ID A0A1I5UMV9_9FIRM Unreviewed; 823 AA.
AC A0A1I5UMV9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN04487928_11387 {ECO:0000313|EMBL:SFP96582.1};
OS Butyrivibrio proteoclasticus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=43305 {ECO:0000313|EMBL:SFP96582.1, ECO:0000313|Proteomes:UP000182624};
RN [1] {ECO:0000313|Proteomes:UP000182624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P18 {ECO:0000313|Proteomes:UP000182624};
RA Varghese N., Submissions S.;
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 -!- 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}.
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DR EMBL; FOXO01000013; SFP96582.1; -; Genomic_DNA.
DR RefSeq; WP_074887991.1; NZ_FOXO01000013.1.
DR AlphaFoldDB; A0A1I5UMV9; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000182624; 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 665
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 823 AA; 94956 MW; 65C546DB15C0A85A CRC64;
MKKKPLKFDK DLFKRSVQYN VKTLYRKTME EATEQELYQA SAYALKDAIV DHWMTTQKKA
AEQDPKIVYY MSMEFLMGRA FGNNLINLQA YKPVKEALDE LNIDLNLIED QEPDPALGNG
GLGRLAACFL DSLSTLGYVA YGCGIRYKYG MFRQKIQDGY QVEVPDTWLE NGNPFELRRN
EYAKEVKFGG YVNMYTDERG RTMFKQEGYQ VVRAVPYDLP VVGYGNGVVN TLRIWDAEPI
QCFQLDSFDK GDYQKAVEQE NLASQLCEVL YPNDNHIAGK ELRLKQQYFF ISASVQTALQ
RYLKHHEDIR KFYEKNVFQL NDTHPTVAVA ELMRLLMDEY YLSWDEAWDV TTKTCCYTNH
TIMAEALEKW PVDLFQRLLP RIYQIVDEIN RRFVDQIMRQ YSGSAGIDVQ AKIRSMAILY
DNQVKMAHLA IVGGHSVNGV ARLHTEILEK RELKDFYEMM PEKFNNKTNG ITQRRFLLHA
NPLLADWVTE KIGDDWIVDL SQMEKLKAFA DDKKAQQEFM DIKLQNKKRL AKYILKHNGI
EVDPKSIFDV QVKRLHEYKR QLLNILQVIH KYNDIKTHPN KDFYPKTYIF GAKAAAGYLT
AKLTIKLINA VADVVNNDPD IDGKIKVVFI EDYKVSNAEL IFAAADVSEQ ISTASKEASG
TGNMKMMLNG AITLGTLDGA NVEIVNEVGE ENAFIFGLTS QEVMDYERNG GYNPMDIYNS
NPNVKKVLDM LVDGTFSNDR ELFRPLYNCL LNTVNSNKAD QYFILKDFES YLEAQKRISD
AYQDKKRWAK MALLNTASCG KFSSDRTIQE YVDEVWHLDK LEM
//