ID A0A1L7D2E3_9CORY Unreviewed; 792 AA.
AC A0A1L7D2E3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CPHO_04535 {ECO:0000313|EMBL:APT92278.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT92278.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT92278.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT92278.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) 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; CP009249; APT92278.1; -; Genomic_DNA.
DR RefSeq; WP_075733579.1; NZ_VXKJ01000035.1.
DR AlphaFoldDB; A0A1L7D2E3; -.
DR STRING; 161895.CPHO_04535; -.
DR KEGG; cpho:CPHO_04535; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000185491; 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:UP000185491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 632
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 792 AA; 89586 MW; 26D51BF635861639 CRC64;
MSNLEFAEAI PGHVRAAAGV SPDAASDRKY WSGLSRSVVR EIADNWEATR KAYAGARQQH
YLSAEFLQGR ALLNNLTNLG RVEEAKEAVR ASGRELVDVL EAEHDAALGN GGLGRLAACF
LDSAVTQDYP VTGYGILYRY GLFRQSFDNG HQVERPDAWM ENGYDFVIRR SAQQYRIHFD
DMEARAVPYD MPITGYGTDN VGTLRLWKAE PVEEFDYDAF NSQRFTEAIV ERERVMDICR
VLYPNDTTYE GKVLRVRQQY FFVSASLQQM IDNYITQHGE DLSGFATYNC IQLNDTHPVL
AIPELMRLLM DVHGLGWDKA WEIVTQTFAY TNHTVLAEAL ESWEVSIFQK LFWRIWQIVE
EIDRRFRLDM AGRGLDQGRI DYMAPVSGGH VHMAWIACYA AYSINGVAAL HTEIIKADTL
SEWHDLWPEK FNNKTNGVTP RRWLKMCNPR LSELLTDKAG SDEWVTDLSQ LQKLAPLADD
AAVLESLQDI KAGNKRDFAA WILNHQGAEV DPESIFDVQI KRLHEYKRQL MNALYILDLY
FRIKEDGEDV PKRTFIFGAK AAPGYVRAKA IIKLINTIGD LVNNDPATKD IIRVVFVENY
NVSPAEKIIP AADVSEQISV AGKEASGTSN MKFMMNGALT LGTMDGANVE IVEAVGEENA
YIFGARVEEI PELRRDYNPS ELYHTVPGLA RVLDALTSDL LGIENQGLFA DLRASLLDGY
GEHAQDQYYV LGDYASYREA RDRMATDYVE DPKAWARMAW LNICHSGRFS SDRTIADYAQ
EVWKLEPTPI SK
//
