ID A0A372QKT4_9GLOM Unreviewed; 869 AA.
AC A0A372QKT4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=C1646_819091 {ECO:0000313|EMBL:RGB28496.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB28496.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB28496.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB28496.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) 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:RGB28496.1}.
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DR EMBL; QKKE01000462; RGB28496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372QKT4; -.
DR STRING; 1803374.A0A372QKT4; -.
DR InParanoid; A0A372QKT4; -.
DR Proteomes; UP000263633; 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:UP000263633};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..22
FT /note="Disordered"
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 869 AA; 99212 MW; EE0506F34E7DD4E1 CRC64;
MSNANVADAD GTAKPGHHKR TNTGFVTKEL KKAIAKLPKE TLALWEKYGA DESDDKESFQ
KSFIRHVTTT LARSIYNIDN FSAYQATAHS VRDRLIKRWN ETQQAHTEIN SKRVYYLSLE
FLLGRSLDNA LLNLGLKDNY GEGIKELGFT MEDVLDQEVD AALGNGGLGR LAACYMDSLA
TMEYPAWGYG LRYTYGIFQQ RLKDGYQIEF PDYWLNFDNP WELPRLDVVV DVQFCGSVNR
YTDENGHKKY VWEGGDTLQA IAYDVPIPGY GTKNCINIRL WSSKPKRQFD LTRFNEGQYE
QAVYEQMQAE NITAVLYPND NHMVGKELRL KQQYFWVAAS LFDIVRRFKK TEKPWGEFPL
QVAIQLNDTH PTLAIVELQR ILVDLEGIGW DEAWGIVTQT FAFTNHTILP EAMERWPVPM
IQYLLPRHMQ IIFDINLFFL QKVEKAIPNN RDLLAKLSII EESTPQFVRM AHLAIVGSHR
VNGVAALHSE LIKKTIFKDF IQFYGESKFE NKTNGITPRR WLHQANPKLS ELITETLGSK
NWLKNLDLLK GLKSYVDNKD FRKRWVAAKH SNKVRLADYI KKATGIIVNS NALFDVQVKR
IHEYKRQFMN ILGVIHRYNT LKKMTSEERA CVVHRVIIFG GKAAPGYYIA KLVIKLINSV
AEVVNNDTSI EDSLKVVFIP DYNVSVAEII IPASDISQHI STAGTEASGT SNMKFVLNGG
LILGTVDGAN IEICEEIGDD NIFMFGNLAH QVEDLRHAHR YRNVPVDPSL QAVINDIESG
HFGDSRIFAP LINTLTHGKD YYLISDDFQS YLDAQKLVDE SYKDQEGWIT KSIMCSAHMG
KFSSDRAIYE YAEKIWDVKP VPVITKKHI
//
