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
//