ID A0A0G2IWJ9_9SYNE Unreviewed; 843 AA.
AC A0A0G2IWJ9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=TE42_03955 {ECO:0000313|EMBL:KKZ12624.1};
OS Candidatus Synechococcus spongiarum SP3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1604020 {ECO:0000313|EMBL:KKZ12624.1, ECO:0000313|Proteomes:UP000035067};
RN [1] {ECO:0000313|EMBL:KKZ12624.1, ECO:0000313|Proteomes:UP000035067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP3 {ECO:0000313|EMBL:KKZ12624.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (JAN-2015) 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}.
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:KKZ12624.1}.
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DR EMBL; JXQG01000016; KKZ12624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2IWJ9; -.
DR PATRIC; fig|1604020.3.peg.2597; -.
DR Proteomes; UP000035067; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 843 AA; 95575 MW; 09D9395A62AB02E8 CRC64;
MTNPTPAEFR LPTPGCYADP ERSGLRASEL FDGMTEHLFF TLGKLAPSAT KHDLYMALSY
AVRDRLMMRY LAGKQALRET PRKTVAYLSA EFLIGPQLGN NLVMLGIEEA AVLALQQFGV
QSLDTVLEVE EEPGLGNGGL GRLAACYMES LASLQVPAVG YGIRYEFGIF DQLIRDGWQV
EITDKWLKAG WPWELPQPDE ACVVGFGGHT ESYTDAKGHY HSRWVPTEHA IGIPHDVPVL
GYQVNTCNRL RLWRADATES FDFYAFNIGD YYGAVEEKVG SETLSKVLYP NDGTDEGRRL
RLKQQHFFVS CSLQDMLRSF EKRQIPLEEF PQHWAIQMND THPAIAVAEL MRLLIDEKHL
PWGTAWGITS RCLAYTNHTL LPEALEKWNL PLFASLLPRH LEIIYEINRR FLQQVRLRYP
GNNQILRTLS IIDEDGDKAV RMAHLATIGS HHINGVAALH SELVKTNLMP EFSALWPEKF
TNVTNGVTPR RWLALANPKL RALLNEVIGE GWIQDLDQLS KLEAFQDDKS FLERWEQTHL
AAKRNLASII HRRTGILVDP ASLFDVQVKR IHEYKRQHLN ALQVAAQYVR LKEGCADHMP
YRTVLFGGKA APGYYMAKLM IRFLNGIANT INSDPDMDGR LRVLFLPDYN VTTGQSIYPA
SDLSEQISTA GKEASGTGNM KFALNGSLTV GTLDGANLEI RDRVGEENFF LFGYTAAELQ
NLRQDGYRPR EVLAQQPLLQ QVVNLVQQGH FSNGDREMFQ PLIHNLTNDD PFFVFADFTD
YLRAQEDVSQ AWLDRPRWNR MSLLNSARNG FFSSDRSVRE YCEHIWKAQP FPVEVKCELP
GIA
//
