ID A0A136WHS8_9FIRM Unreviewed; 817 AA.
AC A0A136WHS8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:KXL53909.1};
GN ORFNames=CLNEO_00010 {ECO:0000313|EMBL:KXL53909.1};
OS Anaerotignum neopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL53909.1, ECO:0000313|Proteomes:UP000070539};
RN [1] {ECO:0000313|EMBL:KXL53909.1, ECO:0000313|Proteomes:UP000070539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL53909.1,
RC ECO:0000313|Proteomes:UP000070539};
RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL Submitted (JAN-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 -!- 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:KXL53909.1}.
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DR EMBL; LRVM01000001; KXL53909.1; -; Genomic_DNA.
DR RefSeq; WP_066083239.1; NZ_LRVM01000001.1.
DR AlphaFoldDB; A0A136WHS8; -.
DR STRING; 36847.CLNEO_00010; -.
DR PATRIC; fig|36847.3.peg.2; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000070539; 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 Reference proteome {ECO:0000313|Proteomes:UP000070539};
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; 93654 MW; 227B37015609687B CRC64;
MGIIGIEKET LKTMIQENVK TLYRKTLETA LPEEIYQAAV FSLRDFITDK WIKTHETYYK
EDVKAVYYLS MEFLMGRFFG NALINMGMDQ VVKEVFAELG IDFNTVEDAE PDPGLGNGGL
GRLAACFLDS LATLELPAYG CGIRYHYGIF EQKLENGYQV EAPDNWLEDG DPWGIRRNEY
AVEIKFGGHV RAVPKENGGY RFVQEGYQSV MAIPYDYPVI GFGNNTVNTL RLWDARAKNR
IDLKSFNEGN YQKAAEEETL AKTLTDVLYP ADEHYQGKEL RLRQQYFFIS ATVQRVVERF
TNDHDDFNLL PEKVAFQLND THPSIAVAEL MRVLVDENDL PWEQAWEITK KVCAYTNHTI
MTEALEKWPL DLFSRLLPRI YQIIEEINRR FCVELMEECG NNPEKIRRLA IIADGQIRMA
YMAIVGSHSV NGVAALHTEI LKNHELKDFY KLFPERFNNK TNGITQRRWL LHANAQLAEL
ITERIGDGWI TDLSQLERIL PLVEEEAFRE RFMEIKQANK MSLAKYIKSA KGIDINPDSI
FDIQVKRLHE YKRQLLNVLH IIGLYNRLKM NPGLDMVPRT FIFGAKAAAG YHRAKLIIKL
INSVAEVVNH DQSIGGKIKV VFLENYRVSL AERLIPAADV SEQISTAGKE ASGTGNMKFM
LNGALTIGTM DGANVEIFEE VGEENIFIFG MSADEVQEKY NKEYDPWSVY NMNQEVRMAM
TALIDGTFDR DTGLFRELYD ALLNGFGGSR ADEYFILEDY ADYDRAQQAV DYAYRDKEKW
AKMAICNVAK SGKFSSDRTI KQYATEIWNL PTVPIDF
//
