GenomeNet

Database: UniProt
Entry: U6MRH7_9EIME
LinkDB: U6MRH7_9EIME
Original site: U6MRH7_9EIME 
ID   U6MRH7_9EIME            Unreviewed;       971 AA.
AC   U6MRH7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=ENH_00003600 {ECO:0000313|EMBL:CDJ65054.1};
OS   Eimeria necatrix.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ65054.1};
RN   [1] {ECO:0000313|EMBL:CDJ65054.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ65054.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ65054.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ65054.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) 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   ---------------------------------------------------------------------------
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; HG723042; CDJ65054.1; -; Genomic_DNA.
DR   RefSeq; XP_013433521.1; XM_013578067.1.
DR   AlphaFoldDB; U6MRH7; -.
DR   GeneID; 25470554; -.
DR   VEuPathDB; ToxoDB:ENH_00003600; -.
DR   OrthoDB; 5473321at2759; -.
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   Transferase {ECO:0000256|RuleBase:RU000587}.
FT   REGION          906..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..971
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         732
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   971 AA;  111566 MW;  E403B914B827CA0E CRC64;
     MATGVEDVFT RDTNQHWEMK RKASFSKLTG AVPRTIPGMY NVVEDPHADD KKEKLWKLME
     TYLPSDVHSI QRSIVNHVEY TLAKTRFNLD PESCYRAAAF SVRDRLIETL NDTNAFFHEK
     DVKRAYYLSL EFLLGRAFQN ALVNLDIEKN YRTALADLGF SLEQLYEFEH DPALGNGGLG
     RLAACFLDSM ATLNLPCWGY GIRYTYGIFE QKIVNGRQVE YPDYWLTLSN PWEIERPDCT
     YAVRIYGSVK EYRDPQSGRM RSKWVGGEIV QAMAYDTPIP GFDTYNTINL RLWKACPSKE
     FDFHLFDVGR YLESVRERQN AESISAVLYP NDNTMEGKEL RLKQQYFFCC ATIQDVLRRF
     KKVPGRDWKE LPDKIQCQLN DTHPTIAIPE LMRILLDVEG LDWDTAWDLT RRCFNYTNHT
     VLPEALEKWS ADLISRLLPR HLLIINEINF RFLNEARSIF GDDWNKIGRM SIYEEGNEKR
     IRMANLAVIG GRHVNGVAAI HSELVKKNLF PEFVEFYSRQ GVNDKFLNVT NGVTPRRWIY
     CSNRGLADLF SNWLGSDSWL KELDMIAGLM NHIDNPSFRA EWAAVKKENK KRLALWVEQR
     CNVKLDVDTM LFDIQVKRIH EYKRQLLNII YIIHRYLTLK RMQPADRSNM LPRACLIGGK
     AAPGYYTAKT IIKMANSVAQ IVNNDPDVDK YLKVVFLPNY NVSNAQVIIP ASDISQHIST
     AGTEASGTSN IKFVMNGGLI IGTLDGANIE IREEGGDETM FIFGAKEHEV DHIRERARNG
     SYPMDHRMRE VFDWIRSGAL ACGDDKSHGD FCAILDTICN NGNGNNGDYY LLIHDFPDYC
     RAQDEVDRTY RNPDKWWRLS IKAAASMGKF STDRCMREYA EKIWGISRCE RPPPDEVLRA
     RSFANDKKSN AGPSHGLNRS NNNINTTSTN TNSNESSGTD NLRAPGESES QKRGKHKKEN
     KQDKREVVVD S
//
DBGET integrated database retrieval system