSGQFSSD KTIMEYAIGI WNVKPVVVK
//
