ID S5SVC5_9CORY Unreviewed; 770 AA.
AC S5SVC5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=B841_08430 {ECO:0000313|EMBL:AGS35159.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS35159.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS35159.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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; CP003924; AGS35159.1; -; Genomic_DNA.
DR AlphaFoldDB; S5SVC5; -.
DR STRING; 1224163.B841_08430; -.
DR KEGG; cmd:B841_08430; -.
DR PATRIC; fig|1224163.3.peg.1694; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_11; -.
DR Proteomes; UP000015388; 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:UP000015388};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 610
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 770 AA; 88168 MW; 0CFD6F0471C1313C CRC64;
MSTRRKFWFG LSRAVVARIA ENWEDTRQAY GATRQQHYFS AEFLMGRALL NNLTNLELEE
TAKETAAELG HDLVDVLESE NDAALGNGGL GRLAACFLDS AVTHDLPVTG YGLLYRYGLF
RQEFVDGFQK ENPDPWREDG SPFTIRRGHQ RRTVRFDDMD VFAIPYDMPI TGYGTDNVGT
LRLWKSEPIE DFDYDAFNSQ HFTEAIVERE RVNDICRVLY PNDTSYEGKK LRVRQQYFFT
SASLQEIVAN YIKHHGEDLS DFAEYNSVQL NDTHPVLAIP ELMRLLMDKH GLGWDEAWKI
TSETFAYTNH TVLTEALETW EISIFQQMFW RIWQIIEEID RRFRLDMTER GLDEDAIHRM
APVSDGLVHM AWIACYAAYS INGVAAIHTE IIKAETLGDW HAIWPEKFNN KTNGVTPRRW
LKMCNPRLSA LLTRLVGSDE WVTDLDVLKS LRPYETDEKV LGELMEIKAA NKVDFAEWIK
DRQGIDIDPE SIYDVQIKRL HEYKRQLMNA LYILDLYFRI KEDGEQDVPP RTFVFGAKAA
PGYVRAKAII KLINEIGELV NNDPEVSKTL KVVFIENYNV SPAEHIIPAT DVSEQISTAG
KEASGTGNMK FMMNGALTLG TMDGANVEIA DAVGEDNAYI FGARVEQFDE LLEHYSPHEL
YETTPGLKRT LDAFDDGTLD DGGTGMFHDL KNSLIHGYGP HSNDTYYVLG DFEDYRATRD
RMAADYVGDP MDWARMCWVN VCESGRFSSD RTIHDYADEV WKLEATPVRK
//
