ID A0A091VD78_NIPNI Unreviewed; 822 AA.
AC A0A091VD78;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=Y956_12661 {ECO:0000313|EMBL:KFR00730.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR00730.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFR00730.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR00730.1};
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; KL410891; KFR00730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VD78; -.
DR STRING; 128390.A0A091VD78; -.
DR eggNOG; KOG2099; Eukaryota.
DR Proteomes; UP000053283; 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:UP000053283};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 660
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR00730.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KFR00730.1"
SQ SEQUENCE 822 AA; 94186 MW; 0A7C5B7126717D74 CRC64;
AEVRKSFNRH LHFTLVKDRN VATPRDFRPG LAHTVRDHLA GSWLRPKCCA MCKHLALPPQ
RIYYLSLEFY MGRTLQNTMV NLGLQNACDE AIYQLGLDLE ELEEIEEDAG LGNGGLGRLA
ACFLDSMATL GLAAYGYGIR YEFGIFNQKI VDGWQVEEAD DWLRYGNPWE KARPEYMIPV
HFYGRVDHTP EGVKWIDTQV VLAMPYDTPV PGYKNNTVNT MRLWSAKAPN DFNLQEFNVG
DYIEAVLDRN LAENISRVLY PNDNFFEGKE LRLKQEYFVV AATLQDIIRR FKSSKFGCRD
PVRTCFETFP DKVAIQLNDT HPALSIPELM RILVDVEKVE WDKAWEITKR TCAYTNHTVL
PEALERWPVS MFEKLLPRHL EIIYALNQMH LDRVAALYPG DIDRLRRMSV IEEGDCKRIN
MAHLCVIGSH AVNGVARIHS DIVKNSVFKD FYELDPEKFQ NKTNGITPRR WLLLCNPGLA
DVIAEKIGEG FITDLSQLKK LLDFINNETF IRDVAKVKQE NKLKFAAYLE EQYKVKINPS
SMFDVQVKRI HEYKRQLLNC LHAITLYNRI RSDPSKSFVP RTIMIGGKAA PGYHMAKMII
KLITSIGEVI NNDPYVGDRL KVIFLENYRV SLAEKVIPAA DLSQQISTAG TEASGTGNMK
FMVNGALTIG TMDGANVEMA EEAGEENLFI FGMRVEDVEA LDRQGYNARE YYERLPELRQ
AIDQISSGFF SPRDPGCFKD VVNMLMYHDR FKVFADYEAY IKCQGQVDQL FMDPREWTKK
VIRNIACSGK FSSDRTIMEY AREIWGVEPS ATKIPPPNLP RD
//