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
//