ID X7EHI7_9RHOB Unreviewed; 798 AA.
AC X7EHI7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=OCH239_21535 {ECO:0000313|EMBL:ETX14593.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX14593.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX14593.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX14593.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX14593.1}.
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DR EMBL; JALZ01000009; ETX14593.1; -; Genomic_DNA.
DR RefSeq; WP_037261954.1; NZ_JALZ01000009.1.
DR AlphaFoldDB; X7EHI7; -.
DR STRING; 1449350.OCH239_21535; -.
DR PATRIC; fig|1449350.3.peg.2097; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000022447; 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:UP000022447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 647
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 798 AA; 89716 MW; B2FFD31AC879E12E CRC64;
MNIATLRTVS SDNLRDAILS HLAYSFGKTP EAAHLEDWRM ALSYAVRDRM VEAWFDATRR
TYDAGAKRVY YLSMEFLIGR LLEDGIVNLR LVDQARAALT ELGLDYHTVL ENEPDAALGN
GGLGRLAACF LESLSTLGVP AMGYGIRYEH GLFRQSFADG RQMEAPETWL LQRHAWEFER
PETRYTIGFG GEVRDEAGRM VWTPDEQVCA EAFDTPIAGW KGRWVNTLRL WSAQSVRPFD
LDSFNRGDFE GAAQPEALAR TISRVLYPDD TTEQGKKLRL KQEFFFTAAA LRDILRRFDS
EYNDVALLPS KVAIQLNDTH PAIAGPELVR LLHDERGLPF EEAQKIAQGC LNYTNHTLLP
EALESWNEGI FGQLLPRHIQ IVDRIDDAHA KANPSRGFSM RANHQVRMGE LSFVMANRVN
GVSALHTGLM KETVFKELHR LHPERIVNET NGVTPRRWLL SCNPRLSGLV SETIGSGWID
DLESLSDLEP HVDDAGWRDL FAAAKRSNKS ELAAWMSDTH GLRVDPAAMF DVQIKRMHEY
KRQHLNILEA IAHWQEIKDA PNAEWTPRVK IFAGKAAPGY VFAKDIIRLI NDVSSVLNAD
AETCDKLQVI FLPNYNVTLA ERLIPAADLS EQISTAGKEA SGTGNMKFAM NGAPTIGTLD
GANVEIRERV GAENFFLFGM TAEEVVARRE VEGHAAKAIE ADPRLARALE AIRSGMFSPD
EPDRYRHIVE NLSGHDYFLV SSDFTDYWRA QREVDRAYAD AASWTRMAAL NTARSGWFSS
DRTIRGYMAD IWDAKGLI
//
