ID A0A1I2E971_9FIRM Unreviewed; 816 AA.
AC A0A1I2E971;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN05216245_13010 {ECO:0000313|EMBL:SFE88820.1};
OS Succiniclasticum ruminis DSM 9236.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Succiniclasticum.
OX NCBI_TaxID=1123323 {ECO:0000313|EMBL:SFE88820.1, ECO:0000313|Proteomes:UP000198896};
RN [1] {ECO:0000313|EMBL:SFE88820.1, ECO:0000313|Proteomes:UP000198896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9236 {ECO:0000313|EMBL:SFE88820.1,
RC ECO:0000313|Proteomes:UP000198896};
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 -!- 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|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; FONL01000030; SFE88820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2E971; -.
DR STRING; 1123323.SAMN05216245_13010; -.
DR Proteomes; UP000198896; 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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000198896};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 669
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 816 AA; 94888 MW; C2318E5159D6EC8B CRC64;
MSLNTRCGNY QTMRTWKSKK EFKELFVKKA EVLFEKSVKE LSHKEVYQII ATMIKDLVTD
EWIQTEKIYN HKRVRQVYYF SIEFLLGRLL NTNLLNCDME NLCRSALQDF GFDLEEIFPE
EPDPGLGNGG LGRLAACYID SMAALQLPGH GCSIRYQYGL FDQRIIDGQQ VELPDAWLRN
GFPWETKKSD KAVDVRFGGH AYMRPGKGGT LVCVHEHYNT VRAVPYDVPV LGYQNHTVNT
LRLWKAEYTR ENMYGQLRYG DYRKALQYKD QAQQISRFLY PNDSTYEGRK LRLMQEYFFV
SAGLQSIMRH YKKHYGSPKL FDRYIALHIN DTHPALIIPE LMRILMDEEG LSWEDAWRIT
TNSVAYTNHT ILPEALERWS IPMFQELLPR IFLIVDEINR RWLEAVQQRF PGQEDKAREV
AILWNNQVHM ASLAVVGSHS INGVAKLHSE ILKINTLKPF YTWFPERFNN KTNGVTHRRW
LIESNPQLTE LICDTIGKDW IHAPEKLLAL EPFGNDAAFR ERLAEVKQKR KEILAEYLHK
ERNITINPHS IFDIQIKRMH MYKRQLLNIL HVYHLYRQLI ENPGMDIVPR TFIFGGKAAA
SYGEAKITIQ LINTVARLID QDYRAARKLK VVFLENYNVS LGQKLFPAAD VSEQISTASK
EASGTGNMKF MFNGAITLGT MDGANVEIHQ EVGDEHSVIF GLRADEVQQY YQQGGYSSWD
IYNSDADVRR ALEVMEENPM FGQLREALLD RNDEFFVLKD FKSYCAAQQE IERRYRDADG
WFRSSTVNIA HAGHFSSDRS IQEYADDIWY LSPVKI
//
