UniProt: A0A1Q2HXL6

Database: UniProt
Entry: A0A1Q2HXL6_9CORY

LinkDB:  A0A1Q2HXL6_9CORY 
Original site:  A0A1Q2HXL6_9CORY

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
All databases (13)   

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ID   A0A1Q2HXL6_9CORY        Unreviewed;       805 AA.
AC   A0A1Q2HXL6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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 {ECO:0000313|EMBL:AQQ15574.1};
GN   ORFNames=CGLAU_08095 {ECO:0000313|EMBL:AQQ15574.1};
OS   Corynebacterium glaucum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=187491 {ECO:0000313|EMBL:AQQ15574.1, ECO:0000313|Proteomes:UP000217209};
RN   [1] {ECO:0000313|EMBL:AQQ15574.1, ECO:0000313|Proteomes:UP000217209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 30827 {ECO:0000313|EMBL:AQQ15574.1,
RC   ECO:0000313|Proteomes:UP000217209};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-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; CP019688; AQQ15574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2HXL6; -.
DR   KEGG; cgv:CGLAU_08095; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000217209; Chromosome.
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:UP000217209};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         637
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   805 AA;  92293 MW;  48FD805687F37DDC CRC64;
     MDTHVHTPEL KDTLAGHVKG FSGKSPSNST VEKFWTGLSA AVVEQIADNW EETRNTYAGA
     RQAAYFSAEF LQGRALLNNL TNLGLVEHAE EITRELGHEL SDVLEAESDA ALGNGGLGRL
     AACFLDSAVT QDYPLTGYGL LYRYGLFRQE FVDGFQKEHP DAWKEAFYPF VVRRNTQQRF
     VKFDDMQVRA VPYDMPITGY GTDNVGTLRL WDALPMHEFD YDAFSSQRFT DAILEREAVH
     DITRVLYPND SSYAGKLLRV RQQYFFVSAS LQELVENYVT HHGDDLSRFH EYNSIQLNDT
     HPVLGIPELM RILLDEHDMS WEDAWNVTTK TFAYTNHTVL QEALETWEES IFKQLFWRIW
     EIVQEIDRRY RIDMEARGIE PELAHKYSPV HDGTVHMAWI ACYASYSING VAAIHTEIIK
     RDTLGYWHEL APEKFNNKTN GVTPRRWLRM CNPRLSELLD RLAGNDDWVT DLSKLKELRH
     FADDPEVMRE LREIKNANKR DFAEWINERQ GAEIDPDSIF DAQIKRLHEY KRQLMNALYI
     IDLYFRIKED GYTDVPKRTF IFGAKAAPGY VMAKGIIKLI NTVADFVNND PEVSKYIHVV
     FVENYNVSPA EHIIPASDVS EQISTAGKEA SGTSNMKFMM NGALTLGTMD GANVEIVDSV
     GEENAYIFGA LEDELPELKR NYNPREAATE TPGLMRALDA LVDGTLDDQG TGMFHDIRES
     LLNGFGYDAA DVYYVLGDFA SYRETRDRMA QEYYADPDHW ARMCWINICE SGRFSSDRTI
     RDYAEEVWKI QPTPIHPEHS NTEVN
//

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