ID A0A318KPJ7_9FIRM Unreviewed; 753 AA.
AC A0A318KPJ7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=DES51_105163 {ECO:0000313|EMBL:PXX79689.1};
OS Dielma fastidiosa.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dielma.
OX NCBI_TaxID=1034346 {ECO:0000313|EMBL:PXX79689.1, ECO:0000313|Proteomes:UP000247612};
RN [1] {ECO:0000313|EMBL:PXX79689.1, ECO:0000313|Proteomes:UP000247612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC118 {ECO:0000313|EMBL:PXX79689.1,
RC ECO:0000313|Proteomes:UP000247612};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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 -!- 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:PXX79689.1}.
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; QJKH01000005; PXX79689.1; -; Genomic_DNA.
DR RefSeq; WP_022937066.1; NZ_QJKH01000005.1.
DR AlphaFoldDB; A0A318KPJ7; -.
DR STRING; 1034346.GCA_000313565_00755; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000247612; 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 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:UP000247612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 604
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 753 AA; 86017 MW; 6EFD16800DCA5481 CRC64;
MTLEKQLNEL FEKASTSFEE ASNEQYYYAL LSVLKQRLAD TSIIQGKKKL YYISAEFLIG
KLLSNNLINL NLYDEAKTLL ESHGRSLAEI EEIEPEPSLG NGGLGRLAAC FLDSIATLGL
AGDGIGLCYH FGLFKQQFVN HQQKEEINPW IEKDSWLRER DVTFTVPFGG FSLDSKLYDI
DVVGYENGKN QLHLFDIQKV DESIVHDGID FDKGNLLRNL TLFLYPDDSD EAGRMLRIYQ
QYFMVSNGAQ YILMNAKKEG LDLHKLNEFV TIQINDTHPT LVIPELIRLL MLEGIDLDEA
IAITSKTCAY TNHTILAEAL ETWPRRFLEE AVPHLMPIIE ALDQRVKAHY DNPSVAIIDD
ADLVHMAHID IHYGYSVNGV AAIHTEILKN TELKPFYQIY PEKFNNKTNG ITFRRWLYAC
NPELDQWLNQ WIGSDYKKDA AKLEQLLAFK DNKQCLDELA AIKQLKKKQL AQMLKATQNI
DLDPESVFCI QIKRLHEYKR QQMNALYIIH KYFEIKAGKL PARPITMIFG AKAAPAYIIA
KDIIHLILCL SEFIAKDPDV APYLKVVMVE NYNVTLAEKL IPACDISEQI SLASKEASGT
GNMKFMLNGA VTLGTADGAN VEIAELVGEQ NIYTFGESSE QVIAHYQNHD YISKKIYKQE
PHIKQCVDFI VSKELCSIGS RKILRQLQQE LINKDWFMTL LDLNAYIAEK DRCLADYEKH
EEWTKKMLVN IAKAGFFSSD RTIAQYNQDI WKL
//
