ID W4QGL2_9BACI Unreviewed; 810 AA.
AC W4QGL2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=JCM9152_1857 {ECO:0000313|EMBL:GAE30449.1};
OS Halalkalibacter hemicellulosilyticusJCM 9152.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE30449.1, ECO:0000313|Proteomes:UP000018895};
RN [1] {ECO:0000313|EMBL:GAE30449.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE30449.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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:GAE30449.1}.
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; BAUU01000011; GAE30449.1; -; Genomic_DNA.
DR RefSeq; WP_052015767.1; NZ_BAZO01000011.1.
DR AlphaFoldDB; W4QGL2; -.
DR STRING; 1236971.JCM9152_1857; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000018895; 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:UP000018895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 656
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 810 AA; 94113 MW; 9346F34C31E0293D CRC64;
MTYQNVDEFI SLITEKIRTL FGKELHNANE KDVYYALASI ANDEMHPHWC KTNEHYEQKK
VKKVYYLSME FLIGRLLESN LLNCGLLDVT NIALKRLGFK RDAVFIHEHD AGLGNGGLGR
LAACFLDSLA SLQYPGHGCG IRYRYGLFEQ RIIHGHQIEL PDYWLKEDYP WETRKSEESI
SVHFGGSVHM HRRANGSLEF RYENTDEVIA VPYDIPISGY HNHTVNTLRL WSAESQDRND
VANHSDHYYH ALDHTHSIDQ ISGFLYPDDS SYEGKKLRLK QQYFLVSASI QNILRHYLNE
GRGPLTQLSE HIVIQINDTH PSLAIPELMR LLMDHYDLNW DQAWETTHKT IAYTNHTTLS
EALEKWPKDM VQNLLPRIYM IIDEINERFC QGLWFDCPEM REHIPALAII ADDQIHMARL
AIVGSFSVNG VARLHTEILK KKEMKLFYQL FPKRFNNKTN GITHRRWLLQ VNPHLANVIT
DVIGPAWIKR PNQLISLLRY SNDPAFLEQI EQVKLQNKRT LAQFIYDKMG IKVNEKSIFD
VQIKRLHEYK RQLLNIFHVI YLYNELKDNP KLDLTPRTFI FGAKAAPSYH LAKEVIKLIH
TVASLVNHDY DVADRIKVIF LENYNVSLAE KIIPAADISE QISTASKEAS GTGNMKMMMN
GALTVGTMDG ANIEIRDLVG DQHIFMFGLT SDEVLHYYEH GGYSARDIYN TDDRISRILD
QLNSGVFGEQ EMEFKDLYYN ILYHNDPYFV LKDFDPYIET HELVEQAYRD RSIWLNKSIT
NIAYSGKFSS DRTIQQYASE IWQLTKNPIK
//
