ID V6LZY3_9EUKA Unreviewed; 873 AA.
AC V6LZY3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SS50377_10547 {ECO:0000313|EMBL:EST49321.1}, SS50377_26853
GN {ECO:0000313|EMBL:KAH0570573.1};
OS Spironucleus salmonicida.
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Hexamitinae;
OC Spironucleus.
OX NCBI_TaxID=348837 {ECO:0000313|EMBL:EST49321.1};
RN [1] {ECO:0000313|EMBL:KAH0570573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0570573.1};
RX PubMed=24516394;
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 10:E1004053-E1004053(2014).
RN [2] {ECO:0000313|EMBL:EST49321.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 0:0-0(2014).
RN [3] {ECO:0000313|EMBL:KAH0570573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0570573.1};
RA Xu F., Kurt Z., Jimenez-Gonzalez A., Astvaldsson A., Andersson J.O.,
RA Svard S.G.;
RT "New Spironucleus salmonicida genome in near-complete chromosomes.";
RL Submitted (DEC-2020) 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; KI545953; EST49321.1; -; Genomic_DNA.
DR EMBL; AUWU02000007; KAH0570573.1; -; Genomic_DNA.
DR AlphaFoldDB; V6LZY3; -.
DR EnsemblProtists; EST49321; EST49321; SS50377_10547.
DR VEuPathDB; GiardiaDB:SS50377_26853; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000018208; 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:UP000018208};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 717
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 873 AA; 98786 MW; 6D5F4BCD924E2E6A CRC64;
MFAKELATKR TSAPVATNGK SVDYTVGSQI GSMQFHSLLS TGVDQQTPQT VSNNIVNYIK
YQLCRDSSNI DVFGMFQATS MALRNKLIDN WQATYRAQIQ NKARTINYLS LEFLMGRALT
NSLYNLEVGK TYHEALRDLG FKLEDLQAEE MDAGLGNGGL GRLAACFIDS LACMDIPAWG
YGLRYNYGMF RQTIKDGYQQ EEPDYWLKHG TPLPLVERLD REFIVRFGGW TEMVENKNKK
LEFKWRDAQL IKAVAYDCLC PGHHTTNVAN IRLWSARPYT EFELGAHCSG DFYNSVREKA
DTENITFVLY PNDSTENGKK LRLKQEYFFV SASIQDMIAR AAEMQIDLSD FHQHFSVQLN
DTHPALGIPE LMHQLIDHHD FSWDQAWSVV TKTFCYTNHT VLPEALEKWP VSICKELLPR
HTEIMFEINR RFIIECNAKN CSGDAVRAMS LVEEGHAQSL RMANLAIVGS RKVNGVAALH
SDIIVNSIFI DFNKMFPGKF TNVTNGVTPR RWIAQANPLL SHFITKNLKK AGFIQSEHDW
VANMDVLKNL TSLQKDPQAL QELLSIKQAN KQRLASYIER HVSNCGGKIP ETMIFDTQVK
RIHEYKRQQM NIIQAISFYL KLKQMTPAQR KEKFGAGVCK IFAGKAASAY EMAKCLIKLI
NAVGDVVNND PDTKDYLRVI FIPNYNVSSA EIIFPATDLS EQISTAGMEA SGTGNMKACM
NGGIIVGTLD GANVEIQEHV GEESIFIFGA LADQVDFIRS EFQQGRQVEL CSDFKEALEA
IRTGMFGNTE YFSMVVNRLQ NGNDFYLTAV DFEAYNEIYL EDILPAYKDK GTWAVMMLNN
VARMGFFSSD RSIQTYCDNI WNIKPMQIAA MGK
//
