ID A0A2T1D4R0_9CYAN Unreviewed; 838 AA.
AC A0A2T1D4R0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=C7B65_24265 {ECO:0000313|EMBL:PSB15469.1};
OS Phormidesmis priestleyi ULC007.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1920490 {ECO:0000313|EMBL:PSB15469.1, ECO:0000313|Proteomes:UP000238634};
RN [1] {ECO:0000313|EMBL:PSB15469.1, ECO:0000313|Proteomes:UP000238634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC007 {ECO:0000313|EMBL:PSB15469.1,
RC ECO:0000313|Proteomes:UP000238634};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB15469.1, ECO:0000313|Proteomes:UP000238634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC007 {ECO:0000313|EMBL:PSB15469.1,
RC ECO:0000313|Proteomes:UP000238634};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) 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 -!- 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|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:PSB15469.1}.
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DR EMBL; PVWG01000060; PSB15469.1; -; Genomic_DNA.
DR RefSeq; WP_073075050.1; NZ_PVWG01000060.1.
DR AlphaFoldDB; A0A2T1D4R0; -.
DR STRING; 1920490.GCA_001895925_02902; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000238634; 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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000238634};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 838 AA; 96242 MW; 613D4412EDABA732 CRC64;
MLGKNDRTGM TLENLKQALI DHLYYIQGRD EQFATLNDYY MALAYTVRDR LTDRRIKTAQ
TYFQKDTKVV YYLSAEFLVG RLSANNLINL GIYDEMKEAT KKMGLNLEDL LEQEEEPGLG
NGGLGRLAAC FLDSLATLEI PAMGYGIRYE FGIFDQFIVD GWQRERPDNW LRYGNPWEIA
RIDYTVEIKL GGHTEAVTDA QGGYRVRWVP QDTVYGVPYD TPIPGYRNNT VNTLRLWSAK
ASEDFDFQVF DAGQYTQAVA EKTFSENISK VLYPNDNTPQ GKELRLQQQY FFVSCSLQDI
IRSYLRNHDN FDQFSNKVAI QLNDTHPSIG VAELMRLLID EHALDWNRAW DITRQTFAYT
NHTLLIEALE RWSVSLFGRL LPRHLEIIYE INNRFLDEIR RKFPGDRDRL ERMSLIQEGD
DKHIRMAYLA FVGSHTTNGV AALHTELLKR DVMHDFYEMY PEKFQNKTNG VTPRRWLLMS
NPKLSDLITS KIGDRWVKDL SELRKLEAFV DDAEFQKTWR EIKQDNKRTL ADYIQSDNNL
EIDPDSMFDV QVKRIHEYKR QLLNALHVIT LYNRIKQHGA SPSDVPRTFI FGGKAAPGYF
MAKLVIKLIN SVAEVVNNDP DVKGLLKVVY LSNFSVSLGQ ITYPAADLSE QISTAGKEAS
GTGNMKFALS GALTIGTLDG ANVEIREEVG EENFFLFGLD AQEVMAMKAQ GYNPLAYYRN
NAALKTVIDQ IASGFFSPKE PALFKSIVDS LLYKDEYMLL ADYQFYVDCQ EKVSLAYQDQ
TQWTRMSILN VARMGKFSSD YTISEYCKSI WHVEPVPVSL EDCELPTPRL KPSLVDQV
//
