ID B3E052_METI4 Unreviewed; 819 AA.
AC B3E052;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:ACD82713.1};
GN OrderedLocusNames=Minf_0658 {ECO:0000313|EMBL:ACD82713.1};
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=481448 {ECO:0000313|EMBL:ACD82713.1, ECO:0000313|Proteomes:UP000009149};
RN [1] {ECO:0000313|EMBL:ACD82713.1, ECO:0000313|Proteomes:UP000009149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149};
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000975; ACD82713.1; -; Genomic_DNA.
DR RefSeq; WP_012462995.1; NC_010794.1.
DR AlphaFoldDB; B3E052; -.
DR STRING; 481448.Minf_0658; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; min:Minf_0658; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000009149; Chromosome.
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:SF25; MALTODEXTRIN 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 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; 93675 MW; 32FEC0D41E7E404D CRC64;
MTSRSGYWRF TTDTTPEGIR EAILTHLRLS LARSPDTATP FDWWVSTAMM CQDHIVDQFL
ATYRAQKADK VKRLYFFSLE YFLGRLLHQN LINLGILEQT KKALTGLGLD IDQIFEEEPQ
IGLGNGGLGR LAACFLDSLS TLRYPAFGYG LHYEFGLFHQ DIINGYQVER PDDWTRFGVP
WEIIRPRFSQ VIRLYGSIDW NKQKPVWVGG KEILGVPYDY LIPGYRSPVV NVLRLWRSKS
TVEFDLEAFN RGGYFEAVAE KSFCESISKV LYPNDKTEIG RELRLIQQYF FVSCSLHDIV
RRFLKEHSHF DDFPSKVVIH LNDTHPAIAI AELMRIFLDE HNLPWSKSWE LVSQCFAYTN
HTLMPEALEK WSVPLFERVL PRHLQIIYEI NKQLLDSVPT TIPERDKLIR QISLIEETQP
KLVRMANLAI CGSYSINGVS ALHSELLKKE LFHPFYTLHP KKFHNVTNGI TPRLWLLASN
PRLSNLITEA IGEDWPSDLE KLEGLKSFMA DPAFQEKYEL VKQSNKAELS SLLKQRYNFV
IDPDALFDVQ IKRIHEYKRQ HLNLLHILSL YRRLLDNPNL DIHPRVFLVA GKAAPGYDLA
KCIIKAINAV GNKINNDPRV NKKIRLYFVP NYGIWLASKI IPAADVSEQI STAGKEASGT
GNMKLALNGA LTVGTMDGAN IEILEAVGEQ NIFIFGLKAE EIRQLSVSGY SSRKIYETDP
EIKYLLDWLG SGEFTPGESP AVLQPLVHSL IGGGDPFFVL ADFHAYKEIQ SKVDQQYKDR
KMWISKAILN TASLGWFSSD RSIQQYASMI WHLAPCLPK
//
