ID A0A2A2JB20_9BILA Unreviewed; 847 AA.
AC A0A2A2JB20;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=WR25_08882 {ECO:0000313|EMBL:PAV58893.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV58893.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV58893.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV58893.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV58893.1}.
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DR EMBL; LIAE01010556; PAV58893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JB20; -.
DR STRING; 2018661.A0A2A2JB20; -.
DR Proteomes; UP000218231; 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 InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 682
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 847 AA; 97390 MW; 55FD5D9E271778E9 CRC64;
MMSDHDRRKQ ISVRGIAQVE NVANIKKAFN RHLHFSIIKD RNVATMRDYY FALANTVRDH
LVSRWIRTQQ YYYENDPKRV YYLSLEFYMG RTLSNTMMNL GIQATVDEAL YQLGLDIEDL
QEIEEDAGLG NGGLGRLAAC FLDSMATLGI PAYGYGLRYE YGIFKQLIRD GWQVEEPDDW
LRFGNPWEKA RPEYMLPVNF YGKVIKDEKG KSKWVDTQLV FAMPYDTPVP GYRNNVVNTL
RLWSAKAENH FHLKFFNDGD YVQAVMDRNL SENITRVLYP NDNMFIGKEL RLKQQYFLVA
ATLQDIIRRY KSSKYGSRES IRVTFENFPE KVAIQLNDTH PSIGIPELMR LLVDLEGLEW
DQAWDVCVRT FAYTNHTLLP EALERWPVSM LQTLLPRHLE IIYEINQKFM EAISVKFPGD
FDRMRRMSIV EEADQFGEKR INMANLCIVA SHAINGVAAL HSDLLKSTTF KDFYEFFPEK
FQNKTNGITP RRWLLLSNPS LADVIVEKIG EDWITNLDEL KKIKEFAAEP QLLDQIRRVK
AENKTRVAQF LSDEYNVDIN PSSLFDVHVK RIHEYKRQLL NILHVITLYN RIKADPNIDM
VPRTVLYGGK AAPGYHMAKQ IIRLITAVGE IVNNDPVVGD KLKVIFLENY RVSMAEKIIP
AADLSEQIST AGTEASGTGN MKFMLNGALT IGTLDGANVE MAEEMGKENI FIFGMNVDEV
EALQKKGYSS QEFIQKTPAL KQIVEQIEGG LFTPEQPDQL RDLSNMLRYH DRFMVCADFE
AYVACQDKVA SVYRDQNAWS RMALLNIAST GKFSTDRTIA EYARQIWGVE PGQTSLPAPY
ETAEEKP
//
