ID K8EN22_9CHLO Unreviewed; 1489 AA.
AC K8EN22;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Bathy13g02560 {ECO:0000313|EMBL:CCO19374.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO19374.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO19374.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO19374.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) 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|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}.
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DR EMBL; FO082266; CCO19374.1; -; Genomic_DNA.
DR RefSeq; XP_007509571.1; XM_007509509.1.
DR STRING; 41875.K8EN22; -.
DR GeneID; 19012208; -.
DR KEGG; bpg:Bathy13g02560; -.
DR eggNOG; KOG2099; Eukaryota.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000198341; Chromosome_13.
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; 3.
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; 3.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 3.
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|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1489 AA; 168390 MW; 68A52B4E7D19AD94 CRC64;
MGPKDENPPP PCPPPPPPPG FWAQLDAQEE QRERNHNHRH RHRRRSREEF SSSSVSSLSP
SRRNDDDDKD ALSEANDEDE EGMKKKTTKE DDNKNNELVN KEEKTNEEVF SRFLEDAANA
QEKDYRNSMR VGSSKSMREL ARYDAAQNME RRRRKERGEE NDEDDDEEDD DDEDERWVET
ENLRSASRMM NTNSTNTNNG SKYEEEDGGL NLAGKHQSSF ADLNYNSSGS DFARGGQAAP
EIYRSLITKR REMEEEEEEE EEEQRRKSDA YFSKHFNSHP YSLAGGGTTG HHFNSIGLGF
GGSARELERQ RQSQILILQR QKQKQRSLES YDDLKNAKED TKFFSRQSYT ESDFEDDDDD
DDNFDKYEDK EEEEDDDDDD ELDDSRSYGD PEIRPMHATM TTTITNGSAA SVASPPVTRL
LHEQHQYPSW VSESGPDGGR STPGTPRASS TNKQKDSTTN NESSTTGTRL SNRFSNGNHS
TVPTAPTSTT QKNFHGEVVS NMNSDRVNNV EALFSPNNKN ITMTTNSEKT KAKFAALTID
PSRKPASTTT PATTKRSYLS SDSSSVRKSI LEHYDYTLAR RRYKMDAVSV YEACALSLRD
RLVERWSDTQ QFYASSEECK DLKMVYYMSL EFLVGRSLGN AASNLGLRMP YADALRTLGH
ELEDIAQREK EPALGNGGLG RLASCFLDSL ATQNYPGWGY GIRYKYGMFE QALIDGKQVE
LPDYWLTSGN PWEVERLDVT YKVRFYGRSV QYTRKRKVSL NKMAASQRMK TIRENPEKEN
FGNVPPPHDA SNGESRANND AYPPSPPTSK KEIDETETRF SWEGGEIVVA VAYDTPVPGY
GTYNANNMRL WSSKPSHEFD LKSFNAGDYI AAIEQKERGE SISSVLYPND DTHVGKELRL
KQQFFFCSAT LQDILHQFKK SAARYNNSVM KAYAADNANA EIKSPSSTSS GNNNTNVIPG
LRTLKDLPKR VAIQLNDTHP AIGVPEFMRL LLDEELLCWE DAWNITKNVF SYTNHTIMTE
AMEKWPVPML SELLPRHAEI IFEINHRFLE SVRKKWPGDE QKVRRMSIVE ESEPKMFRMA
NLAVIGSHTV NGVAEMHTNL VKTILFADFC ELGDTKFRNV TNGVTPRRWI LQANPKLAKM
YTDLAGPGWV NDMKRLEALQ SFCDDDDFCE RFRAIKKQNK RRVASFLEQT CRLNYKIAPN
ALFDMQIKRI HEYKRQLLNV LGIIHRFDAV LRATPQERAK IVPRVFIIAG KAAPGYDTAR
LIIQLACAVA KVVNETPECA GVLTVCFVPN FNVSIAELLI PASDVSQHIS LAGTEASGTG
NMKFAMNGGL IVGTRDGANV EIARAIGSDN IFQFGATVDE VKSLKKTANT RNPAPDERLA
NVCAIIHSGI FGDAKKLGFN RLCSSTLTPT TDLYLCGHDF ASYLDAQARA DEVYLDEHLW
TRKSVLSALR MAKFSTDRTI KEYAEKIWNV EAKAFLPQHV KERLKVGRK
//
