ID K5W064_PHACS Unreviewed; 866 AA.
AC K5W064;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PHACADRAFT_260910 {ECO:0000313|EMBL:EKM52475.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM52475.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM52475.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM52475.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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; JH930475; EKM52475.1; -; Genomic_DNA.
DR RefSeq; XP_007398819.1; XM_007398757.1.
DR AlphaFoldDB; K5W064; -.
DR STRING; 650164.K5W064; -.
DR GeneID; 18917839; -.
DR KEGG; pco:PHACADRAFT_260910; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; K5W064; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000008370; 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:UP000008370};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 866 AA; 98434 MW; 0BBA3404DEE85D77 CRC64;
MTSTIDPKAI GKPAPKRKHA RTLTGYLPEV DESGQEKWPR GEEKVWKEGT RGPDRDVSTI
TKSFVNHVHT SLARQAYNLD DLGAYQAAAL SVRDNLIINW NATQLNFTRK SPKRAYYLSL
EFLMGRTFDN ALLNLGLKKE YSEGVNQLGF NLEDLLEKER DAGLGNGGLG RLAACYLDSS
ASQELPVWGY GLRYQFGIFQ QLIAPDGSQL EAPDPWLQHD NPWELPRPDV SYEIRFYGHS
ERLDGMKAVW SGGQEVLAVA YDTMIPGYDT KNTNNLRLWE SKPKRGFDLN SFNAGDYERA
IESSNSAAAI TSVLYPNDHT TFGKELRLKQ QYFWTAASLA DILRRFKNID KPITEFPEHV
AIQLNDTHPT LAIPELMRIL LDEEDVPWDV AWNIITNTFF FTNHTVLPEA LEKWPIPLME
NLLPRHLQII YDINLLFLQA VEKKFPGDRD KLARMSLIEE GFPKNVRMAN LAVLGSRKVN
GVAELHSELL QATILKDFVE FYGQSKFFNV TNGITPRRWL DQCNPGLSNL IHETLRIPKA
DFLKDLYKLE GILEYIDNPS FQKKWVAVKQ SNKERLANYV ENTLGYKVNT QAMFDVQIKR
LHEYKRQTMN IFGVIYRYLT IKAMTPEERK KVNPKVVFFA GKAAPGYYIA KLTIRLIVNV
ARVINADPDT KDLLTLFFLS DYSVSLAEIL IPASDISQHI STAGTEASGT SNMKFCLNGG
LLLGTVDGAN IEIAEEVGES NVFFFGHLTP AVEDLRYQHM YHPQPIEQKC PNLARVLNEI
SSGRFGDGGV YEPLLNTIRN VDYYLLTEDF DSYIQALANV DNAYQNRVEW IKKSITTTAK
MGKFSSDRAI NDYAQECWNI ESLHLK
//
