UniProt: D4MYT0

Database: UniProt
Entry: D4MYT0_ANAHA

LinkDB:  D4MYT0_ANAHA 
Original site:  D4MYT0_ANAHA

All links

Ontology (6)   
   GO (5)   
   CAZY (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
All databases (19)   

Download RDF

ID   D4MYT0_ANAHA            Unreviewed;       818 AA.
AC   D4MYT0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=malP_1 {ECO:0000313|EMBL:CUM95245.1};
GN   Synonyms=malP_2 {ECO:0000313|EMBL:CUP79156.1};
GN   ORFNames=CL2_07430 {ECO:0000313|EMBL:CBL37775.1}, ERS852425_01658
GN   {ECO:0000313|EMBL:CUM95245.1}, ERS852475_00486
GN   {ECO:0000313|EMBL:CUN60563.1}, ERS852520_02207
GN   {ECO:0000313|EMBL:CUP79156.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL37775.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL37775.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37775.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL37775.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37775.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000095564, ECO:0000313|Proteomes:UP000095598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM95245.1,
RC   ECO:0000313|Proteomes:UP000095598}, 2789STDY5834860
RC   {ECO:0000313|EMBL:CUN60563.1, ECO:0000313|Proteomes:UP000095611}, and
RC   2789STDY5834908 {ECO:0000313|EMBL:CUP79156.1,
RC   ECO:0000313|Proteomes:UP000095564};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP929061; CBL37775.1; -; Genomic_DNA.
DR   EMBL; CYXT01000011; CUM95245.1; -; Genomic_DNA.
DR   EMBL; CYZM01000001; CUN60563.1; -; Genomic_DNA.
DR   EMBL; CZAU01000022; CUP79156.1; -; Genomic_DNA.
DR   RefSeq; WP_008392561.1; NZ_JANGBA010000044.1.
DR   AlphaFoldDB; D4MYT0; -.
DR   STRING; 649756.ERS852387_00745; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GeneID; 15230866; -.
DR   KEGG; bprl:CL2_07430; -.
DR   PATRIC; fig|245018.3.peg.932; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000008960; Chromosome.
DR   Proteomes; UP000095564; Unassembled WGS sequence.
DR   Proteomes; UP000095598; Unassembled WGS sequence.
DR   Proteomes; UP000095611; 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         660
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   818 AA;  94140 MW;  27236EF0F867D12E CRC64;
     MKTERFDKKL FKQEVLNNLK TQFRVELDNA SQQQIYQAVA YALKEWIIED WMDTQKTYEE
     KDPKILYYMS MEFLMGRALG NNLINMSMYG EVKEALDELG VDLNAVEDQE PDPALGNGGL
     GRLAACFLDS LATLGYAAYG CGIRYQYGMF KQKIKDGYQI EVPDEWLKNG NPFELKRPEY
     AKEVRFGGNI RTEYDEATGR TNFIQENYQS VMAVPFDYPI VGYGNHIVNT LRIWDAEAIT
     DFQLDSFDKG EYDKAVEQKN LAKNIVEVLY PNDNHYEGKE LRLKQQYFFV SASLQAAVAK
     YKKNHDDITK LYEKMTIQMN DTHPTVSVAE LMRILMDEEG LGWDEAWEVT TKTCAYTNHT
     IMAEALEKWP IDLFSKLLPR VYQIVEEIDR RFVNKIREMY PGNEEKVKKM AILWDGQVRM
     AHMAIAAGYS VNGVAKLHTE ILKNQELKDF YQMMPEKFNN KTNGITQRRF LMHGNPLLAD
     WVTKKLGTDT WATDLSLMSG LKKYVDDPKA QKEFMDIKLQ NKKRLAKYIL EHNGVEVDPT
     SIFDVQVKRL HEYKRQLMNI LHVMYLYNQL KKNPNMKFYP RTFIFGAKAA AGYLRAKQTI
     KLINSVADKV NNDASIKGKL KVVFIEDYRV SNAEWIFAAA DVSEQISTAS KEASGTGNMK
     FMLNGAPTLG TMDGANVEIV DEVGAENAFI FGMSSEEVIN YENNGGYHPY EIYQKDKDIH
     EVLDQLVDGT YANGDPELYK DLYQSLLFGD TGSQADMYFI LKDFRSYAEA QKKVEEAYRD
     TKGWAKMAMT NTAGCGKFSS DRTIQEYVDD IWHLDKIR
//

DBGET integrated database retrieval system