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Database: UniProt
Entry: A0A1I5UMV9_9FIRM
LinkDB: A0A1I5UMV9_9FIRM
Original site: A0A1I5UMV9_9FIRM 
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
//
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