ID U3GYL1_9CORY Unreviewed; 794 AA.
AC U3GYL1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=CARG_06210 {ECO:0000313|EMBL:AGU15366.1};
OS Corynebacterium argentoratense DSM 44202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15366.1, ECO:0000313|Proteomes:UP000016943};
RN [1] {ECO:0000313|EMBL:AGU15366.1, ECO:0000313|Proteomes:UP000016943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15366.1};
RX PubMed=24092787;
RA Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA Ruckert C., Tauch A.;
RT "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL Genome Announc. 1:e00793-13(2013).
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; CP006365; AGU15366.1; -; Genomic_DNA.
DR RefSeq; WP_020976524.1; NC_022198.1.
DR AlphaFoldDB; U3GYL1; -.
DR STRING; 1348662.CARG_06210; -.
DR GeneID; 78250014; -.
DR KEGG; caz:CARG_06210; -.
DR PATRIC; fig|1348662.3.peg.1216; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000016943; 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:UP000016943};
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 794 AA; 89990 MW; A2CA1738D77A5C5C CRC64;
MSKHFDAATV GSFVRAASGT APTDATDRKF WFGLSANVME ELADKWQATT DAYSATRQQH
YLSAEFLMGR ALLNNLTNLG LVEDAEQAAR EHGHELVDVL EAENDAALGN GGLGRLAACF
LDSCATQDLP VTGYGILYRY GLFKQNIEGG YQTEEPDAWM EDGYPFVIRR EEQQRIVTFD
DMIVRAVPYD MPISGYGTNN VGTLRLWKAE PLEEFDYDAF NSQRFTDAIV ERERVMDLCR
VLYPNDTTYA GKALRVRQQY FFSSASLQAM IANYIEHHGE DLSDFAKYNS IQLNDTHPVI
AIPELMRLLM DDHGLGWDEA WKIVTETFAY TNHTVLPEAL EQWEVSIFQQ LFYRVWEIVA
EIDRRFRLDM AERGLDEGTI HYLSPVHDGH VYMGWLACYA AYSINGVAAI HTEIIKAETL
KQWHELWPEK FNNKTNGVTP RRWLKMCNPR LSDLLTRLAG GDQWVKNLDE LKKLRSFADN
DAVMQELLEI KDANKQDFAE WIAQRQGIDV DPHSIFDVQI KRLHEYKRQL MNALYILDLY
FRITDGEVVI DDVPARTFIF GAKAAPGYVR AKAIIKLINE IAELVNNDPV VSTKLRVVFV
ENYNVSPAEH IIPAADVSEQ ISTAGKEASG TSNMKFMMNG ALTLGTLDGA NVEIADAVGE
DNAYIFGAKV EELPELKAHY NPYALYETVP GLKRVLDALI DGTLGDDHSG AFHDLRGSLL
DGNGWETPDV YYVLGDFAAY RETRDAMAND YYADRLHWAR MCWINICESG RFSSDRTISD
YANEVWKIEP TPVR
//
