ID A0A087QPB6_APTFO Unreviewed; 797 AA.
AC A0A087QPB6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Flags: Fragment;
GN ORFNames=AS27_06129 {ECO:0000313|EMBL:KFM03070.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03070.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM03070.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03070.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC enzymatically active phosphorylase A. {ECO:0000256|ARBA:ARBA00038533}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KL225792; KFM03070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QPB6; -.
DR STRING; 9233.A0A087QPB6; -.
DR Proteomes; UP000053286; 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:0005977; P:glycogen 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:SF29; GLYCOGEN PHOSPHORYLASE, BRAIN FORM; 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 635
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM03070.1"
FT NON_TER 797
FT /evidence="ECO:0000313|EMBL:KFM03070.1"
SQ SEQUENCE 797 AA; 91550 MW; C9144AF27EC133E4 CRC64;
APPRDYYFAL AHTVRDHLVG RWIRTQQHYY ERDPKRIYYL SLEFYMGRTL QNTMVNLGLQ
NACDEAIYQL GLDLEELEEI EEDAGLGNGG LGRLAACFLD SMATLGLAAY GYGIRYEFGI
FNQKIVDGWQ VEEADDWLRY GNPWEKARPE YMLPVHFYGR VDHTPEGVKW IDTQVVLAMP
YDTPVPGYKN NTVNTMRLWS AKAPNDFNLQ EFNVGDYIEA VLDRNLAENI SRVLYPNDNF
FEGKELRLKQ EYFVVAATLQ DIIRRFKSSK FGCRDPVRTC FETFPDKVAI QLNDTHPALS
IPELMRILVD VEKVDWDKAW EITKRTCAYT NHTVLPEALE RWPVSMFEKL LPRHLEIIYA
LNQMHLDRVA ALYPGDTDRL RRMSVIEEGD CKRINMAHLC VIGSHAVNGV ARIHSDIVKN
SVFKDFCELE PEKFQNKTNG ITPRRWLLLC NPGLADVIAE KIGEGFITDL SQLKKLLDFI
NNEAFIRDVA KVKQENKLKF AAYLEEQYKV KINPSSMFDV QVKRIHEYKR QLLNCLHAIT
LYNRIRSDPS KSFVPRTIMI GGKAAPGYHM AKMIIKLITS IGEVINNDPY VGDRLKVIFL
ENYRVSLAEK VIPAADLSQQ ISTAGTEASG TGNMKFMVNG ALTIGTMDGA NVEMAEEAGE
ENLFIFGMRV EDVEALDRQG YNAQEYYERL PELRQAIDQL SSGFFSPRDP GCFRDVVNML
MYHDRFKVFA DYEAYIKCQG QVDQLFMDPR EWTKKVIRNI ACSGKFSSDR TIMEYAREIW
GVEPPATKIP PPNLPRD
//
