ID A0A1H8Q2X6_9FIRM Unreviewed; 809 AA.
AC A0A1H8Q2X6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN04490178_102162 {ECO:0000313|EMBL:SEO48331.1};
OS Propionispora vibrioides.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=112903 {ECO:0000313|EMBL:SEO48331.1, ECO:0000313|Proteomes:UP000198847};
RN [1] {ECO:0000313|EMBL:SEO48331.1, ECO:0000313|Proteomes:UP000198847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13305 {ECO:0000313|EMBL:SEO48331.1,
RC ECO:0000313|Proteomes:UP000198847};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FODY01000002; SEO48331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8Q2X6; -.
DR STRING; 112903.SAMN04490178_102162; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000198847; 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:UP000198847};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 654
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 809 AA; 92971 MW; 1D621F56303661E7 CRC64;
MNFDKAGFKN SFINQLQSMY GKGLEEADLY EQYMAFGACV REVISQNWIR TRQQYRSKNE
KQVFYFSMEF LLGKLLDMYL IHLGLKEPCR QALAELGIDL AALAEAEPDA GLGNGGLGRL
AACLLDSMAA MHLPGHGCGI RYKYGLFEQK IVDHHQVELP DNWLKNGYIW EYRKADKTVE
VRFGGRITQI IQPDKWMFVH EDYEPVLAVP YDIPIVGYQN RTVNTLRLWS AEPAAIDFDL
SSFNRGDYSR AVEYRHSVER ISKILYPDDT HYEGRLLRLK QQYFFVSAGL QSILHCFKQR
ALPWRTLPEK VGVHINDTHP ALAIPELMRL LIDEAGLGWE EAWNITVNTI SYTNHTTMPE
ALEKWPVDML EKLLPRIYLI IQEIHERLCR TVWDKTQSWD AVSEIAIIAD GQVHMARLAV
VGSYSVNGVA QIHSEILKNH TFAGFSRLYP YKFNNKTNGI THRRWLIKSN PALAELISRT
IDSSWIKYPC DLIQLVNYAQ DESLQQQFAA IKRQNKLKLA QFISNKYDIQ VDVDSIFDVQ
VKRLHAYKRQ ILNVLHIMHL YNKLRENPQL DMVPRTFIFA GKAAPGYYIA KQTIKLIHVL
AEKINHDTAI QGKLKVVFLE NYSVSLAEMI ISAADVSEQI STASKEASGT GNMKFMMNGA
ITIGTMDGAN IEIKQAVGDA NIVIFGLTAK QVFDYYHYGG YSAWDMYHND PRIKTVMEQL
VDGFFQEERE EFRPLYNDLL HNNDEFFVLK DFAAYCDAQR VVENKFRHSR EWQKMALMNI
AHSGIFSSDR MGSEYSVGIW KIKPVIITG
//
