ID A0A1X6Z181_9RHOB Unreviewed; 797 AA.
AC A0A1X6Z181;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=malP {ECO:0000313|EMBL:SLN37765.1};
GN ORFNames=ROJ8625_01734 {ECO:0000313|EMBL:SLN37765.1};
OS Roseivivax jejudonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1529041 {ECO:0000313|EMBL:SLN37765.1, ECO:0000313|Proteomes:UP000193570};
RN [1] {ECO:0000313|EMBL:SLN37765.1, ECO:0000313|Proteomes:UP000193570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8625 {ECO:0000313|EMBL:SLN37765.1,
RC ECO:0000313|Proteomes:UP000193570};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 ---------------------------------------------------------------------------
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; FWFK01000003; SLN37765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6Z181; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000193570; 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:UP000193570};
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 797 AA; 89390 MW; 005696E377CF34CD CRC64;
MNIATLPAVS TDTLRDAILS HLAYSFGKTP EAAQIEDWRM ALSFAIRDRM VARWFEATRR
TYEAEAKRVY YLSMEFLIGR LLEDGIVNLR LQEQARAALY DLGLDYDAVL ADEPDAALGN
GGLGRLAACF LESLSTLSCP AMGYGIRYEH GLFRQSFHDG RQVEAPETWL LQRHAWEFER
PEARYRIGFG GQVRESGGRA VWTPEEEVDA EAFDTPIAGW QGHWVNTLRL WSAKAVHPFD
LTSFNRGDFA AAAAPEALAR TISRVLYPDD TTEQGKELRL KQEFFFTAAA LRDILRRFDS
EYDDLGRLPE KVAIQLNDTH PAIAGPELVR ILHDERGIDF DTAMTLAQGT LNYTNHTLLP
EALESWHEGV FGKLLPRHLQ IVDRIDDAHA RAHPSRGFSM RADHQVRMGE LSFVMANRVN
GVSALHTGLM KETVFAELNA LHPEKIVNQT NGVTPRRWLL SCNPGLSELI TDTIGDGWVA
DLERLREIEP EVEDAGWRDR FAAAKRANKA TLSDWLGETQ GLQVDPEAMF DIQIKRMHEY
KRQHLNILEA IAHWQEIKDA PDAGWVPRIK IFAGKAAPGY AFAKDIIRLI NDVSRVVNAD
QATREALQVA FLPNYNVTLA ERLIPAADLS EQISTAGKEA SGTGNMKFAL NGAPTIGTLD
GANVEIREHV GAENFFLFGM TAPEVTARRE VEAHARQAIE ADPRLARALE AVGSGVFSPD
EPDRYAHIVE NLSGHDYFLV ASDFTDYWRA QREVDSAYAD RDRWTRMAAL NTARSGWFSS
DRTIRGYMDD IWGAKSL
//
