ID F0GU48_9FIRM Unreviewed; 751 AA.
AC F0GU48;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HMPREF9290_1268 {ECO:0000313|EMBL:EGC82485.1};
OS Anaerococcus prevotii ACS-065-V-Col13.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=879305 {ECO:0000313|EMBL:EGC82485.1, ECO:0000313|Proteomes:UP000005286};
RN [1] {ECO:0000313|EMBL:EGC82485.1, ECO:0000313|Proteomes:UP000005286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-065-V-Col13 {ECO:0000313|EMBL:EGC82485.1,
RC ECO:0000313|Proteomes:UP000005286};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JAN-2011) 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 -!- 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|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={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:EGC82485.1}.
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DR EMBL; AEXM01000012; EGC82485.1; -; Genomic_DNA.
DR RefSeq; WP_004834361.1; NZ_AEXM01000012.1.
DR AlphaFoldDB; F0GU48; -.
DR STRING; 879305.HMPREF9290_1268; -.
DR PATRIC; fig|879305.3.peg.328; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000005286; 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: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; 2.
DR InterPro; IPR000811; Glyco_trans_35.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000005286};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
SQ SEQUENCE 751 AA; 88210 MW; 261FAFFB3EF5C46F CRC64;
MKLKQTNNET NLLERIQIFL YSFYAKDIKN ARINEVYDCL CRALMEDIGK KWVYSKSNDD
DFEVYVLSFE YLPGKFIERN IARLGKEKEV RETLDKIGFS YDEIIDFEKE ANLGLGDIGI
GSSYLISELA NKNIRSVAYA LRYENGDLKQ KIVDGRQVEY SEYWLEEGNN WEHKKGFSYE
INIDGRKHKS IAYDIPILSN KADFVTSLRL FQSEPTKAVS YSDFARGDIL KAYDEYISTS
SINQFLYLDD SSYDGKLLRL KQEYFYSASA VRDIFKRYKN RYGSIDKIDK RIKIIVNDIH
PTLALIEFIR ILTRDFNLDI RKSIDITRSV FEHIAFSITD DSLEAYPVEM VKRVNPDILD
TILNIQEALK LDNIDSVLIK NGYVMFKNIN MALSNEYIYL SKILKNNRSS KRTLSYTNFG
TDRLLYLDKN NIQLMEVFKE FGIDSSSYDQ INKLNDLKDN NYFIDKVEEA KFINKKKLIE
LSNEPINPYS IFDVQLSIFH EGKRQILNAL AIAYRYYLLK TNANLRDVST TYIFSGKANE
GYFMAKETIK FILALKKMID KDKIIREKIK IVFIEDIDIH KSKIILKSLD VYNNLTLSTL
DNQDFNMLNA AFNMSNIVTS RGGISQNIEG DNSFYTIGES YDDIVKSNVN DLYNANDFYY
SNDMVKYTVE NLIRESYENF PYDFKQMYDQ IMMYNDSFRI FKDLNNLIET RNKRELDYLN
KEKWVRNEID NILWANNFRL DNKIIRNGID D
//
