ID A0A1L7CMR1_CORFL Unreviewed; 795 AA.
AC A0A1L7CMR1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CFLV_07980 {ECO:0000313|EMBL:APT87137.1}, F4V60_07810
GN {ECO:0000313|EMBL:KAA8721378.1};
OS Corynebacterium flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=28028 {ECO:0000313|EMBL:APT87137.1, ECO:0000313|Proteomes:UP000185479};
RN [1] {ECO:0000313|EMBL:APT87137.1, ECO:0000313|Proteomes:UP000185479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ8 {ECO:0000313|EMBL:APT87137.1,
RC ECO:0000313|Proteomes:UP000185479};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium flavescens OJ8(T)(=DSM
RT 20296(T)), isolated from cheese.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8721378.1, ECO:0000313|Proteomes:UP000322697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 28791T {ECO:0000313|EMBL:KAA8721378.1,
RC ECO:0000313|Proteomes:UP000322697};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) 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; CP009246; APT87137.1; -; Genomic_DNA.
DR EMBL; VXKK01000033; KAA8721378.1; -; Genomic_DNA.
DR RefSeq; WP_075730073.1; NZ_VXKK01000033.1.
DR AlphaFoldDB; A0A1L7CMR1; -.
DR STRING; 28028.CFLV_07980; -.
DR GeneID; 82880653; -.
DR KEGG; cfc:CFLV_07980; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000185479; Chromosome.
DR Proteomes; UP000322697; 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:UP000185479};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 635
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 795 AA; 90050 MW; A1DF51A5FDA62DFD CRC64;
MSKPQHSAFE SAVPAHVRAA AGVSPQRATD LKFWSGISAG VIDHIADNWE ATRATYAATR
QQHYFSAEFL QGRALLNNLT NLDLVEDAKV AAAAAGHELS DVLDAEHDAA LGNGGLGRLA
ACFLDSAVTQ DFPVTGYGLL YRYGLFRQTF ENGFQKEEPD SWMENGYSFV IRRASEQRRV
HFDDIDVRAI PYDMPITGYG TDNVGTLRLW KSEPINEFDY DAFNSQRFTD AIVERERVMD
ICRVLYPNDT TYEGKVLRVR QQYFFVSASL QAMVDNYIAQ HGGDLSGFAR YNSIQLNDTH
PVLAIPELMR ILLDHHAMSW DDAWKVVTET FAYTNHTVLA EALESWEISI FQKLFWRIWE
LIEEIDRRFR IDMAERGLDQ ARIDYMAPVS GGQVHMAWIA CYAAFSINGV AAIHTEIIKA
ETLKDWYQLW PEKFNNKTNG VTPRRWLRMC NPRLSALLTK LSGSNDWVTH LSQLKELRHF
GEDSAVLTEL MDIKAANKRD FAQWIKQHQG AEVDPDSIFD VQIKRLHEYK RQLMNALYIL
DLYFRIKEDG EDVPKRTFIF GAKAAPGYVR AKEIIKFINS VADLVNNDPD TNGIIRVIFV
ENYNVSPAEH IIPAADVSEQ ISLAGKEASG TSNMKFMMNG ALTLGTLDGA NIEIVEAAGE
ENAYIFGARN EEIPTLRETY DPGKLVAEVP GLSRVLDALT DGTLGDETRG LFGDLRSSLV
DGYGVYAQDT WYVLGDFASY RQTRDQMARD YVDRPEHWAK MCWANICESG RFSADRTIAD
YANEVWKIKP TRLQR
//
