ID A0A091KLC2_9GRUI Unreviewed; 764 AA.
AC A0A091KLC2;
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=N324_04428 {ECO:0000313|EMBL:KFP40015.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP40015.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP40015.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP40015.1};
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; KK745211; KFP40015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KLC2; -.
DR Proteomes; UP000053330; 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:UP000053330};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 602
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP40015.1"
FT NON_TER 764
FT /evidence="ECO:0000313|EMBL:KFP40015.1"
SQ SEQUENCE 764 AA; 87572 MW; 7F774B88CFD2B7C9 CRC64;
PQRIYYLSLE FYMGRTLQNT MVNLGLQNAC DEAIYQLGLD LEELEEIEED AGLGNGGLGR
LAACFLDSMA TLGLAAYGYG IRYEFGIFNQ KIVDGWQVEE ADDWLRYGNP WEKARPEYML
PVHFYGRVDH TPEGVKWVDT QVVLAMPYDT PVPGYKNNTV NTMRLWSAKA PNDFNLQEFN
VGDYIEAVLD RNLAENISRV LYPNDNFFEG KELRLKQEYF VVAATLQDII RRFKSSKFGC
RDPVRTCFET FPDKVAIQLN DTHPALSIPE LMRILVDVEK VDWDKAWEIT KRTCAYTNHT
VLPEALERWP VSMFEKLLPR HLEIIYALNQ MHLDRVAALY PGDIDRLRRM SVIEEGDCKR
INMAHLCVIG SHAVNGVARI HSDIVKNTVF KDFYELEPEK FQNKTNGITP RRWLLLCNPG
LADVIAEKIG EGFITDLSQL KKLLDFINNE TFIRDVAKVK QENKLKFAAY LEEQYKVKIN
PSSMFDVQVK RIHEYKRQLL NCLHAITLYN RIRSDPSKTF VPRTIMIGGK AAPGYHMAKM
IIKLITSIGE VVNNDPYVGD KLKVIFLENY RVSLAEKVIP AADLSQQIST AGTEASGTGN
MKFMVNGALT IGTMDGANVE MAEEAGEENL FIFGMRVEDV EALDRQGYNA REYYDRLPEL
RQAIDQISSG FFSPRDPGCF RDVVNMLMYH DRFKVFADYE AYIQCQSQVD QLFMDPREWT
RKVIRNIACS GKFSSDRTIM EYAREIWGVE PSATKIPPPN LPRD
//
