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Database: UniProt
Entry: A0A3S0XRM8_CHLFR
LinkDB: A0A3S0XRM8_CHLFR
Original site: A0A3S0XRM8_CHLFR 
ID   A0A3S0XRM8_CHLFR        Unreviewed;       860 AA.
AC   A0A3S0XRM8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=PCC6912_43470 {ECO:0000313|EMBL:RUR76175.1};
OS   Chlorogloeopsis fritschii PCC 6912.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC   Chlorogloeopsis.
OX   NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR76175.1, ECO:0000313|Proteomes:UP000268857};
RN   [1] {ECO:0000313|EMBL:RUR76175.1, ECO:0000313|Proteomes:UP000268857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR76175.1,
RC   ECO:0000313|Proteomes:UP000268857};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUR76175.1}.
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DR   EMBL; RSCJ01000021; RUR76175.1; -; Genomic_DNA.
DR   RefSeq; WP_016876029.1; NZ_RSCJ01000021.1.
DR   AlphaFoldDB; A0A3S0XRM8; -.
DR   STRING; 211165.GCA_000317285_03406; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000268857; 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:UP000268857};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         676
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   860 AA;  99172 MW;  766A749024FC3428 CRC64;
     MNPPVETLQQ TIKVEDDRTG LSLETLKRAI ADNLFYIQGK YPAIATKNDF YMALAYTVRD
     RLLQRWLNTT ETYLKSKVKV VCYLSAEFLM GPHLSNNLVN LGIYDQVRRA VEESGLDFVE
     LREQEEEPGL GNGGLGRLAA CYMDSLASLE IPAIGYGIRY EFGIFDQEIR DGWQIEITDK
     WLRYGNPWEI ERPEASIDVK FGGYTQAYND ENGHYRVRWI PDIIVKGVPY DTPILGYKVN
     TANTLRLWKA EAPESFEFEA FNVGDYYGAV NEKVVAENIT KVLYPNDEPI QGKQLRLQQQ
     YFFVSCSLQD MIRLHLHRQD SLDNFHESFA VQLNDTHPAI GVAELMRLLV DEHQIDWDRA
     WQITQNTFAY TNHTLLPEAL EKWPLSLFGR LLPRHLQIIY EINQRFLGQV RAKYPDDHQR
     IARLSLIDES GEKYIRMAHL ASVGSHAING VAALHTKLLQ QDVLRDFYEL WPEKFTNKTN
     GVTPRRWIVV SNPKLAELIN RKIGTNWIKH LEELKQLEAF VEDAEFRQQW RQIKQDIKRD
     LAEYVKKNHA IDINPQSLFD VQVKRIHEYK RQHLNALYII TLYNQIKQNP NIDVVPRTFI
     FGGKAAPGYF MAKLIIKLIN SVAQVVNNDP DVRERLKVVF LPDYNVRFGQ RVYPAADLSE
     QISTAGKEAS GTGNMKFSMN GALTIGTLDG ANIEIREEVG AENFFLFGLT TPEVYALKAK
     GYNPWDYYHA NSQLKTVIDL ISSGFFSHGD TNLFRPLVDS LLYHDQYMLF ADYQSYVDCQ
     EQVNQAYRDE EKWTRMSILN AVRMGKFSSD RAIREYCQEI WNAQPVNVEM QEYVQPKPDM
     GKEAQSVAAQ ASQAWLGAKT
//
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