ID S7TVN6_DESML Unreviewed; 819 AA.
AC S7TVN6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=dsmv_2313 {ECO:0000313|EMBL:EPR40810.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR40810.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR40810.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR40810.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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 -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
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|ARBA:ARBA00001275,
CC 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:EPR40810.1}.
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DR EMBL; ATHJ01000080; EPR40810.1; -; Genomic_DNA.
DR RefSeq; WP_020876744.1; NZ_FUWN01000021.1.
DR AlphaFoldDB; S7TVN6; -.
DR STRING; 897.B2D07_00805; -.
DR PATRIC; fig|1121405.3.peg.1883; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000014977; 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:UP000014977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 664
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 819 AA; 94588 MW; 86428D8075F345FE CRC64;
MMKPSLLGNS KAALKKSMDY HLRCSLCKEP VSKEGRDLFL ATAFSLRDRM AEKILQTERR
YRETKTKRVY YLSLEFLIGR LMGNTLHNLG MFDSYKGLLT DAGFDIEEVR EQETDPGLGN
GGLGRLAACF LDSMATLDIA GFGYGIHYEY GLFKQEIDNG YQREKPDNWL AELNPWEIKR
TDEKCIIPIH GRIEHFQDRA GEYNPMWLDW KVIMGIPFDI PVVGYGGKTV NWLRLYGAGS
SADFDIQIFN EGDYFRAVEQ KVSSETITKM LYPLDTLKSG RELRLVQEYF LVACALRDII
RRYLRDHENF DRFPERVAIQ MNDTHPSLAV AELMRLFVDE YALPWDHAWE ITRETLAYTN
HTVLAEALEK WPVGLLEKVI PRHLQIIYEI NRRFLDKVAP LYPGDIDLIR RISLIEEGET
KQVRMAHLAL VGSHSVNGVS ALHTEILKNE NFSDFYALRP EQFVNITNGI TQRRWLLEAN
PRLAGLISDT IGDAWITDLR QLRRLEPMAD QKAFKDAFHD IKRANKEILA GIISDTVWLS
VDPDSLFDVH VKRIHEYKRQ LLKIMQIVHE YLQIIRDEKK PVIAKTHIFA GKAAPGYWIA
KQMIKLIHNV GQVINQDKRI GDALKVVFLP DYRVSLAEKI IPATDLSEQI SMAGREASGT
GNMKFMLNGA LTVGTLDGAN VEMLEEVGEE NIFIFGLKAK EIAEMVKQKR YRPLDYYHRF
PEIRRVLDAF RDDTFCAAER GLFQWIYHRV MNNEDPYFHL PDFMQYIEAH DKIEAEFQAP
ATWTQKAILN VARCGKFSSD RAIADYNRLI WNKNGLKEK
//
