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Database: UniProt
Entry: W8TEQ6_PEPAC
LinkDB: W8TEQ6_PEPAC
Original site: W8TEQ6_PEPAC 
ID   W8TEQ6_PEPAC            Unreviewed;       550 AA.
AC   W8TEQ6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   Name=glgP2 {ECO:0000313|EMBL:AHM56303.1};
GN   ORFNames=EAL2_c10040 {ECO:0000313|EMBL:AHM56303.1};
OS   Peptoclostridium acidaminophilum DSM 3953.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM56303.1, ECO:0000313|Proteomes:UP000019591};
RN   [1] {ECO:0000313|EMBL:AHM56303.1, ECO:0000313|Proteomes:UP000019591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM56303.1,
RC   ECO:0000313|Proteomes:UP000019591};
RX   PubMed=24926057;
RA   Poehlein A., Andreesen J.R., Daniel R.;
RT   "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT   acidaminophilum al-2 (DSM 3953).";
RL   Genome Announc. 2:e00573-14(2014).
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; CP007452; AHM56303.1; -; Genomic_DNA.
DR   RefSeq; WP_025435315.1; NZ_CP007452.1.
DR   AlphaFoldDB; W8TEQ6; -.
DR   STRING; 1286171.EAL2_c10040; -.
DR   KEGG; eac:EAL2_c10040; -.
DR   PATRIC; fig|1286171.3.peg.955; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_015112_1_0_9; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000019591; 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; 2.
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   ECO:0000313|EMBL:AHM56303.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019591};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHM56303.1}.
SQ   SEQUENCE   550 AA;  62618 MW;  300A87E5509226BD CRC64;
     MKNEPCKQLT RVAYFCMEYA LQSSMKTFAG GLGILAGDYM KAAKDSSCSV IGIGILWKQG
     YGGQAVDSTG RVHDKYCNYK YDFLQDTGVK VTVDIKDKEV TCKVWKVDCF GNSPVYLLDT
     DIPENDNANV KLRWVTSKLY GGVEEERLAQ EIVLGVGGVR ALRKLGIETD VYHFNEGHAA
     FAGFELIREK MAGGLDFEEA LERTREQIVF TTHTPVKEGN EKHPINALVY MGANLGLSGQ
     QLERIGGSPF NMTVAGLRLC KAANAVSRLH AVTANKMWEN IEDRPYIIPI TNGIHRPTWV
     DMRLHRHIAD GETIWKHHQE NKKKLLSFVH KRTGHKLLEE SITIGFARRA VDYKRPDLFM
     RNIEDFEALV KKWNVQIIFS GKAHPLDDSG KRVLENLIAL SKKYPQNVVF IKNYDMEIAQ
     RLVQGCDVWL NSPRRPNEAC GTSGMKAAMN GVLNLSVLDG WWPESCIDGV NGWQFGDGFE
     STDAGIVDEW DRKKLIEVFD NHVAPTYYED RQRWIEMMRS SINTTWDAFD IKRMINEYYE
     KMYTPSEKNR
//
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