ID C0NRD2_AJECG Unreviewed; 882 AA.
AC C0NRD2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HCBG_05562 {ECO:0000313|EMBL:EEH06246.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH06246.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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; GG663369; EEH06246.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NRD2; -.
DR STRING; 447093.C0NRD2; -.
DR VEuPathDB; FungiDB:I7I50_03659; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; C0NRD2; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000001631; 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:UP000001631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 729
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 882 AA; 99725 MW; 7D5FEE876B212FDB CRC64;
MTSPTRERRP SIGAPISDLQ GPVGPGFSRP KHKRTFTGLL PQDIKKVEAS IPEPQREAYK
EVVRHVETTL ARSLFNCDEL AAYSGTALAF RDRLIIEWNK TQQRQTFADQ KRVYYLSLEF
LMGRALDNAM LNVGLKQVAR GMIPVPGPKV TTNATIVDGL KDLGFRIEDV ISQEHDAALG
NGGLGRLAAC FLDSLASLNY PAWGYGLRYR YGIFKQEIIN GYQIEVPDYW LDFNPWEFPR
HDVTVDIQFY GSVRKYQDEN GKTNYSWEDG EIVQAVAYDV PIPGYATPTT NNLRLWSSKA
ASGEFDFQKF NAGEYESAVT DQQRAETISA VLYPNDSLDR GKELRLKQQY FWCAASLYDI
VRRFKKTKRA WSEFPDQVAI QLNDTHPTLA IVELQRILID QEGLEWNAAW TIVSSTFGYT
NHTVLPEALE KWSVPLIQTL LPRHLQIIYD INLLFLQMVE KMFPKDRDLL RNVSIIEESQ
PKMVRMAHLA IIGSHKVNGV AELHSDLIKT TIFKDFVEIY GPDKFTNVTN GITPRRWLHQ
ANPRLSNLIA SKLGDGFLKD LTLLDKLEAY IDDESFRREW ADIKHANKVR LANHIFSTTG
IRVDPKALFD IQVKRIHEYK RQQLNIFGVI HRYLKIKAMS ANERAKLVPR VSIFGGKAAP
GYWMAKSIIH LINQVGSVVN SDPDVGDLLK VIFVEDYNVS KAEMICPASD ISEHISTAGT
EASGTSNMKF VLNGGLIIGT CDGANIEITR EIGEQNIFLF GTLAEDVEDL RHAHIYEKDN
VTLGNHLTAV FDTIKSGTFG DASSFSALIS AITEHGDYYL VSDDFHSYIT TQDMVDEAYR
DQDGWLEKCI LSVSRMGFFS SDRVIAEYAD SIWNIEPVDA PE
//
