ID A0A1C1CY55_9EURO Unreviewed; 896 AA.
AC A0A1C1CY55;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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};
GN Name=GPH1 {ECO:0000313|EMBL:OCT53401.1};
GN ORFNames=CLCR_09513 {ECO:0000313|EMBL:OCT53401.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT53401.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-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}.
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:OCT53401.1}.
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DR EMBL; LGRB01000008; OCT53401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CY55; -.
DR STRING; 86049.A0A1C1CY55; -.
DR VEuPathDB; FungiDB:CLCR_09513; -.
DR VEuPathDB; FungiDB:G647_00369; -.
DR eggNOG; KOG2099; Eukaryota.
DR Proteomes; UP000094526; 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:0005975; P:carbohydrate 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:SF3; GLYCOGEN PHOSPHORYLASE; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 733
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 896 AA; 101897 MW; 9945BE4C53873E08 CRC64;
MAAAAAAQTP RERKPSTSAP ISTLTGPVGP GFTRPKHKRT ATGFGAGDIK AVESSIPEHM
REAWRKFSPR GFTTKEEFEA EAVKHIETTL ARSLFNCDEL AAYSGTALAF RDRLIIDWNK
TQQRQTFADQ KRIYYLSLEF LMGRALDNAM LNVGLKNVAK EGLADLGFRI EDIIEQEHDA
ALGNGGLGRL AACFLDSLAT LNYAAWGYGL RYRYGIFKQE IQDGYQVEIP DYWLDFNPWE
FPRHDVSVDV QFYGWVNKYT DDEGKQIVSW QDGEIVTATA YDVPVPGYGT PTVNNLRLWS
SKASSGEFDF AKFNSGEYES AVADEQRAET ISAVLYPNDN LERGKELRLK QQYFWCAASL
HDIVRRFKKS KRKWSEFPDQ VAIQLNDTHP TLAIVELQRI LIDMEGLEWD AAWDIVTRTF
GYTNHTVLPE ALEKWSVPLV QNLLPRHIQI IYEINLYFLQ SVERRFPKDR DLLGRVSIIE
ESQPKMVRMA FLAIIGSHKV NGVAELHSDL IKTTIFKDFV KVYGPDKFTN VTNGITPRRW
LHQANPRLSE LIASKLGNYE FLKDLTLLNK LEPYVDDKDF KKEWAEIKYA NKVRLAQHIQ
KTKGYSVNPK ALFDIQVKRI HEYKRQQLNI FGVIHRYMAI KAMSPEERKK LVPRVSVFGG
KAAPGYWMAK TIIHLINKVG DVVNKDPDVG DLLKVVFLED YNVSKAEIII PASDISEHIS
TAGTEASGTS NMKFVLNGGL IIGTLDGANI EITREIGEQN IFLFGNLSED VEDLRHHHFY
GDYQINSELL KVFDFIKKGT FGDESAFGAL ISGIVEHGDY YLVSDDFNSY CQTQDLIDEA
YKDQDSWVSK SIISVARMGF FTSDRCINEY ADSIWNIEPL QVKEENEVRS RTGLET
//
