ID   A0A1J1JBY9_9DIPT        Unreviewed;       863 AA.
AC   A0A1J1JBY9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=CLUMA_CG021252 {ECO:0000313|EMBL:CRL08601.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL08601.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRL08601.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   EMBL; CVRI01000075; CRL08601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1JBY9; -.
DR   STRING; 568069.A0A1J1JBY9; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000183832; 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:UP000183832};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         701
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   863 AA;  99523 MW;  F7486125229E5A2E CRC64;
     MSRPISDIDK RKQISVRGIA QVEDVGEVKK GFNRHLHFTL IKDRNVATPR DYYFALAHCV
     KDHLVSRWIR TQQHYFEKDP KRVYYLSLEF YMGRSLTNTM INIGLQGTVD EALYQMGLDI
     EELEDMEQDA GLGNGGLGRL AACFLDSMAT LAMPAVGYGI RYDYGIFAQR IRNFEQTEEP
     DDWLRFGCPW EKARPEYMIP VNFFGRVLDT PDGKRWVDTQ IVYAMPYDNP IPGYNNNVVN
     TMRLWSAKSP IEFNLKFCKC QKFNLLLFIY FLAFSLVVND GDYIQAVLDR NLAENISRVL
     YPNDNMFEGK ELRLKQQYFL SAASLADIIR RFKTSKYAQA KNPRDAMKTM YEKVAVQLND
     THPSISIPEL MRVLVDEEKL SWDEAWNVTT KVFSYTNHTV LPEALERWPT SLLESMLPRH
     LEIIYHINFL WLKEVEKNFP GDMDRLRRMS MVEEDGEKRI NMARLSIVGS HAVNGVAAIH
     TEILKRDLFR DFFELSPDKF QNKTNGITPR RWLLLCNPGL ADLICEKIGD EWPVHLDQLA
     QLRKWAKDPT FQRAVAKVKQ ENKFKLASIL EHDYGVKVNP SSMFDIQVKR IHEYKRQLLN
     LLYIVTMYNR IKRDPTANFV PRTVMIGGKA APGYYMAKKI IQLINKVGHA VNNDPIVGDK
     LKVIFLENYR VTLAEKIMPA SDLSQQLSTA GTEASGTGNM KFMLNGALTV GTLDGANVEM
     AEEMGNENIF IFGMNVDEVE AMQKRGYNAW DYYNKNSELK QVIDQISGGY YSPGNPDEFK
     DVTNMLMQYD RFLTFADFDD YVKKQDEVSA TYQNQSKWLE MAIHNIASSG KFSSDRTISQ
     YAREIWGVEP SFEKLPNPHE VIA
//