ID F5TA40_9FIRM Unreviewed; 817 AA.
AC F5TA40;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:EGL36751.1};
GN ORFNames=HMPREF9124_1112 {ECO:0000313|EMBL:EGL36751.1};
OS Oribacterium sp. oral taxon 108 str. F0425.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=904296 {ECO:0000313|EMBL:EGL36751.1, ECO:0000313|Proteomes:UP000003787};
RN [1] {ECO:0000313|EMBL:EGL36751.1, ECO:0000313|Proteomes:UP000003787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0425 {ECO:0000313|EMBL:EGL36751.1,
RC ECO:0000313|Proteomes:UP000003787};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-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 -!- 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}.
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:EGL36751.1}.
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DR EMBL; AFIH01000001; EGL36751.1; -; Genomic_DNA.
DR RefSeq; WP_009428364.1; NZ_AFIH01000001.1.
DR AlphaFoldDB; F5TA40; -.
DR STRING; 904296.HMPREF9124_1112; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000003787; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 94261 MW; DD96712492A02922 CRC64;
MQKFDKAMLK KEIENNARKL FRRELTELNE KEAFHAVAAA IQNQIIDDWI LTTKRAEEED
RKRVYYLSME FLMGRALGNN ILNLSAHEEI KEVLEELGLN LSALEDAEPD WALGNGGLGR
LAACFLDSLA TLGYWACGCG IRYKYGFFKQ QIVDGYQKEV ADDWLKDGNP FEIRRAELAK
EVRFGGWVET VQEADGRLRF IQKGYQSVEA IPYDTPVVGY NNHIVDTLRV WDANAKETFS
LDEFDKGNYQ KAVESANMAK NIVEVLYPND NHYAGKELRL RQQYFFISAS VQTAVEYYAR
KHNGDVRNLP EKVAFQLNDT HPTVAVAELM RVLMDDYQLS WDEAWEITVK TCAYTNHTIM
AEALEKWPIE LFSKLLPRIY QIVEEINRRF CEEVRRKYPD RAEAKIAKMA IIYDGQVKMA
HLAIIGGHAV NGVAALHTEI LEKQELKDFY EMYPEKFSNK TNGITQRRWL LHANPELAEW
VTNKIGDQWI TDLPQIEKLA VYAEDKKAQA EFMAIKRHNK ERLARYVFEH NGIKLNVDSI
FDVMVKRLHE YKRQLMNILH VMYLYNQIKD HPEKDFYPHT FIFGAKAAAG YKTAKLTIKL
INNVAEVINN DASIRDKIKV VFVEDYKVSS AEVIIPAADF SEQISTASKE ASGTSNMKLM
LNGALTIGTM DGANVEIVKE VGAENAFIFG MSSDEVIQLE QNRSYNPMDI FNNDQEIRRV
LMQLVNGFYS PEDPELFRPL YNSLLNTKES DVADRYFILK DLRSYIKAQE EAVKQFQNRD
WWAKAAILNT SHAGKFSSDR TIEEYVRDIW HLDKITL
//
