ID A0A0V7ZCK2_9CYAN Unreviewed; 853 AA.
AC A0A0V7ZCK2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=BC008_08580 {ECO:0000313|EMBL:KST62076.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST62076.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST62076.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST62076.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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:KST62076.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMTZ01000163; KST62076.1; -; Genomic_DNA.
DR RefSeq; WP_027846513.1; NZ_LMTZ01000163.1.
DR AlphaFoldDB; A0A0V7ZCK2; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000053372; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053372};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..121
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 853 AA; 97155 MW; 9ED51DDD20A7F288 CRC64;
MQPIRTFNVS PSLPQRLEPL RQLAYNLHWD WNAESKDLFN RLDPELWESS RHNPVLMLGT
ISQKRLMEVV EDDGFLAQMD RAAQQLADYL KEHTWYQKQR SDKPKECYAY FSAEFGLTDC
LPIYSGGLGV LAGDHLKSAS DLGLPLVGVG LLYQQGYFAQ YLNADGWQQE RYPINDFYNM
PLHLERNADG SELRIAVNYP GREVYARVWR VQVGKVPLYM LDTNIEPNKT YDHDITDQLY
GGDIDMRIHQ EIMLGIGGVQ MLKALGYDVT AYHMNEGHAA FSALERIRIL IQEQGLNYAQ
AKQVVAASNI FTTHTPVPAG IDLFPPDKVL YYLGYYGDIF GLSKDQFLAL GRENTGDLSS
PFSMAVLALK MAVFSNGVAQ LHGKVSRQMF KGLWRNLPVN EVPIAAITNG VHARSCVAKS
TQELYDRYLG PNWSSTPADR PMWGKMEVIP DEELWRNHER CRLDMTLYVR QRLVKHLRDR
GASPREIAQA QEVLDPKVLT IGFARRFATY KRATLWMRDL ERIKKILLGD KNRKLQFVIA
GKAHPKDIPG KELIRDINRF IREQGLEKQV VFVPNYDIHI ARLMVSGCDV WLNTPRRPRE
ASGTSGMKAA MNGLPNLSVL DGWWDEANYV LTGWAIGHGE TYEDPNYQDE IEANALYDII
EKEVMPLFYN RDGDGLPRGW IAKMKDAIRL NCPFFNTARM LAEYAQRGYF PASDRYYSLS
SNNYTPAKEV AAWEENLKEN WYNIKIKDID VSSSPDIQVN QTVAVKAKID LTSLTNNDVR
VELYQGAINA DGDIVNGVPV VMDYQGEDPS NLSIYTADIT YKTSGLQGLS LRVLPKHKHL
SNPYEPRLIV WAE
//
