ID A0A1C7AEV8_9GAMM Unreviewed; 563 AA.
AC A0A1C7AEV8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=SVA_3167 {ECO:0000313|EMBL:BAU49715.1};
OS Sulfurifustis variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfurifustis.
OX NCBI_TaxID=1675686 {ECO:0000313|EMBL:BAU49715.1, ECO:0000313|Proteomes:UP000218899};
RN [1] {ECO:0000313|EMBL:BAU49715.1, ECO:0000313|Proteomes:UP000218899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skN76 {ECO:0000313|Proteomes:UP000218899};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of Sulfurifustis variabilis.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; AP014936; BAU49715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7AEV8; -.
DR KEGG; sva:SVA_3167; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000218899; Chromosome.
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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000218899};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 563 AA; 62888 MW; 40D76A1AC92E1B5A CRC64;
MLHRFVHQER IAYFTMEVAL RNEISTYSGG LGVLAGDTVR SAADLELPLV TVSLVSRQGY
FRQSLDAEGR QIEHPDPWEP ARFAQPLPAK VSVPIEGRVV WVAAWLYVLE SHRGGRQPVI
LLDTSLPENA EPDRAITDYL YGGDPTYRLK QEAVLGIGGV RMLYALGFRV RQFHMNEGHS
ALLTLELLER YAYPPEDVRP GELRYDIPRV RELCNFTTHT PVEAGHDRFP YDLVQRVLGD
FVDLPTLKQL AGAGELNMTQ LALSMSEYIN GVAKRHAETS RRMFPGYQVR AVTNGVHPFA
WTAPPLAKLY DAHVPGWCHE PELLVRAECC IGDEAIWAAH REAKAALLDK VATLSGVRLD
ADTAMLGFAR RMTAYKRPEL LFSDLERLAS IATNHRIQIV LAGKAHPRDE GGKRAIEQLH
RHIRALSGRV RVVFLPNYDM ALALLMVSGV DVWVNTPLRP LEASGTSGMK AALNGVPSLS
VLDGWWVEGR IEGITGWAIG DDDGPGERDA ESLYDKLERV VLPLYYENRA GWIAVMKGAI
AKNGSVFNSH RMMRRYATDA YIR
//
