UniProt: A0A1M4Z1C1

Database: UniProt
Entry: A0A1M4Z1C1_9CLOT

LinkDB:  A0A1M4Z1C1_9CLOT 
Original site:  A0A1M4Z1C1_9CLOT

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

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ID   A0A1M4Z1C1_9CLOT        Unreviewed;       811 AA.
AC   A0A1M4Z1C1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=SAMN05443638_13511 {ECO:0000313|EMBL:SHF11765.1};
OS   Clostridium fallax.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1533 {ECO:0000313|EMBL:SHF11765.1, ECO:0000313|Proteomes:UP000184035};
RN   [1] {ECO:0000313|EMBL:SHF11765.1, ECO:0000313|Proteomes:UP000184035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2631 {ECO:0000313|EMBL:SHF11765.1,
RC   ECO:0000313|Proteomes:UP000184035};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQVM01000035; SHF11765.1; -; Genomic_DNA.
DR   RefSeq; WP_072897578.1; NZ_UAVV01000005.1.
DR   AlphaFoldDB; A0A1M4Z1C1; -.
DR   STRING; 1533.SAMN05443638_13511; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000184035; 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:UP000184035};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         655
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   811 AA;  93988 MW;  1843D4C2ED4EFD59 CRC64;
     MFYIDKNTFK EDYLEKYIEL HGEEFKFGNM RQKYEALGSL VRDYITKIKI ENNKTNNHDN
     KQVYYFSMEF LLGRLLGSNL LNLGIRDICK EGLNELGIDL DELESFEQDQ GLGNGGLGRL
     AACFLDSMAS LNIPGHGCGI RYKYGFFEQK IINGSQVEAP ENWLKCENVW EIRKPSNSQI
     VRFGGEVRME KINGRLSFIH INYDPVLAVP YDTLIIGHEN SAVNNLRLWS AEPVSNEFDF
     SSFSRGEYLK AIEYKNSVEA ISNVLYPDNT FYEGQMLRLK QQYFFVSAGI QSIISNFKKH
     GGDIFNLNES IAIHINDTHP TLAIPELMRI LLDEELLSWE DAWRITTSTI SYTNHTIMAE
     ALEKWPIEMF KKLLPRIYMI VNEINERFCK DLWDKYTYQW DKISRMAIMA DGYIRMANLA
     IVGSYSVNGV AKLHTEILKK QVMSDFYYFY PNKFNNKTNG ITHRRWLIKC NPQLSNLLKE
     TIGDGWVKHP TDMEYLYKFK DDENIKDRLA LIKKNNKIAL SEFIKNNQGI NIDTNSIFDV
     QVKRIHAYKR QVLNVLRIMN LYNQLIENPN LDIEPRTFIF AGKAAPGYYL AKKIIELINA
     IATKINNDRR VKDKIKVVFM ENYRTSLAEI IIPAADISEQ ISTTTKEASG TSNMKFMMNG
     AITVATLDGA NIEIKDQVSE ENIIIFGLTE KEVLDYYSKG GYSSYDIYNN DIRINRILND
     LVNGAYCNDK ENFRAIYNHL LTYNDEFFDL RDFDSFVKAQ DRVDKLYRDK SKWYSMSIIN
     IAKSGIFSSD RTIYEYAKGI WDVPNSSCKD K
//

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