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Database: UniProt
Entry: A0A091VD78_NIPNI
LinkDB: A0A091VD78_NIPNI
Original site: A0A091VD78_NIPNI 
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
//
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